UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
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Q96H80
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MFSAGAESLLHQAREIQDEELKKFCSRICKLLQAEDLGPDTLDSLQRLFLIISATKYSRRLEKTCVDLLQATLGLPACPEQLQVLCAAILREMSPSDSLSLAWDHTQNSRQLSLVASVLLAQGDRNEEVRAVGQGVLRALESRQPEGPSLRHLLPVMAKVVVLSPGTLQEDQATLLSKRLVDWLRYASLQQGLPHSGGFFSTPRARQPGPVTEVDGAVATDFFTVLSSGHRFTDDQWLNVQAFSMLRAWLLHSGPEGPGTLDTDDRSEQEGSTLSVISATSSAGRLLPPRERLREVAFEYCQRLIEQSNRRALRKGDSDLQKACLVEAVLVLDVLCRQDPSFLYRSLSCLKALHGRVRGDPASVRVLLPLAHFFLSHGEAAAVDSEAVYQHLFTRIPVEQFHSPMLAFEFIQFCRDNLHLFSGHLSTLRLSFPNLFKFLAWNSPPLTSEFVALLPALVDAGTALEMLHALLDLPCLTAVLDLQLRSAPAASERPLWDTSLRAPSCLEAFRDPQFQGLFQYLLRPKASGATERLAPLHQLLQPMAGCARVAQCAQAVPTLLQAFFSAVTQVADGSLINQLALLLLGRSDSLYPAPGYAAGVHSVLSSQFLALCTLKPSLVVELARDLLEFLGSVNGLCSRASLVTSVVWAIGEYLSVTYDRRCTVEQINKFFEALEALLFEVTQCRPSAALPRCPPQVVTVLMTTLTKLASRSQDLIPRASLLLSKMRTLAHSPATSSTHSEEGAEAIRTRATELLTLLKMPSVAQFVLTPSTEVCSPRYHRDANTALPLALRTVSRLVEREAGLMPG
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As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair. Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11. By SDS-PAGE, 2 isoforms have been observed, the shorter seems to be predominantly nuclear and the longer is mostly cytoplasmic. The disease is caused by variants affecting the gene represented in this entry. Extended N-terminus.
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Q8C488
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MFSAGAESLLHQAREIQDEELRRFCSRVTKLLQEAPGPATVDALQRLFLIVSATKYPRRLEKMCVDLLQTTLCLPASPEQLQVLCAAILREMSPFNDLALSCDHTPNTRQLSLVASVLLAQGDRKGEIRCVSQRIFKILENRQPEGPSVRPLLPILSKVIGLAPGILMEDQTNLLSKRLVDWLRYASIQQGLPYSGGFFSTPRTRQPGPITEVDGAVASDFFTVLSTGQHFTEDQWVNMQAFSMLRKWLLHSGPEDPCSPDADDKSELEGSTLSVLSAASTASRLLPPRERLREVAFEYCQRLLEQSNRRALRKGDSDLQKACLVEAVSVLDVLCRQDPSFLYRTLSCLKALHRRLGEDPGSERALVPLAQFFLNHGEAAAMDAEAVYGQLLRGLPSERFHSPTLAFEVIHFCTHNLALFDSHFLSLLRLSFPSLFKFLAWNSPPLTAEFVVLLPALVDAGTAVEMLHALLDLPCLTAALDLQLRSTQTPSERLLWDISLRVPSCLEAFQDPQFQGLFRHLLRTKASGSTERLTPLHQVLKPMASCARVTQCAEAVPVLLQAFFSAVTQTADGALINQLALLLLERSDSLYPVPQYEARVHGVLSSQLLVLCKLKPSLVVELSRELLEFVGSVSSIHSRASVFTCVVWAIGEYLSVTWDKRCTAEQINKFFEALEALLFEVTQSRPLADLPCCPPEVVTALMTTLTKLASRSQDLIPRVSLFLSKMRTLAQNPATSSVHSEEGAESIRTRASELLTLLKMPSVAQFVFTPPAGVCQPRYHRDTNVALPLALRTVSRLVEKEAGLLPG
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As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11 (By similarity). Truncated N-terminus.
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P82964
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XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS
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Strong antimicrobial activity against P.immobilis and M.luteus, less active against E.coli D22. On the 2D-gel the determined MW is: 6.5 kDa. To bovine bactenecin 7.
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O57523
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MKFLALALTILLAAGTQAFPMQADAPSQLEHVKAALSMYIAQVKLTAQRSIDLLDDTEYKEYKMQLTQSLDNLQQYADATSQSLAPYSEAFGTQLTDATAAVRAEVMKDVEELRSQLEPKRAELKEVLDKHIDEYRKKLEPLIKEHIELRRTEMEAFRAKMEPIVEELRAKVAINVEETKTKLMPIVEIVRAKLTERLEELRTLAAPYAEEYKEQMIKAVGEVREKVSPLSEDFKGQVGPAAEQAKQKLLAFYETISQAMKA
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). Belongs to the apolipoprotein A1/A4/E family.
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O57524
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MQFLALALTILLAAATQAVPMQADAPSQLEHVKVAMMEYMAQVKETAQRSIDHLDDTEYKEYKVQLSQSLDNLQQYAQTASESLAPYSEAIGVQLTEATAAVRAEVMKDVEELRSQLEPKRAELKEVLDKHIDEYRKRLEPLIKDIVEQRRTELEAFRVKIEPVVEEMRAKVSANVEETKAKLMPIVETVRAKLTERLEELRTLASPYAEEYKEQMVKAVGEVREKVVPLTTDFKGQLGPAAEQAKEKLMALYETISQAMKA
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). Belongs to the apolipoprotein A1/A4/E family.
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Q38934
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MKIYSRTVAVSLIVSFLLCFSAFAERNDGTFRVGLKKLKLDSKNRLAARVESKQEKPLRAYRLGDSGDADVVVLKNYLDAQYYGEIAIGTPPQKFTVVFDTGSSNLWVPSSKCYFSLACLLHPKYKSSRSSTYEKNGKAAAIHYGTGAIAGFFSNDAVTVGDLVVKDQEFIEATKEPGITFVVAKFDGILGLGFQEISVGKAAPVWYNMLKQGLIKEPVFSFWLNRNADEEEGGELVFGGVDPNHFKGKHTYVPVTQKGYWQFDMGDVLIGGAPTGFCESGCSAIADSGTSLLAGPTTIITMINHAIGAAGVVSQQCKTVVDQYGQTILDLLLSETQPKKICSQIGLCTