UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
D6W2S1
|
MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRNMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
|
Increases frequency of mitochondrial genome loss. Present with 2870 molecules/cell in log phase SD medium. Belongs to the AIM41 family.
|
C5DXN2
|
MFRRAAFIKPRLTGFIRFNSTESYNAALGGLKKDLKQAMLAKDELKKTTIRGLLSTIKNKEIDNKDKTLDEFTLFDLYSKLISQRKDSITEFLANKREDLVAKEQHEMGIIEQYRSALPVASKEEIDSKVLQLLKNLKEKEPTLQMKQAFGKIDWKTVNSEWKASPNAVKASIVQQFKNVF
|
Belongs to the AIM41 family.
|
Q75BX3
|
MPIGKLRRSKAISFRGPASPSLKFKSFETLQGKPLGEMGQNGHKQEEDMAAQRPHFPAEAGAEQEMKCHVAETPAQNSQVPSTTMENGFYSFANISDNTTNKNTNRYSYLSDNTACQLLAPATGTDYYKSLTPTMKPITERQNHAGTTMSLDTIPTAENISFQITLPTVPPSVISSRSSLINRQRSLSMRYSSPSSMSSLGSTPTKLTTLKRSNAIRCKGGLLQFFSQYAVKTGKKLVKWKIALRKRLFKFQRRSTKNKKNSSPTTSHLKRVNGYVSNVRRSFSTQSRLALVPEIVRRTPSRRHLTANTGMKDATPASPSRTSIRRTPSSIKRAASTLSSNYVYRDGSDTSSQAPELKSTGSSLAPAPSQMVRSTALTSLNSIVRQPSIVVNNKVIPLSRFPGEKMQLPIREEDEEEEEPSTKTDDYVIDTSKRMSTIGEIQASRISSSSGSISSHSSSIQSSHFDDASNSCPLNDSIESDSDIECTRTAWNHFLRTVIAERIRMRLQLAKLQELALLKDDSLDILYAVLRKTLDEPADKSSSTYDPDIMPENNSETGLGNGFRSSDQLSRLKEGSRKRNTSSSTMLALPEALATVRRSITMPVGLNYI
|
Belongs to the AIM44 family.
|
Q6FK06
|
MSGMIIRTPTRTKTKSFNGKQMDFTFPSPVRGSVDEHSLDNHRIVNETLSLKPQEDIEVSSQMLSDYTSSASNANTYSGNSSNGYYSFANISDNTTASPKLHNHNNMVSPILENTESSFQLQTVESLDPQRQRIRSTYEYGHMGSNQNLRQTREKSKTAESISTTIAQQTIPTADNISFDFSDISGYEDAVSNKSENKNHKPQNSVVKNQLRATSRAAISTNDSPSLSNVYMSSLINSSLESTRKTSTASSSVRSSRSSLKRSNAVRCKGGLLQYFTKLGIKIRKNCNKLRLVMRRKLFRFKKNSKSFSRSNSIRSGLEISKLPKVRHEKKLRQESSSIAPHTLHQKRTHGFNNKLHKSMSLKSLQPALVSETVPEINNNLHDILESKEKTADVPAATKTMKTTPSLRRTPSSIRRAASILTSNVATPKASANNRNSMIEYDTVENSRISSRNSSIKSKGRLVRSSGSVGLSSIARQPSIVVKNKVIPLSMSRFSIKEEIKEEEEESEESTSDYYVETEPVEAAPRTLAGPKSYAPENFRYGANVDDIKTLYKHYLSTVISRRIKMRLEMAQGEHSATNEPALTHQSTASLKDPIASVLTEYDSEGSEGTNLFDDEDDSSASEEDDEVVLPPLKGHNSTMSFVVQSPFTRQNSMASSSALLYLPVKRSLTLPIGMKIT
|
Belongs to the AIM44 family.
|
Q6CRV9
|
MIRTPTRTKTKSYNGSQSEFRFPDVEVLAHLKLPEHGLNNHHLLNEQLNKKPEDDIHSQHLSDYTTTNSNSGNSSNGYYSFANISDNTTNPDKLSAVKNTACAIGNNRYSYISSSGSSVHYPGTLAPDRTPRICPTNSPEFGRPLDGNFDMQCIPEAYSTVTSDFTLPTADNISFQFTLSSGNSTAMLKKRSTPSTKTRNATNLSEKRKSSVKRSTSTVSRRSNIKRSNAIRCKGGLLHYFTKLGKRVRLNLKKFHLALKRKLFTYKQRHFAKSDKRTTSHLLRSNGYFANIKRSQSMRSMASYSDTSSPTVPSGLDIKNTPIVKHSSNINHRSLRRTPSSIKRAASILTSSNSLIFSRSNSSVGRTDSTRLVRSQPSLNLNLAVRQPSIVVKNKVIPLSQFDHDDYCIREEDEDEEDEDEYIIDTQKMQPLKSEMGSITSSLHDGDSVFEDAMSSSASMESLSESVKILNANKAWDSYLRAVISQRILMRLQVAKFQASQDHHTYKELLDAIVTDYESDAIFSNNDAQTENDSMSECDSPHEFDTLTDSSRSTPAVVPQSLRESFSSLANFQTSVKAGVRRNLTLPVGISI
|
Belongs to the AIM44 family.
|
C5DF10
|
MIRTPTRTKTLSFAGPQVDFHFPSPESAPNGSLDNYHMSNHHLLNDAVARSPSQNSSGTSNGVDSAHYSFANISDNTTGVRNAGNGKRSSQAPSWSSGSGSCRRYPVTLAPITNASALARPGDSGAADVRKNDTAAFLRRKRSPEDCALHSISTSAYTIPTADNISFQITFGSSDKSHSLGSLRRSPSFGRRLPSRRTAGSSNNAPVSASLPARAASVKSTQSTLKRSQAVRCKGGLLQFFMQVGVRAKNRIRRWRLAVRKKLFTYKAKRLAKKNKKQTTSHLKRGNGYVSNIQRSISSASLRNSQRKNSDSASKETPATVARSGTLPNPLETPPKTTRKSLRRSPSSIKRAASILTRANSSGTITQGTAEKNNAGENIPRTKLVRSGPSLSLSSIARQPSIVVNNKVIPLTSLNEDTKDFTIEEEDEDEYVIDTDCMKKSVRGYSQSSSGSSNSGKSSDETYHDSLENPTPDESLLPDEKVSRALDAWNHYLRAVVAQRVLMRLQIRRFQESGGDPECQELIDAIISDYEENSSSHCDSDLRSDSTSLTSVSDCEGRVSSSVASDVSVGITGSIFSARPFQQTMKNSVKRSLTLPVGFRV
|
Belongs to the AIM44 family.
|
A7TKN1
|
MEKQHLQSHILREPERKKTKSFHGPQSDFKFPSTESLLKNEMDEYHLDNHHLLNDSIPRVNVTTANMHSGSAIDSDTNSQILSDYTSFSNPNSSNGYYSFANISDNTTSRNGPNSYQSYGLFSNDELQETEYRHTLDPEKISSNDTNHNNGYIHSTAGNDTQENNTETKVLGRGISNSISTANHSIPTIENISYRIESATSSLKSSKSVIQTKRLERPSINRVPTITRIGSIASYSSSSLNVGTSSLSLNRKRSNVSSLKRSGAIRCKGGLLYYFTTMGAKFRKQFHKMRMAIKRKLFGYQRSNSIHRSASIKSELNKKAKKSTSIKNRPVTSHLKRTQGYITNLQRSMSYKSLEPVLVPRFTDIMPNATSPMRKISNSQKAANYKKTASLRRTPSSIRRAASVFTSHNNSANATTENLANIVHATEEGPKSPELLHQQNNTIKGKISRSQGHSSLNTIIREPSIVVRNKVIPLSMKHYAIKEEDEEKLSSDEIKEENEENIDEYVIKTEQLEKQISNKHNITNLEPAEEIDNDDSSFDDVDFVSMDNDNEHLLASEIIKKNESEQLQKMLKQYLTHVIAQRIKLRLQLAKFQETGKIERESNSSHYDDKHLSTLVSLISEQESRNRRSQIFEKSRTYLSSETSSEDSIFNHATSDLALPFQYKNTSNDNVYSSDRLSLSIHTDFGESQGKHSTSVLSFHAQDVKRSLTLPISMKV
|
Belongs to the AIM44 family.
|
B3LKR9
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQILSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSSVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVNANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNNKSNVVYMNKSAETNSTIYEDLADSLLTEYEADGSSSQIFDGVSVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNSAYSNSIISLPTGVVKRSLTLPVGMKI
|
Belongs to the AIM44 family.
|
C7GJB0
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQILSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSSVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRLDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVNANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNNKSNVVYMNKSAETNSTIYEDLADSLLTEYEADGSSSQIFDGVSVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNSAYSNSIISLPTGVVKRSLTLPVGMKI
|
Belongs to the AIM44 family.
|
B5VT12
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQILSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSSVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVNANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNNKSNVVYMNKSAETNSTIYEDLADTLLTEYEADGSSSQIFDGVSVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDEEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNSAYSNSIISLPTGVVKRSLTLPVGMKI
|
Belongs to the AIM44 family.
|
A6ZW95
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQILSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSSVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVNANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNNKSNVVYMNKSAETNSTIYEDLADSLLTEYEADGSSSQIFDGVSVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNSAYSNSIISLPTGVVKRSLTLPVGMKI
|
Belongs to the AIM44 family.
|
C8ZIM0
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQILSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSSVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVNANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNNKSNVVYMNKSAETNSTIYEDLADSLLTEYEADGSSSQIFDGVSVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNSAYSNSIISLPTGVVKRSLTLPVGMKI
|
Belongs to the AIM44 family.
|
D6W3L0
|
MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQTLSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSNVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVDANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNYKSNVVYMNKSAETNSTIYEDLVDSLLTEYEADGSSSQIFDGVTVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNPAYSNSIISLPTGVVKRSLTLPVGMKI
|
Expression is controlled by SWI5. Increases frequency of mitochondrial genome loss. Present with 238 molecules/cell in log phase SD medium. Belongs to the AIM44 family.
|
C5DXS6
|
MIIRAPTRTMTKSFNGRQMGFKFPSVENMPQNPLDEYHMNNHHLLNDNIAKSQQAQAHPHPPPHQKPISTDEDALSNINSDYTSGSNTNTNSGNSSNGYYSFANISDNTTPLPNKMYSYPSSPKSNESSEGGKMSELTVPKDEHNQSSQKSTEPMEVIPEDNGFTSMSLNVQSIPTADNFSFDIASSNSLRPGSTTDKPGVATLARTPSSNTSRSSLLSPSVRNPSSSSARIRQSKRRSQLKRSPSIRCKGGLLKYFHLLGSRIKKTLRKIKLALRGKNSKRQASYRRSTSSTAAPKVARKPQVNVTRASSKKELTSHLKRTNGYVSNLKRSMSQRSLRPLLETPEKCATAGSLHTPHPDTSSSDAFVTPPGSRIVRNPTTSLRRTPSSIRRAASVIRTPIPAVPSATVAPSESFVYEDATTASPGSANGSENRSGLVRSTASKSLNSLVRQRSIVVKNKVIPLSMHQYSIKEEDEDKEHDSQFMIRPSSDYSLSPVHSVSSEGNGSNYDSDFEKYYSTGDYTDAYEDAEMGSFISSKRTSSTNTSSTAASSDAVSYTESVVPSVEPTVEPAVESKSIDDGEDIDETTDSVSFNNEIEELRSNINHYFRCVIARRIKLRLQFSHYESSNSLSPSYLDIMESLLKDYDDESTAGKDPAEFNTIDEEDEVAASELWSPRDSKTGSIRVNVQTPYLKRGPTQHSLISLNSRDVRRSLTLPIGMKV
|
Belongs to the AIM44 family.
|
A9MJC7
|
MLAFILRFIKNKSYFALLAGAWVIIAGLTSQHAWSGNGLPQINGNTLAALAKQYPVVVLFRHAERCDRSDNTCLSDSSGITVNGAQNARSLGKDFNADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNVVIFTHNHCLTYIAKNKRGVKFEPDYLDALVMHAANGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
Q57M58
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHVERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B5FNT6
|
MLAFTLRFIKNKRYFAILAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVKGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B5R269
|
MLAFTLRFIKNKRYFAILAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVKGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B5RCC1
|
MLAFTLRFIKNKRYFAILAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVKGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B4TBG3
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B4SYW8
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQNARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
Q5PC78
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSFTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
A9N5B6
|
MLAFTLRFIKNKRYFAILAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVKGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
C0Q072
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYPSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B5BCP9
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSFTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
B4TPH9
|
MLAFTLRFIKNKRYLATLAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLDALVMHAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
Q7CB83
|
MLAFTLRFIKNKRYFAILAGALVIIAGLASQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVNGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTADKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMYAENGKLFLDGEFVPG
|
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
Q8ZNF4
|
MLAFTLRFIKNKRYFAILAGALVIIAGLTSQHAWSGNGLPQINGKALAALAKQHPVVVLFRHAERCDRSDNTCLSDSTGITVKGAQDARALGKAFSADIQNYNLYSSNTVRTIQSATWFSAGRSLTVDKKMMDCGSGIYASINTLLKKSQNKNIVIFTHNHCLTYIAKNKRGVKFDPDYLNALVMHAENGKLFLDGEFVPG
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Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Required for iron(3+) resistance. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Induced by BasR. Belongs to the phosphoglycerate mutase family. Ais subfamily.
|
Q31YK5
|
MSIGGVYELAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADIPDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCLTYIAKNKRDATFKPDYLDGLVMHVEKGKVYLDGEFGNAANLLI
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Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
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Q0T2N1
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MLAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADIPDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCMTYIAKNKRDAIFKPDYLDGLVMHVEKGKVYLDGEFVNH
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Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
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Q7UC65
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MLAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADISDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCLTYIAKNKRDAIFKPDYLDGLVMHVEKGKVYLDGEFVNH
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Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
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Q3YZV4
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MLAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADIPDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCLTYIAKNKRDATFKPDYLDGLVMHVEKGKVYLDGEFVNH
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Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Bacterial outer membrane biogenesis; lipopolysaccharide metabolism. Belongs to the phosphoglycerate mutase family. Ais subfamily.
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Q9Y229
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MWIQQLLGLSSMSIRWPGRPLGSHAWILIAMFQLAVDLPACEALGPGPEFWLLPRSPPRPPRLWSFRSGQPARVPAPVWSPRPPRVERIHGQMQMPRARRAHRPRDQAAALVPKAGLAKPPAAAKSSPSLASSSSSSSSAVAGGAPEQQALLRRGKRHLQGDGLSSFDSRGSRPTTETEFIAWGPTGDEEALESNTFPGVYGPTTVSILQTRKTTVAATTTTTTTATPMTLQTKGFTESLDPRRRIPGGVSTTEPSTSPSNNGEVTQPPRILGEASGLAVHQIITITVSLIMVIAALITTLVLKNCCAQSGNTRRNSHQRKTNQQEESCQNLTDFPSARVPSSLDIFTAYNETLQCSHECVRASVPVYTDETLHSTTGEYKSTFNGNRPSSSDRHLIPVAFVSEKWFEISC
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Plays a role in cell adhesion and cell migration. Forms a complex with CDH1 and CTNNB1; interacts directly with CTNNB1. Interacts with AP1M2. Interacts with isoform 2 of BSG/CD147. Mainly basolateral (PubMed:16707570). Localization is mediated by AP1M2 (PubMed:16707570). Expressed in uterus and pancreas (at protein level). Thr-237 and Ser-239 may be phosphorylated; however as this position is probably extracellular, the in vivo relevance is not proven.
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B2RVK0
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MWIQQLLGLSSMSIRWPGRSLGSHAWILIAMLQLAVDFPSCDSLGPGPEFRLLSRPQRPQRLWSLRSGPPTRLPTPAWSPRAARAERAHGPIQMQTPRARRAHRPRDQVATLGPKGGLTKPPAATRSSPSLASATASSSIVTAGAAEHQGLLRRGRRHTHDTEFNDFDFRGGRPTTETEFIAWGPTGDEDALESNTFPGGFGPTTVSILQTRKTTVATTTTTTAASTATAMTLQTKGVTESLDPWKRTPVGVSTTEPSTSPSSNGKDIQPPRILGETSGLAVHQIITITVSLIMVIAALITTLVLKNCCAPSGHTRRNSHQRKMNQQEESCQNLTDFTPARVPSSVDIFTAYNETLQCSHECVRASVPVYADETLHSTGEYKSTFNGNRTSSADRHLIPVAFVSEKWFEISC
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Plays a role in cell adhesion and cell migration. Forms a complex with CDH1 and CTNNB1; interacts directly with CTNNB1 (By similarity). Interacts with AP1M2 and isoform 2 of BSG/CD147 (By similarity). Mainly basolateral. Localization is mediated by AP1M2.
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G3UWD5
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MVFAPGEKSGKELEEVKLQNTSKQIVQNAILQAMRQVSQESLRREGRPGDSRAWGQLGGCELTKKHEKK
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Protein kinase A (PKA)-binding protein. Binds to type II regulatory subunits of protein kinase A (PKA) and may block the A-kinase anchoring protein (AKAP)-mediated subcellular localization of PKA. Binds cAMP-dependent protein kinase (PKA). Interacts specifically with RII-regulatory subunits of PKA (PRKAR2A and PRKAR2B). Preferentially expressed in the neural tissues. The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
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Q9BW14
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MAIQFRSLFPLALPGMLALLGWWWFFSRKKGHVSSHDEQQVEAGAVQLRADPAIKEPLPVEDVCPKVVSTPPSVTEPPEKELSTVSKLPAEPPALLQTHPPCRRSESSGILPNTTDMRLRPGTRRDDSTKLELALTGGEAKSIPLECPLSSPKGVLFSSKSAEVCKQDSPFSRVPRKVQPGYPVVPAEKRSSGERARETGGAEGTGDAVLGEKVLEEALLSREHVLELENSKGPSLASLEGEEDKGKSSSSQVVGPVQEEEYVAEKLPSRFIESAHTELAKDDAAPAPPVADAKAQDRGVEGELGNEESLDRNEEGLDRNEEGLDRNEESLDRNEEGLDRNEEIKRAAFQIISQVISEATEQVLATTVGKVAGRVCQASQLQGQKEESCVPVHQKTVLGPDTAEPATAEAAVAPPDAGLPLPGLPAEGSPPPKTYVSCLKSLLSSPTKDSKPNISAHHISLASCLALTTPSEELPDRAGILVEDATCVTCMSDSSQSVPLVASPGHCSDSFSTSGLEDSCTETSSSPRDKAITPPLPESTVPFSNGVLKGELSDLGAEDGWTMDAEADHSGGSDRNSMDSVDSCCSLKKTESFQNAQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDDQFSPEADAAMSEMTGNTALLAQVTSYSPTGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYTSL
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Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (PubMed:31522117). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity). Interacts with SLC8A3 (By similarity). Interacts with CFAP91 (PubMed:12223483). Interacts with CLPB (PubMed:31522117). Interacts with NDUFS1 (By similarity). Isoform 1 is detected in thymus, prostate, testis, ovary, colon and small intestine (PubMed:8769136). Isoform 2 is highly expressed in testis and detected at much lower levels in kidney, pancreas, liver, lung and brain (PubMed:7499250). RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
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P97488
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MAIQLRSLFPLALPGMLALLGWWWFFSRKKDRLSSSDKQVETLKVGPAIKDRRLSEEACPGVLSVAPTVTQPPGREEQRCVDKPSTEPLALPRTRQVRRRSESSGNLPSVADTRSQPGPCRDEIAKVELSLMGDKAKSIPLGCPLLPKDASFPYEAVERCKQESALGKTPGRGWPSPYAASGEKARETGGTEGTGDAVLGENVSEEGLLSQECVSEVEKSEFPILAPGGGEGEEVSHGPPQVAELLKKEEYIVGKLPSSFVEPVHSEPVKDEDALEPQVKGSSNTSDRDLAGELDKDETVPENDQIKQAAFQLISQVILEATEEFRATTVGKTVAQVHPTSATQPKGKEESCVPASQETSLGQDTSDPASTRTGATASPSAEALPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLEGASNPRGDDNFVACMANNSQSVLSVSSLGQCSDPVSTSGLEDSCTETISSSGDKAMTPPLPVSTQPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQSVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYASL
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Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A (PubMed:9065479, PubMed:9182549). Anchors them to the cytoplasmic face of the mitochondrial outer membrane or allows them to reside in the endoplasmic reticulum (PubMed:9065479, PubMed:9182549). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (PubMed:32072193). Under diabetic conditions, myocardial AKAP1 expression decreases which blocks the translocation of NDUFS1 from the cytosol to mitochondria (PubMed:32072193). Reduction of NDUFS1 in mitochondria decreases ATP production and increases mitochondrial ROS level, which causes mitochondrial dysfunction and cell apoptosis, respectively, thereby leading to cardiac dysfunction (PubMed:32072193). Interacts with SLC8A3 (PubMed:24101730). Interacts with CFAP91. Interacts with CLPB (By similarity). Interacts with NDUFS1 (PubMed:32072193). Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 2 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 4 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. Highest expression in testis, heart, liver, skeletal muscle, intestine and kidney, followed by brain and lung. No expression in spleen. Isoform 1/D-AKAP1A is expressed predominantly in testis whereas isoform 4/D-AKAP1D is expressed primarily in liver (PubMed:9065479). Expression is decreased in hearts of diabetic mice (at protein level) (PubMed:32072193). RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Knockout in diabetogenic agent streptozotocin-treated mice results in significant cardiac dysfunction which is accompanied by impaired mitochondrial function and increased cardiomyocyte apoptosis.
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O88980
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MAIQFRSLFPLALPGMLALLGWWWFFSRKKDRLSSNGKQVGTLKVGPAIEDRLPTEEACPGVLSVTPSVTQPPGKEEQRSMDRPLSDPPALPRTRQVRRRSESSGNLPSIVDTRLQAGQCSDENSKVVLSLMGDEAKSIPLGRPLFPKDLSFPYEAVEGCKQESALGRTPGRGWLSQCAASGENARETGGAEGTGDAVLGESVLEEGLLPQECVSEVEKSEFPILAPGGGGGEKVRSGPPQVDELLKKEEYIVGKLPSSFVGPVHSELVKDEGALVPQVKGSQDRSLARELDKDKTLPEKDQIEQTAFQIISQVILEATEEIRATTVGKTVAQVHPTPGTQPQGQEESCVPASQETSLGQEIPDPASTRTGATASPSAGAPPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLDGASNPRGDDTFVTCTSNNSQSVLSVTSLGLCSDPVSTSRLEDSCTETISSSGDKAVTPPLPDSTEPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQTVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSCYASL
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Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity). Interacts with SLC8A3. Interacts with CFAP91. Interacts with CLPB (By similarity). Interacts with NDUFS1 (By similarity). Testis specific. By thyroid stimulating hormone (TSH) and cAMP or cAMP-analog. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
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Q9UG26
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MEIEVSVAECKSVPGITSTPHPMDHPSAFYSPPHNGLLTDHHESLDNDVAREIRYLDEVLEANCCDSAVDGTYNGTSSPEPGAVVLVGGLSPPVHEATQPEPTERTASRQAPPHIELSNSSPDPMAEAERTNGHSPSQPRDALGDSLQVPVSPSSTTSSRCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEDDEHEKEQYCIRKVRPSEEMLELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHKKYKERKERRAQQEQLLLQKQLQQQQQQPPSQLCTAPASSHERASMIDKAKEDIVTEQIDFSAARKQFQLMENSRQAVAKGQSTPRLFSIKPFYRPLGSVNSDKPLTNPRPPSVGGPPEDSGASAAKGQKSPGALETPSAAGSQGNTASQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDDDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETTNALQENSLADFSLPQTPQTDNPSEGRGEGVSKSFSDHGFYSPSSTLGDSPLVDDPLEYQAGLLVQNAIQQAIAEQVDKAVSKTSRDGAEQQGPEATVEEAEAAAFGSEKPQSMFEPPQVSSPVQEKRDVLPKILPAEDRALRERGPPQPLPAVQPSGPINMEETRPEGSYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTKNAPSLPSRTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQRPKNLMQTLMEDYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYANQEEEDNE
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Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity). The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Based on a naturally occurring readthrough transcript which produces a PALM2-AKAP2 fusion protein. Based on a naturally occurring readthrough transcript which produces a PALM2-AKAP2 fusion protein.
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Q8C5W1
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MEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEREKEQFCVRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQQQLQQQQLQQQQLQQQLQQQQLSTSQPCTAPAAHKHLDGIEHTKEDVVTEQIDFSAARKQFQLMENSRQTLAKGQSTPRLFSIKPYYKPLGSIHSDKPPTILRPATVGGTLEDGGTQAAKEQKAPCVSESQSAGAGPANAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPSALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEAHTSKEGSEQQEPEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNLPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQRPKNLMQTLMEDYETHKSKRRERMDDSSYTSKLLSCKVTSEVLEATRVNRRKSALALRWEAGIYANQEEEDNE
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Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP. Highly expressed in lung and weakly in thymus and cerebellum. Little or no expression in liver, heart and cerebral cortex. All isoforms are expressed in lung, but KL2A and KL2B isoforms are the principal isoforms in cerebellum. The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Produced by alternative splicing. Produced by alternative splicing. Produced by alternative initiation at Met-125 of isoform KL1A. Produced by alternative initiation at Met-125 of isoform KL2A.
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Q5U301
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MEIGVSVAECKSVPGITSTPHSKDHSSPFYSPSHNGLLTDHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSATKVEPIEKASGRQLPPHIELSRSPSDSMAEGERANGHSTDQPQDMLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEHEKEQFCIRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQKKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQLQQLQQQQQQQLSTSQLCTAPAAHEHLDSIEHTKEDVVTEQIDFSAARKQFQQMENSRQTLAKGQSTPRLFSIKPFYKPLGSINSDKPPTILRPATIGGTVEDSSTQAAKEQKALCVSESQSAGAGTGNAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPNALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEVHTSKEGSEQQEPGAMVEEAGSQAPGSEKPQGMFAPPQVSSPVQEKRDVLPKILPGEDKTLREKGPSQPPTAVQPSGPVNMKETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAQNAPSLPSRTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGAQRPKNLMQTLMEDYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYANQEEEDNE
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Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity). The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
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A6QQY3
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MSDRVDWLQSQNGVCKVDVYSPGDSQPQDWKMSDESLSIFKEASHDPIRVLSWLRRDLEKSTAGFQDIRFKPGESSLGREMVSSGDPRKGFCVDYYNTTSRGSPGRLHFEMSHRENPHQGPTCNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENRCVHQSVYMGDEPPPNKSLSKVASELVNETVTACSKNTPSDKAPGSGDRASGTLQSPPNLKYKSTLKIKESNKGGRGPDDRPSSKKSFFYKEVFESRNAGDAKEGGRTLPAERKMFRGYERPDDFTASISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATIVLKKVLIKHAKEVVSDLIDSFMKNLHNVTGTLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYSVIFAKKPPETVRKTKDKSESYSLVSMKGMGDPKHRNVNFASMKSEGKVRERVCTPTPKPEKSCVETLGEHIIKEGLTLWHNSQQKEGISACLQGSPFVTPKRQYKPVPDFPLGFPFDPCNFSLPMQCPEKPENFMCDSDSWAKDLLVSALLLIQYHLAQGGNMDAQSFLEAAGTSNLYPTKSPAVSHESSLRSPQVGADPEEVEKKDLMSVFFNLIRNLLSETIFKSDHSCDPKATKEDNSPQCERPVTPSPAKLNECDETGGAFAGLTKMVANKLDGHMNGQMVDHLMDSVMKLCLIIAKSCDSPLAELGDDKSGDASRPTSAFPESLYECLSTKGTGTAETLLQNAYQAIHNELRSLSAQPPEGCTAPKVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMVNL
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May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Interacts with ROPN1 AND ROPN1L. Interacts with QRICH2 (By similarity). Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment (By similarity). RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Phosphorylated on tyrosine. Belongs to the AKAP110 family.
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Q9UM61
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MSEKVDWLQSQNGVCKVDVYSPGDNQAQDWKMDTSTDPVRVLSWLRRDLEKSTAEFQDVRFKPGESFGGETSNSGDPHKGFSVDYYNTTTKGTPERLHFEMTHKEIPCQGPRAQLGNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENKCVYQSLYMGNEPTPTKSLSKIASELVNETVSACSRNAAPDKAPGSGDRVSGSSQSPPNLKYKSTLKIKESTKERQGPDDKPPSKKSFFYKEVFESRNGDYAREGGRFFPRERKRFRGQERPDDFTASVSEGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLLKHAKEVVSDLIDSFLRNLHSVTGTLMTDTQFVSAVKRTVFSHGSQKATDIMDAMLRKLYNVMFAKKVPEHVRKAQDKAESYSLISMKGMGDPKNRNVNFAMKSETKLREKMYSEPKSEEETCAKTLGEHIIKEGLTLWHKTQQKECKSLGFQHAAFEAPNTQRKPASDISFEYPEDIGNLSLPPYPPEKPENFMYDSDSWAEDLIVSALLLIQYHLAQGGRRDARSFVEAAGTTNFPANEPPVAPDESCLKSAPIVGDQEQAEKKDLRSVFFNFIRNLLSETIFKRDQSPEPKVPEQPVKEDRKLCERPLASSPPRLYEDDETPGALSGLTKMAVSQIDGHMSGQMVEHLMNSVMKLCVIIAKSCDASLAELGDDKSGDASRLTSAFPDSLYECLPAKGTGSAEAVLQNAYQAIHNEMRGTSGQPPEGCAAPTVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVDKGCSVGEVLQSVLRYEKERQLNEAVGNVTPLQLLDWLMVNL
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May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Interacts with ROPN1 AND ROPN1L. Interacts with QRICH2 (PubMed:30683861). Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment. Testis specific; only expressed in spermatids. RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Phosphorylated on tyrosine residues. Belongs to the AKAP110 family.
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Q497M9
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MADRVDWLQSQSGVCKVGVYSPGDNQHQDWKMDTSTDPVRVLSWLRKDLEKSTAGFQDSRFKPGESSFVEEVAYPVDQRKGFCVDYYNTTNKGSPGRLHFEMSHKENPSQGLISHVGNGGSIDEVSFYANRLTNLVIAMARKEINEKIHGAENKCVHQSLYMGDEPTPHKSLSTVASELVNETVTACSKNISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPGTKKSFFYKEVFESRNAGDAKEGGRSLPGDQKLFRTSPDNRPDDFSNSISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLMKHAKEVVSDLIDSFMKNLHGVTGSLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYNVMFAKKFPENIRRARDKSESYSLISTKSRAGDPKLSNLNFAMKSESKLKENLFSTCKLEKEKTCAETLGEHIIKEGLHMWHKSQQKSPGLERAAKLGNAPQEVSFECPDPCEANPPHQPQPPENFANFMCDSDSWAKDLIVSALLLIQYHLAQGGKMDAQSFLEAAASTNFPTNKPPPPSPVVQDECKLKSPPHKICDQEQTEKKDLMSVIFNFIRNLLSETIFKSSRNCESNVHEQNTQEEEIHPCERPKTPCERPITPPAPKFCEDEEATGGALSGLTKMVANQLDNCMNGQMVEHLMDSVMKLCLIIAKSCDSPLSELGEEKCGDASRPNSAFPDNLYECLPVKGTGTAEALLQNAYLTIHNELRGLSGQPPEGCEIPKVIVSNHNLADTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSATAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMANL
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May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Interacts with ROPN1 AND ROPN1L. Interacts with QRICH2 (By similarity). Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment. RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Phosphorylated on tyrosine. Belongs to the AKAP110 family.
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Q5JQD3
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MMAYSDTTMMSDDIDWLRSHRGVCKVDLYNPEGQQDQDRKVICFVDVSTLNVEDKDYKDAASSSSEGNLNLGSLEEKEIIVIKDTEKKDQSKTEGSVCLFKQAPSDPVSVLNWLLSDLQKYALGFQHALSPSTSTCKHKVGDTEGEYHRASSENCYSVYADQVNIDYLMNRPQNLRLEMTAAKNTNNNQSPSAPPAKPPSTQRAVISPDGECSIDDLSFYVNRLSSLVIQMAHKEIKEKLEGKSKCLHHSICPSPGNKERISPRTPASKIASEMAYEAVELTAAEMRGTGEESREGGQKSFLYSELSNKSKSGDKQMSQRESKEFADSISKGLMVYANQVASDMMVSLMKTLKVHSSGKPIPASVVLKRVLLRHTKEIVSDLIDSCMKNLHNITGVLMTDSDFVSAVKRNLFNQWKQNATDIMEAMLKRLVSALIGEEKETKSQSLSYASLKAGSHDPKCRNQSLEFSTMKAEMKERDKGKMKSDPCKSLTSAEKVGEHILKEGLTIWNQKQGNSCKVATKACSNKDEKGEKINASTDSLAKDLIVSALKLIQYHLTQQTKGKDTCEEDCPGSTMGYMAQSTQYEKCGGGQSAKALSVKQLESHRAPGPSTCQKENQHLDSQKMDMSNIVLMLIQKLLNENPFKCEDPCEGENKCSEPRASKAASMSNRSDKAEEQCQEHQELDCTSGMKQANGQFIDKLVESVMKLCLIMAKYSNDGAALAELEEQAASANKPNFRGTRCIHSGAMPQNYQDSLGHEVIVNNQCSTNSLQKQLQAVLQWIAASQFNVPMLYFMGDKDGQLEKLPQVSAKAAEKGYSVGGLLQEVMKFAKERQPDEAVGKVARKQLLDWLLANL
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Major structural component of sperm fibrous sheath. Plays a role in sperm motility. Interacts with PRKAR1A and PRKAR2A. Interacts with ENO4. Localizes to the principle piece of the sperm flagellum. Testis specific; only expressed in round spermatids. Post-meiotic phase of spermatogenesis. RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Belongs to the AKAP110 family.
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Q8R2G7
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MIAYCGTTTMSDDIDWLHSRRGVCKVDLYSPKGQQDQDRKVICFVDVSTLNVEDKDSKGAAGSRSEGELNLETLEEKEIIVIKDTEKQDQSKTEGSVCLFKQAPSDPISVLNWLLNDLQKYALGFQHALSPSASSCKHKVGDLEGDYSKIPSENCYSVYADQVNFDYLNKGPQNLRLEMAASKNTNNNQSPSNPATKSPSNQRSVATPEGECSMDDLSFYVNRLSSLVIQMARKEIKDKLEGGSKCLHHSMYTSGDKGKTSPRSAVSKIASEMAHEAVELTSSEMRGNGEDCRDGRKTFLYSEMCNKNKCGEKQQMCPKDSKEFADSISKGLMVYANQVASDMMVSVMKTLKVHSCGKPIPACVVLKRVLLKHTKEIVSDLIDSCMKNLHNITGVLMTDSDFVSAVKRNLFNHGKQNAADIMEAMLKRLVSALLGEKKETKSQSLAYATLKAGTNDPKCKNQSLEFSAMKAEMKGKDKCKSKADPCCKSLTSAERVSEHILKESLTMWNNQKQGNQGKVTNKVCCTSKDEKREKISPSTDSLAKDLIVSALMLIQYHLTQQAKGKDPCEEECPGSSMGYMSQSAQYEKCGGGQSSKSLSMKHFETRGAPGPSTCMKENQLESQKMDMSNMVLSLIQKLLSESPFSCDELTESDNKRCCDPRSSKAAPMAKRPEEQCQDNAELDFISGMKQMNRQFIDQLVESVMKLCLIMAKYSNNGAALAELEEQAALVGSGSRCGRDAMMSQNYSETPGPEVIVNNQCSTTNLQKQLQAVLQWIAASQFNVPMLYFMGDDDGQLEKLPEVSAKAAEKGYSVGDLLQEVMKFAKERQLDEAVGNMARKQLLDWLLANL
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Major structural component of sperm fibrous sheath. Plays a role in sperm motility (PubMed:12167408). Interacts with PRKAR1A and PRKAR2A (PubMed:9852104). Interacts with ENO4 (PubMed:23446454). Localizes to the principle piece of the sperm flagellum. Spermatid. Post-meiotic phase of spermatogenesis. RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Belongs to the AKAP110 family.
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O35774
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MIAYCGTTKMSDDIDWLHSRRGVCKVDLYSPEGQQDQDRKVICFVDVSTLNVEDDSKGAAGPRSDGELNLENLEEKEIIVIKDTEKQDQPKTEGSVCLFKQAPSDPISVLNWLLNDLQKYALGFQHALSPSASSCKHKVGDLEGDYHKIPSENCYSVYADQVNLDYLNKGPQNLRLEMAASKNTNNNQSPSNPATKSPSNQRSVATPDGECSMDDLSYYVNRLSSLVIQMARKEIKDKLEGGNKCLHHSMYTSGEKGKTSPRSAVSKIASEMAHEAVELTSSEMRGNGEEGRDGRKTFLYSELSNKNKCGEKQQMCPKDSKEFADSISKGLMVYANQVASDMMVSVMKTLKVHSCGKPIPACVVLKRVLLKHTKEIVSDLIDSCMKNLHNITGVLMTDSDFVSAVKRNLFNHGKQNAADIMEAMLKRLVSALLGEKKETKSQSLAYATLKAGTHDPKCKNQSLEFSAMKAEMKGKDKGKTKGDPCCKSLTSAERVSEHILKESLTMWNNQKQGTQGRVPNKVCPSKDEKREKISPSTDSLAKDLIVSALMLIQYHLTQQAKGKDPCEEECPGSSMGYMSQSAQYEKSGGGQSSKSLSMKHFESRGAPGPSTCAKENQLESQKMDMSNMVLSLIQKLLSESPFSCDELSESENKRCCDSRSKQAAPVAKRPEDQSQDSTEMDFISGMKQMNRQFIDQLVESVMKLCLIMAKYSNNGAALAELEEQAALASNGPRCGREAVMSQSYLETPGPEVIVNNQCSTSNLQKQLQAVLQWIAASQFNVPMLYFMGDDDGQLEKLPEVSAKAAEKGYSVGDLLQEVMKFAKERQLDEAVGNMARKQLLDWLLANL
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Major structural component of sperm fibrous sheath. May play a role in sperm motility (By similarity). Interacts with PRKAR1A and PRKAR2A. Interacts with ENO4. Localizes to the principle piece of the sperm flagellum. Expressed in flagella of epididymal sperm. RI-alpha binding site, predicted to form an amphipathic helix that is required for binding to Prkar1a. Belongs to the AKAP110 family.
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P24275
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MEITVSEIQVESKDETRSAEVRPQDERQEEKASMLCFKRRKKAAKAMKPKASSKAADAAKKCPPEARASDQPQRPGGAWDSIKRLVTRRKRSESSKQQKPFKAKLQSEINAEDANPSKKKAKSRLKIPCIKFSKGEKRSNHSKIIEDSDRSVKVQEAENLVTKTQTQSDDQATKSKSPQDVREDVSQKGDDEVCESNVNNSITSPGEKVISVELELDMGHSAIQRGTLILEKDTEMLEEKQSIQPQHVSPLEASDTEQELPVGSEVPPSSAVPDQQILEEARNGVLESGPDWKEHESREIVVEESKPKDTELSQELDFQENEITAEKPKPEESKRMEPIAIIITDTEISEFDVKKSKNVPKPFLISIENEQVGVFANDSGFEGRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNTINNRLQ
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Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses. Interacts with ADCY8, and enhances its phosphorylation at lipid rafts (By similarity). Binds dimer of the RII-beta regulatory subunit of cAMP-dependent protein kinase. Associates with lipid rafts. Predominantly in brain, and to a lesser extent in adrenal medulla, lung and anterior pituitary. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. The N-terminal region, which is highly basic, is required for interaction with calmodulin. Palmitoylated. Palmitoylation at Cys-36 and Cys-129 play a key role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis.
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A2RRB8
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METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVARKCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKKAKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQDLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQDVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIVAEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPKQFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNKINNLLQ
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Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors (PubMed:1512224). Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses (PubMed:25589740). Binding protein for dimer of the RII-beta regulatory subunit of cAMP-dependent protein kinase (PKA) and also for the protein kinase C (PKC) and the phosphatase calcineurin (PP2B). Each enzyme is inhibited when bound to the anchoring protein. Also binds the beta2-adrenergic receptor. Part of a complex containing AKAP5, ADCY5, ADCY6 AND PDE4C (By similarity). Interacts with ADCY8, and enhances its phosphorylation at lipid rafts. Associates with lipid rafts. Predominantly in the cerebral cortex and the postsynaptic densities of the forebrain, and to a lesser extent in adrenal medulla, lung and anterior pituitary. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. The N-terminal region, which is highly basic, is required for interaction with calmodulin. Palmitoylated (PubMed:21771783, PubMed:25589740). Palmitoylation at Cys-36 and Cys-129 play a key role in the targeting of AKAP5 to lipid rafts (PubMed:21771783). Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis (PubMed:25589740).
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D3Z5C9
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METSVSEIQVETKDEKGPVAASPQKERQERKTATLCFKRRKKANKTKPKAGSRTAEETKKHTPEAGGSGQRQPAGAWASIKGLVTHRKRSEPAKKQKPPEAEVQPEDGALPKKKAKSRLKFPCLRFSRGAKRSRHSKLTEDSGYVRVQGEADDLEIKAQTQPDDQAIQAGSTQGLQEGVLVRDGKKSQESHISNSVTSGENVIAIELELENKSSAIQMGTPELEKETKVITEKPSVQTQRASLLESSAAGSPRSVTSAAPPSPATTHQHSLEEPSNGIRESAPSGKDDRRKTAAEEKKSGETALGQAEEAAVGQADKRALSQAGEATAGHPEEATVIQAESQAKEGKLSQAEETTVAQAKETVLSQAKEGELSQAKKATVGQAEEATIDHTEKVTVDQAEETTVGQAEEATVGQAGEAILSQAKEATVVGQAEEATVDRAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGQAEEATVDWAEKPTVGQAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGHTEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDQAEEPTVDQAEEAISSHAPDLKENGIDTEKPRSEESKRMEPIAIIITDTEISEFDVKKSKNVPKQFLISMENEQVGVFANDSDFEGRTSEQYETLLIETASSLVKNAIELSVEQLVNEMVSEDNQINTLFQ
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Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses. Interacts with ADCY8, and enhances its phosphorylation at lipid rafts. Binds dimer of the RII-beta regulatory subunit of cAMP-dependent protein kinase (By similarity). Associates with lipid rafts. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. The N-terminal region, which is highly basic, is required for interaction with calmodulin. Palmitoylated. Palmitoylation at Cys-36 and Cys-123 play a key role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis.
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P70593
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METSVSEIQIETKDEKRPEAASPQKERQERKTATLCFKRRKKVNKKKAKAGSKTAEETEKHAPEAGGSGQRQPAGAWASIKRLVTHRKPSESAEKQKPSEAEMQPEDGALPKKKTKSKLKIPCIRFSRGAKRSRPSKLTEDSGYVRVQGEADDLEIKAQIQPDEQATQAKSTQGLQEDVIVRDGKEIQESHISNNVISGEHVIGIELELEKESSALRMRTPGSEKEAKVILVKQGVQVQEASVLENSAADSPQPVTSTAPLSPATTHQLGLEEPSDSIRESAPSGKDDGRRKTAAEEKKSGETALGQAEEASSVSQADKSVLSQAEEATVGHTEEATVIQAQSQAKEGKLSQAEEATVAQAKETVLSQAEEVKLSQIEEPAISQAKKATVGQAKEAYVSQAEEAIVGHTEKATMGQAEEATVGHIEKTTVGQAEEATVGQAEEATVGQAEEATVGQAEEATVGQAEEATVGQAGEATVSHIEKTTVGQAEEAIVGQAEEATVGQAEEATVGQAEEATVGQAEEATVDQAEEATVGQAEEATVGQAGEAAVGQAEEAIVAQAEEATVGQAGEATVGQAEKATVGQAEEPIVGQAEETVLRHASDLKVNGVDAEKPRSEESKRMEPIAIIITDTEISEFDVKKSKNVPKQFLISMENEQVGVFANDSDFEGRTSEQYETLLIETASSLVKNAIELSVEQLVNEMVSEDNQINTLFQ
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Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses. Interacts with ADCY8, and enhances its phosphorylation at lipid rafts (By similarity). Binds dimer of the RII-beta regulatory subunit of cAMP-dependent protein kinase. Associates with lipid rafts. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. The N-terminal region, which is highly basic, is required for interaction with calmodulin. Palmitoylated. Palmitoylation at Cys-36 and Cys-123 plays a key role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis.
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O15028
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MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGLGDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPGLTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEETFKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISSSLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQRSWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDILSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDSINEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAPSSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNSGSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKVGDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQPDVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSINEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPSDTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENLGSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSDALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENEVAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACVEGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAENLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR
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Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes. Interacts with RII subunit of PKA, phosphatase 2B (calcineurin) and AKAP79. Interacts with SYNPO2. In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences. Highly expressed in cardiac and skeletal muscle, followed by brain. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
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Q9WVC7
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MLTMSVTLSPLRSQGPDPMATDASPMAINMTPTVEQEEGEGEEAVKAIDAEQQYGKPPPLHTAADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQDYLSLDCGITAFELSDYSPSEDLLGGLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGEANEDSSQASLSDDHKGEHGEDGAPVPGQQLDSTVGMSSLDGTLANAAEHPSETAKQDSTSSPQLGAKKTQPGPCEITTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETQKNERKGSDRKGQVVDLKPELSRSTPSLVDPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGLGNLENIVRSHIKEISSSLGRLTDCHKEKLRLKKPHKTLAEVSLCRIPKQGGGSGKRSESTGSSAGPSMVSPGAPKATMRPETDSASTASGGLCHQRNRSGQLPVQSKASSSPPCSHSSESSLGSDSIKSPVPLLSKNKSQKSSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLESLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCLPLSSVKKFTDEKSERPSSSEKNESHSATRSALIQKLMHDIQHQENYEAIWERIEGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAGLKDTLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCHLETQRDAVEQMSLKLYSEQYTSGSKRKEEFANMSKAHAEGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEKVDSINEKWELLGKTLREKIQDTIAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDPEPMLPAVKLEETHHKDSGYEEEAGDCGGSPYTSNITAPSSPHIYQVYSLHNVELHEDSHTPFLKSSPKFTGTTQPTVLTKSLSKDSSFSSTKSLPDLLGGSGLVRPYSCHSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETEHPDPQMGDAANVLEQKFKDNGESIKLSSVSRASVSPVGCVNGKAGDLNSVTKHTADCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQPQSEKAHVEDPLLGGFYFDKKSCKAKHQASESQPDAPPHERILASAPHEMGRSAYKSSDIEKTFTGIQSARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDMTLQSSSQKMPFAGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLTREKKRSGVTDEIKVNKDGGGNEKANPSDTLDIEALLNGSIRCLSENNGNGKTPPRTHGSGTKGENKKSTYDVSKDPHVADMENGNIESTPEREREKPQGLPEVSENLASNVKTISESELSEYEAVMDGSEDSSVARKEFCPPNDRHPPQMGPKLQHPENQSGDCKPVQNPCPGLLSEAGVGSRQDSNGLKSLPNDAPSGARKPAGCCLLEQNETEESASISSNASCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSSTPLPPDAVDSGLDDKEDMDCFFEACVEDEPVNEEAGLPGALPNESAIEDGAEQKSEQKTASSPVLSDKTDLVPLSGLSPQKGADDAKEGDDVSHTSQGCAESTEPTTPSGKANAEGRSRMQGVSATPEENAASAKPKIQAFSLNAKQPKGKVAMRYPSPQTLTCKEKLVNFHEDRHSNMHR
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Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes (By similarity). Interacts with RII subunit of PKA, phosphatase 2B (calcineurin) and AKAP79. Interacts with SYNPO2. In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
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B0X6E8
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MTLDSYDKLLGTVLQEYKILTEYKRLQSEDLGGIYVIPSHENSFVWFGVLFVRSGPYKNGVFRFTLTLPDKFPNDSAVPTVVFQSETFHPLVCPYNGTLELSEAFAKWKSGENHLWQVLKFIQYVFAHFEEYMAVAELTANNVAHELFQQSRADFLQRVEECVRLSQAKVYDPAPVQDRNYIVFEQFDGAVHGPVLESMKQGRANEVGTTPPSSGLSWVKEGVFQPLSKQG
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q6P3I9
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MNPFWSMSTNAGRKRSDGEEQSGSGEQRASPARPPFGKKQLPSIPKNAVPITKAASPASSTQSANGTHASYGPFYLEYSLLAEFTLVIKQKLPGIYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPKVVFDTPVFHPLVDPVSGELDVRRAFTKWRRNHNHIWQVLMYARTIFYKINTMEPLNPEAAVLYDKDIQLFKSKVVDSVKLCNSHLFDQPKIDDPYAISFSPWNPAVHEEAKEKMFAHKRRPEDFNKGLPVSGLSWVKPGSTQPFSKEDNPLQT
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May function to promote vesicle trafficking and/or fusion. May also regulate apoptosis (By similarity). Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q53H38
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MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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Component of the FTS/Hook/FHIP complex (FHF complex) (PubMed:32073997). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2 and HOOK3 (PubMed:18799622, PubMed:32073997). The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex) (PubMed:18799622). Also interacts with AKT1. May interact with FHIP1A (PubMed:32073997). Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q4R5E1
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MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1. May interact with FHIP1A. Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q3TYE3
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MNPLWSMSAGSVRKRAEGEEKTLAGDVKTSPPRSAPKKQLPSIPKNALPIAKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLLFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPDEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1. May interact with FHIP1A. Ubiquitous. Highest expression in kidney, testis and brain and lowest in spleen and liver. Defects in Aktip are a cause of embryonic death in homozygous animals. Death occurs at about 10 days of development. Symptoms include loss of left-right asymmetry, malformation of the developing brain and of the spinal cord, syndactyly and polydactyly. Heterozygous animals are characterized by polydactyly and thymic hyperplasia. Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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A7RRG3
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MLNVTHQLKKKLFLSDLDEKSSSSPHDEKKPGDGREVREEKSKRKALPALPSPAEEKSMNLSIARQRSPSGSSPEQVKAYGPFFLEYTLMAEYNQLRSQRLPGVYVLPAAKSALVWYGVIFIRMGLYQDGIFKFQMTIPENFPDGDCPTLVFKPTIFHPVVNIETGELDVRRAFPRWRRNINHLWQVLLYAKRIFYKIDSRDPLNPEAAEMYQNDKDRYKQKVNECLRRCHNELHLAVADDPHAIKFVELTPEKQDDVKNQIIESQSKPECLPTANAHKSGLSWMKKGGAIFSKEES
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q5RE48
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MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVQVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1. May interact with FHIP1A. Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q5FVH4
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MNPLWSMSSGSVRKRAEGEEKTLAGDVKTSPPRSAPKKQLPSIPKNALPISKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTMVVKQKLPGVYVQPSYRSALVWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLLFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPDEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1. May interact with FHIP1A. Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B5X1G6
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MNLNPFWSMSTNTGRKRSDGEEQSGEQQQQQRASPARPSFGKKQLPSIPKNALPITKPASPAATAQLANGTHASYGPFYLEYSLLAEFTLVIKQKLPGIYVQPSYKSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGECPRVVFDIPVFHPLVDPVSGELDVRRAFTKWRRNHNHIWQVLMYARTVFYKINTMEPLNPEAAVLYDKDVQLFKSKVVDSVKLCNSHLFDQPKMDDPYAISFSSWNPAIHDDAKERMFTHKRRPEDHHKGLQVSGLSWVKPGSTQPFSKDDNPPQN
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May function to promote vesicle trafficking and/or fusion. May also regulate apoptosis (By similarity). Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q28IA3
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MNPFWNMSSAAVRKRSDNDEKIATGDQKISPPRSSSAKKQLPSIPKNAVPITKPISPSPSVQPTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGECPRLVFDVPVFHPLVDPVSGELDVKRAFTKWRRNHNHIWQVLMYARRIFYKIDTTSPLNPEAAVLYEKDVQLFKSKVVDSVKLCNSHLFDQPKIEDPYAIIFSPWNPVLHDDARERMLAQKKSEEQSKGLHVSGLSWVKPGSVLPFSKEENSLQT
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May function to promote vesicle trafficking and/or fusion. May also regulate apoptosis (By similarity). Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B3MEZ6
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MTLDLDASKKDEKLLITTIQQEYKILAEYKMIESEKLSGIYVIPSYENSLQWYGVFFGRQGFYAESVFRFSILLPDRFPDEKSLPSIIFQQDVMHPHVCPFTHTLDISHAFSEWRCGEDHLWQVLKYMQAIFFDPVDSIRGIETDKLKNAEAAELLMNNRQEYAARVQENIKESKAHIYDTPPTEDPHYIVFEKFQPDVHGPVLERIKAGRNKAEASQQANGGHATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B3N6U7
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MTLDLDANKKDDKLLLTTIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRQGFYTESVFRFTILLPDRFPDDKSLPTIIFQQDVIHPHVCPYTHGLDVSHAFPEWRCGEDHLWQLLKYLQTIFSDPLDSIRGIELDKLKDSEAAELLMTNKEEYVARVQKNIKESKEHIFDTPPTEDPHYIVFEKFQQDVHGPVLERIKAGRSKQTEPSAQQANGGHATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4J613
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MTLDLDAQKKDEKLLLATIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRHGFYEKSVFRFSILLSDGFPDDKSVPAIVFQHNVVHPLVCPYTYSLDLSHAFHEWRPAEDHLWQVLKYMQAIFADPLESIRNVSTVHERSNAEIIKLLNNNRDAYAALVQESILESKAHIYDNPHTEDPHYIIFEKFQDDIHGPVLEQIRQNRATVGSTESGGGGGAATGLSWVKFKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q7JRK3
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MTLDLDAHKKDDKLLITTIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRQGLYAESVFRFTILLPDRFPDDKSLPSIIFQQDVIHPHVCPYTHSLDVSHAFPEWRCGEDHLWQLLKYLQVIFSDPLDSIRGIEVDKLKNSEAAELLMNNKEEYVARVQENIKESKEHIFDTPPTEDPHYIVFEKFQQDVHGPVLERIKAGRSKLTEPSAQQANGGHATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4KMF8
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MTLDVDAQKKDEKLLLATIHQEYKILAEYKMIESEKVSGIYVIPSYANSLQWFGVFFGRQGFYENSVFRFSILLPDGFPQDKTTPAIVFQQNVVHPLVCPFTNSLDISHAFPEWRCGEDHLWQVLKYMQVIFADPLECIRSVGSTQELSNVEASKLLTTNRDAFAALVQESIAESKAHIYDTPPTEDPHYIVFEKFQEDIHGPVLEQIRNGRTTNSPAESGGGGAATGLSWVKVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4H581
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MTLDLDANKKDDKILITTIQQEYKILAEYKMIESEKLGGIYTIPSLANSLQWFGVFFGRQGLYSESVFRFSLLLPDRFPDDKSLPTVIFQQNILHPHVCPYTNSLDISHAFPEWRCGEDHLWQLFKYMQAIFSDPIDSIRGIEMDKIKNPEAAELLLTNREEFAARVLENIKESKEHIYDPQPTEDPHYIVFEKFQPDVHGPVLERIKAGRNNQTDSTLQQTNGGTATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q28XA5
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MTLDLDANKKDDKILITTIQQEYKILAEYKMIESEKLGGIYTIPSLANSLQWFGVFFGRQGLYSESVFRFSLLLPDRFPDDKSLPTVIFQQNILHPHVCPYTNSLDISHAFPEWRCGEDHLWQLFKYMQAIFSDPIDSIRGIEMDKIKNPEAAELLLTNREEFAARVLENIKESKEHIYDPQPTEDPHYIVFEKFQPDVHGPVLERIKAGRNNQTDSTLQQTNGGTATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4HT57
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MTLDLDAHKKDDKLLITTIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRQGLYAESVFRFTILLPDRFPDDKSLPTIIFQQDVIHPHVCPYTHSLDVSHAFPEWRCGEDHLWQLLKYLQVIFSDPLDSIRGIEVDKLKNREAAELLMNNKEEYVARVQENIKESKEHIFDTPPTEDPNYIVFEKFQQDVHGPVLDRIKAGRSKQTEPSAQQGNGGHATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4QHS6
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MTLDLDAHKKDDKLLITTIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRQGLYAESVFRFTILLPDRFPDDKSLPTIIFQQDVIHPHVCPYTHSLDVSHAFPEWRCGEDHLWQLLKYLQVIFSDPLDSIRGIEVDKLKNREAAELLMNNKEEYVARVQENIKESKEHIFDTPPTEDPHYIVFEKFQQDVHGPVLERIKAGRSKQTEPSAQQGNGGHATGLSWVKEGEFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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B4LNV5
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MTLDVDAQKKDEKLLLSTIQQEYKILAEYKMIESEKVSGIYVIPSYANSLQWFGVFFGRQGFYENSVFRFSILLPDGFPDDKAVPAIIFQHNVVHPLVCPYTNSLDISHAFPEWRCGEDHLWQVLKYIQAIFADPLDSIRSVANIQELSNPEASKLLNTNRDAYAALVQESIVESKSRVYDTPPTEDPHYIVFEKFQANVHGPVLDQIRKSRNTIVPAESGVGGAATGLSWVKVKEGDFKPLSIE
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Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily. Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.
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Q3MHL5
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MSSSAMPDVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEEKLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLIERDHLLLATMEAMNGGKLFSNAYLMDLGGCIKTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQIIPWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGSLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSALQSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTIKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:7786847). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (PubMed:7786847). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (Probable). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Has a much higher catalytic efficiency toward all-trans retinal. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). Expressed in muscle, liver, small intestine, kidney, brain, lung, heart but not detected in erythrocytes (at protein level). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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P27463
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MKKQGSPSNPAPVLPALPEPLKDLKIKYTKIFINNEWHDSVSGKKFEVFNPANEEKICEVAEGDKADIDKAVKAARKAFELGSPWRTMDASERGRLLNKLADLVERDRLTLATMEAIDGGKLFSTAYLMDLGACIKTIRYCAGWADKIHGRTVPMDGNFFTFTRHEPVGVCGQIIPWNFPLVMFIWKIAPALCCGNTVVVKPAEQTPLSALYMGSLIKEAGFPPGVVNIVPGFGPTAGAAISHHMDIDKVSFTGSTEVGKLIKEAAGKTNLKRVTLELGGKSPNIIFADADLDEAAEFAHIGLFYHQGQCCIAGSRIFVEEPIYDEFVRRSIERAKKYTLGDPLLPGVQQGPQIDKEQFQKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDDMRIAKEEIFGPVQQIMKFKTIDEVIKRANNTTYGLAAAVFTKDIDKALTFASALQAGTVWVNCYSAFSAQCPFGGFKMSGNGRELGEYGLQEYTEVKTVTIKIPQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (By similarity). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer. Belongs to the aldehyde dehydrogenase family.
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P15437
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MSSSGTPDLPVLLTDLKFQYTKIFINNEWHDSVSGKKFPVFNPATEEKLCEVEEGDKEDVNKAVAAARQAFQIGSPWRTMDASERGRLLYKLADLVERDRLILATMESMNGGKLFSNAYLMDLGGCLKTLRYCAGWADKIQGRTIPSDGNFFTYTRHEPVGVCGQILPWNFPLLMFLWKIAPALSCGNTVVVKPAEQTPLSALHVATLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPFIVFADADLETALEVTHQALFYHQGQCCVAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVSDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTTYGLFAGSFTKDLDKAITVSAALQAGTVWVNCYGVVSAQCPFGGFKMSGNGREMGEYGFHEYTEVKTVTVKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (By similarity). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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Q5SYR1
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MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:19296407, PubMed:12941160, PubMed:15623782, PubMed:17175089, PubMed:26373694, PubMed:25450233). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (By similarity). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:19296407, PubMed:12941160, PubMed:15623782). Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (PubMed:17175089). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Inhibited by citral, disulfiram, and cyanamide. Activated by diethylstilbestrol (PubMed:19296407). Inhibited by duocarmycin analogs (PubMed:26373694). Optimum pH is 7.1-9 for the 3-deoxyglucosone dehydrogenase activity. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (PubMed:33495566). Expressed by erythrocytes (at protein level). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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Q8HYE4
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MSSSGTSDLPVLPTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGATQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTNDIDKAVTISSALQAGTVWVNCYGVVTAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12576512). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (PubMed:12576512). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (Probable). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal. Optimum pH is 9.0. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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P86886
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MSSPAQPEVPAPLANLKIQYTKIFINNEWHDSVSGKKFPVINPATEEVICHVEEGDKADIDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLMERDRLLLATLEATNGGKVFASSYLFDLGGCIKALKYCAGWADKVHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPLLMFIWKIGPALGCGNTVIVKPAEQTPLTALYMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDTAVEFAHYGVFYHQGQCCVAASRLFVEESIYDEFVRRSVERAKKYVLGNPLNSGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGYFVQPTVFSNVTDDMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTSYGLAAGVFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGIYEYTELKTVAIKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (By similarity). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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Q811J0
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MSSPAQPAVPAPLADLKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12851412). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (PubMed:12851412). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (Probable). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:17567582). Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (PubMed:26430123). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH The aminobutyraldehyde dehydrogenase activity is negatively regulated by ethanol in vivo. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). Expressed in retina (PubMed:1935685). Expressed in lens and cornea (at protein level) (PubMed:17567582). Expressed by midbrain dopamine neurons (PubMed:26430123). The N-terminus is blocked most probably by acetylation. Mice lacking Aldh1a1, obtained at the expected Mendelian ratio, are viable and fertile without obvious defects in growth or survival (PubMed:12851412). However, they are more sensitive to retinol toxicity and are less efficient at metabolizing excess retinol to retinoic acid/RA (PubMed:12851412). An excess of retinol leads to the accumulation of retinaldehyde in these mice (PubMed:12851412). Enhanced alcohol consumption and preference is also observed in knockout mice (PubMed:26430123). A consistent lenticular opacification is also detected in old mice (PubMed:17567582). Belongs to the aldehyde dehydrogenase family. Extended N-terminus.
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Q8MI17
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MADLPTPLTNLKIQYTKIFINNEWHDSVSGKKFPVLNPATEEQICLIEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESLNAGKLFPNAYLMDLGGCIKTLRYCAGWADKIQGRTMPMDGDFFCYTRHEPVGVCGQIIPWNFPLVMLIWKIGPALSCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERAKKYVLGNPLAPEVNQGPQIDKEQYNKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTTYGLSAGIFTKDLDKAVTVSSALQAGTVWVNCYSVVSAQVPFGGFKMSGNGRELGEYGLQQYTEVKTVTVKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12941160). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:12941160). Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Has a lower activity toward propanal. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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O09184
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MSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATIEAINGGKVFANAYLSDLGGSIKALKYCAGWADKIHGQTIPSDGDIFTFTRREPIGVCGQIIPWNFPLLMFIWKIGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVRKSVERAKKYVLGNPLTQGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDDVIKRANNTTYGLAAGVFTKDLDRAITVSSALQAGVVWVNCYMILSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:7832787, PubMed:15623782). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (PubMed:7832787). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:15623782). Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Inhibited by chloral hydrate. Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal. Cofactor metabolism; retinol metabolism. Homotetramer (By similarity). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver. The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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P51977
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MSSSAMPDVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEEKLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCIKTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQIIPWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGSLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSALQSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTIKISQKNS
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Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:26373694). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity). an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH 9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) + NADH 11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) + NADH 13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) + NADH 3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-gluconate + 2 H(+) + NADH (E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-enoate + 2 H(+) + NADH H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) + NADH H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH Inhibited by duocarmycin analogs. Cofactor metabolism; retinol metabolism. Homotetramer (PubMed:26373694, PubMed:9862807). Interacts with PRMT3; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (By similarity). The N-terminus is blocked most probably by acetylation. Belongs to the aldehyde dehydrogenase family.
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Q549A6
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MTSSKIEMPGEVKADPAALMASLHLLPSPTLNLEIKHTKIFINNEWQNSESGRVFPVYNPATGEQICEIQEADKVDTDKAVRAARLAFSLGSVWRRMDASERGQLLDKLADLVERDRAVLATMESLNSGKPFLQAFYVDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGFGPIVGAAIASHVGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIYVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGITEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTVDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGESGLREYSEVKTVTIKIPQKNS
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Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral. H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate Cofactor metabolism; retinol metabolism. Homotetramer. Belongs to the aldehyde dehydrogenase family.
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Q9UFY0
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MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
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Converts retinaldehyde to retinoic acid (PubMed:29240402). Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity). H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate Cofactor metabolism; retinol metabolism. Homotetramer. Belongs to the aldehyde dehydrogenase family.
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Q6DI79
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MTSSEIAMPGEVKADPAALMASLQLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVCNPATGEQVCEVQEADKVDIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRATLATMESLNGGKPFLQAFYIDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFTWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVKRSVERAKRRIVGSPFDPTTEQGPQIDKKQYNKVLELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALMVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
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Converts retinaldehyde to retinoic acid (PubMed:8797830). Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal (By similarity). Lacks activity with benzaldehyde, acetaldehyde and octanal (PubMed:8797830). Displays complete lack of activity with citral (By similarity). H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate Cofactor metabolism; retinol metabolism. Homotetramer. Belongs to the aldehyde dehydrogenase family.
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Q4FZY8
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MTSSEIAMPGEVKADPAALMASLQLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVCNPATGEQVCEVQEADKVDIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRATLATMESLNGGKPFLQAFYIDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFTWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVKRSVERAKRRIVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALMVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
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Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral. H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate Cofactor metabolism; retinol metabolism. Homotetramer. Found in testis and less abundantly in lung, brain, heart, liver and kidney. Belongs to the aldehyde dehydrogenase family.
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Q9I8W8
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MTSSKIEMPGEVKADPAALMASLHLLPSPTLNLEIKYTKIFINNEWQNSESGRIFPVYNPATGEQICDIQEADKVDTDKAVRAARLAFSLGSVWRRMDASERGHLLDKLADLVERDRAILATMESLNSGKPFLQAFYVDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGFGPIVGAAIASHVGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIYVEESIYEEFVRKSVKRAKRKIVGSPFDPTTEQGPQIDKKQYNKILELIQSGITEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGSKSGNGREMGECGLREYSEVKTVTIKIPQENS
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Converts retinaldehyde to retinoic acid (PubMed:10985355). Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal (By similarity). Has only very low activity with benzaldehyde and acetaldehyde. Displays complete lack of activity with citral (PubMed:10985355). It is responsible for the ability of brain sites to synthesize retinoic acid. Its activity in the high vocal center (HVC) is required for the song of juvenile zebra finches to become stereotyped (PubMed:10985355). H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate Cofactor metabolism; retinol metabolism. Homotetramer. Expressed in the high vocal center (HVC) which integrates auditory and motor activities and constitutes a nodal nucleus on the song system. Belongs to the aldehyde dehydrogenase family.
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Q6NT64
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MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
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NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (PubMed:27759097). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (PubMed:27759097). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity). all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer. Expressed at low levels in many tissues and at higher levels in salivary gland, stomach, and kidney. The disease is caused by variants affecting the gene represented in this entry. Belongs to the aldehyde dehydrogenase family.
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Q9JI72
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MATTNGAVENGQPDGKPPALPRPIRNLEVKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLEEKNP
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NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (PubMed:11044606, PubMed:11013254, PubMed:14623956). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (By similarity). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (PubMed:14623956). all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer. Detected in embryonic head (at protein level) (PubMed:14623956). Ventral retina. In mouse embryos, RALDH3 expression is first noticed in the ventral optic eminence at 8.75 dpc, then in the optic vesicle/cup, otic vesicle and olfactory placode/pit from 9.5 dpc to 11.5 dpc. Mutant mice are born at the expected Mendelian rate, but all die within 10 hours after birth (PubMed:14623956, PubMed:23536097). Lethality is due to respiratory distress, caused by choanal atresia, i.e. the lack of communication between the nasal and oral cavities. Mutant embryos at 11.5 dpc lack detectable retinoic acid in the ventral retina, nasal epithelium and in the nasolacrimal groove. At 14.5 dpc mutant embryos display shortening of the ventral retina associated with lens rotation and persistence of the retrolenticular membrane, indicative of retinoic acid deficiency. Still, at 18.5 dpc the ventral retina appears normal. Embryos at 18.5 dpc lack Harderian glands, and display multiple malformations in the nasal region, including choanal atresia, lack of maxillary sinuses and nasolacrimal ducts (PubMed:14623956). Oral gavage of pregnant females with retinoic acid prevents choanal atresia and other malformations of the nasal region (PubMed:14623956, PubMed:23536097). Females that were fed retinoic acid give birth to pups with malformations of the inner ear vestibular organ, causing repetitive circling behavior with head tilting (PubMed:23536097). Likewise, mice display impaired ability in crossing a beam without slipping and an impaired ability to swim (PubMed:23536097). Belongs to the aldehyde dehydrogenase family.
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Q8K4D8
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MATANGAVENGQPDGKPPALPRPIRNLEVKFTKIFINNDWHEPKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLIERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVMCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGRNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWVNCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLDEKNP
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NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (By similarity). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (By similarity). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity). all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH Cofactor metabolism; retinol metabolism. Homotetramer. Belongs to the aldehyde dehydrogenase family.
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Q80ZX7
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MSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQISQKNS
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Can oxidize benzaldehyde, propionaldehyde and acetaldehyde (By similarity). No detectable activity with retinal. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Highest level in liver, high level in lung, low level in kidney and testis. Xenopus embryos injected with Aldh1a7 mRNA failed to produce retinoic acid in contrast to embryos injected with Aldh1a1. Belongs to the aldehyde dehydrogenase family.
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P13601
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MSSPAQPAVPAPLANLKIQHTKIFINNEWHNSLNGKKFPVINPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGCLLNKLADLMERDRVLLATMESMNAGKIFTHAYLLDTEVSIKALKYFAGWADKIHGQTIPSDGDVFTYTRREPIGVCGQIIPWNGPLILFIWKIGAALSCGNTVIVKPAEQTPLTALYMASLIKEAGFPPGVVNVVPGYGSTAGAAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYVLGNPLDSGISQGPQIDKEQHAKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSIDEVIKRANNTPYGLAAGVFTKDLDRAITVSSALQAGTVWVNCYLTLSVQCPFGGFKMSGNGREMGEQGVYEYTELKTVAMKISQKNS
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Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal. Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Very low levels in lung and liver. By phenobarbital. Belongs to the aldehyde dehydrogenase family.
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Q7V6D4
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MPTLEMPVAAVLDSTVGSSEALPDFTSDRYKDAYSRINAIVIEGEQEAHDNYIAIGTLLPDHVEELKRLAKMEMRHKKGFTACGKNLGVEADMDFAREFFAPLRDNFQTALGQGKTPTCLLIQALLIEAFAISAYHTYIPVSDPFARKITEGVVKDEYTHLNYGEAWLKANLESCREELLEANRENLPLIRRMLDQVAGDAAVLQMDKEDLIEDFLIAYQESLTEIGFNTREITRMAAAALVS
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Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane. a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+) Binds 2 metal cations per subunit. The catalytic dinuclear metal-binding site could be either a di-iron or a manganese-iron cofactor. Belongs to the aldehyde decarbonylase family.
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Q54764
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MPQLEASLELDFQSESYKDAYSRINAIVIEGEQEAFDNYNRLAEMLPDQRDELHKLAKMEQRHMKGFMACGKNLSVTPDMGFAQKFFERLHENFKAAAAEGKVVTCLLIQSLIIECFAIAAYNIYIPVADAFARKITEGVVRDEYLHRNFGEEWLKANFDASKAELEEANRQNLPLVWLMLNEVADDARELGMERESLVEDFMIAYGEALENIGFTTREIMRMSAYGLAAV
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Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane. a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+) Binds 2 metal cations per subunit. The catalytic dinuclear metal-binding site could be either a di-iron or a manganese-iron cofactor. Belongs to the aldehyde decarbonylase family.
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Q55688
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MPELAVRTEFDYSSEIYKDAYSRINAIVIEGEQEAYSNYLQMAELLPEDKEELTRLAKMENRHKKGFQACGNNLQVNPDMPYAQEFFAGLHGNFQHAFSEGKVVTCLLIQALIIEAFAIAAYNIYIPVADDFARKITEGVVKDEYTHLNYGEEWLKANFATAKEELEQANKENLPLVWKMLNQVQGDAKVLGMEKEALVEDFMISYGEALSNIGFSTREIMRMSSYGLAGV
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Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane. a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+) Binds 2 metal cations per subunit. The catalytic dinuclear metal-binding site could be either a di-iron or a manganese-iron cofactor. Abolishes the presence of alkanes. Belongs to the aldehyde decarbonylase family.
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C5I9X1
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MSSGANGSSKSASHKIKFTKLFINGEFVDSISGNTFDTINPATEEVLATVAEGRKEDIDLAVKAAREAFDNGPWPRMSGEARRKIMLKFADLIDENADELTTLEVIDGGKLFGPVRHFEVPVSSDTFRYFAGAADKIRGATLKMSSNIQAYTLREPIGVVGHIIPWNGPAFMFATKVAPALAAGCTMVIKPAEHTPLTVLFLAHLSKLAGVPDGVINVVNGFGKTAGAAVSSHMDIDMVTFTGSTEVGRTVMQAAALSNLKPVSLELGGKSPLIVFDDADVDKAAEFAILGNFTNKGEMCVAGSRVFVQEGIHDVFVKKLEGAVKAWATRDPFDLATRHGPQNNKQQYDKVLSCINHGKKEGATLVTGGKPFGKKGYYIEPTLFTNVTDDMTIAKEEIFGPVISVLKFKTVEEVIKRANATKYGLASGVFTKNIDVVNTVSRSIRAGAVWVNCYLALDRDAPHGGYKMSGFGREQGLEALEHYLQIKTVATPIYDSPWL
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Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (Ref.1, PubMed:27488942). Catalyzes the NAD(P)-dependent oxidation of artemisinin precursors, artemisinic and dihydroartemisinic aldehydes, thus producing artemisinic and dihydroartemisinic acids, respectively (Ref.1). Can use both NAD and NADP as proton donors (Ref.1). (+)-artemisinic aldehyde + H2O + NADP(+) = (+)-artemisinate + 2 H(+) + NADPH (11R)-dihydroartemisinic aldehyde + H2O + NADP(+) = (11R)-dihydroartemisinate + 2 H(+) + NADPH (11R)-dihydroartemisinic aldehyde + H2O + NAD(+) = (11R)-dihydroartemisinate + 2 H(+) + NADH H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate (E)-non-2-enal + H2O + NADP(+) = (E)-non-2-enoate + 2 H(+) + NADPH kcat is 1.53 sec(-1) with artemisinic aldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) (Ref.1). kcat is 7.74 sec(-1) with dihydroartemisinic aldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) (Ref.1). Optimum pH is 8.5. Sesquiterpene biosynthesis. Homotetramer. Expressed both in apical and sub-apical cells of glandular secretory trichomes (PubMed:22195571, Ref.1). Also present in flower buds and, at low levels, in leaves (Ref.1). Also present in non-glandular trichome cells (PubMed:30851440). Artemisinin and derivatives (e.g. artesunate), are antimalarial drugs due to their endoperoxidase properties; they also display multiple pharmacological actions against inflammation,viral infections, and cell and tumor proliferation (PubMed:32514287, PubMed:32405226). Artesunate may be a promising treatment for COVID-19 mediated by the severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) because of its anti-inflammatory activity, NF-kappaB (nuclear factor kappa B)-coronavirus effect and chloroquine-like endocytosis inhibition mechanism (PubMed:32514287, PubMed:32405226). Yeast (S.cerevisiae) has been engineered to produce artemisinic-acid, a precursor of the antimalarial artemisinin compound, by expressing AMS1/ADS, CYP71AV1, ADH1 and ALDH1 in conjunction with CYB5 and CPR1. Belongs to the aldehyde dehydrogenase family.
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Q28399
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MSSSGMPDLPAPLTNIKIQHTKLFINNEWHESVSGKTFPVFNPATEEKICEVEEADKEDVDKAVKAAREAFQMGSPWRTMDASERGQLIYKLADLIERDRLLLATLESINAGKVFASAYLMDLDYCIKALRYCAGWADKIQGRTIPVDGEFFSYTRHEPIGVCGLIFPWNAPMILLACKIGPALCCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKMIQEAAAKSNLKRVTLELGAKNPCIVFADADLDSAVEFAHQGVFTNQGQSCIAASKLFVEEAIYDEFVQRSVERAKKYVFGNPLTPGVNHGPQINKAQHNKIMELIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDDMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTYYGLVAGVFTKDLDKAVTVSSALQAGTVWVNCYLAASAQSPAGGFKMSGHGREMGEYGIHEYTEVKTVTMKISEKNS
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Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Eye specific, with very high expression in the lens. Belongs to the aldehyde dehydrogenase family.
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P30840
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MEAYVLSLSDVLFNILFIGVCILSVLLLISHALKYIIGDSKEKKLFNQRLEQIKNQQPLEPTKYQDIQTICKTLKESYSTNALRHLDARKEVLYCLYRMVLDNKQAISNAIREDLHRDVGMCVAEVNSVIHEINFLRKNLNKYLKRKQVPTVCAQLFGKSFVEREPYGCVCVISPWNFPANLSLIPCAGALACGNTVFLKMSKYSMATSKLIAELCDKYIPSEYLRCEYLTGREAIQECCSASFDYYFFTGSTYVGKLINQAAAEKMVPATLELGGKNPAIVDKSVNLKVAAKRIAWAKSINAGQICVCVDHVFVPRSIKNEFCEAVKNSFIKFFGEDQKKSEDFGRIITKSAAKKMKEIIDQSDVYYGGEVDIENKYVQPTILQNVKIDDLCMKEEIFGPILPVIEYDTLDEVFEMVKQHPNPLACYVFTEDNDMFEHVIANINSGAIYNNDSIVHLLNPNLPFGGNCQSGIGCYHGKYTFDTFSRPRAVCNGHTSFDLSLKDWPFTSFQSWAVDRMAASEIPVVSYL
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an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Belongs to the aldehyde dehydrogenase family.
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Q29490
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MSSSGMPDLPAPLTNIKIQHTKLFINNEWHDSVSGKTFPVFNPATEEKICEVEEADKEDVDKAVKAAREAFQMGSPWRTMDASERGQLIYKLADLIERDRLLLATLESINAGKIFASAYLMDLDYCIKVLRYCAGWADKIQGRTIPVDGEFFSYTRHEPIGVCGQIFPWNAPMILLACKIGPALCCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKMIQEAAAKSNLKRVTLELGAKNPCIVFADADLDSAVEFAHQGVFTNQGQSCIAASKLFVEETIYDEFVQRSVERAKKYVFGNPLTPGVNHGPQINKAQHNKIMELIESGKKEGAKLECGGGPWGNKGYFIQPTIFSNVTDDMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTYYGLVAGVFTKDLDKAVTVSSALQAGTVWVNCYLAASAQSPAGGFKMSGHGREMGEYGIHEYTEVKTVTMKISEKNS
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Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Homotetramer. Eye specific, with very high expression in the lens. Belongs to the aldehyde dehydrogenase family.
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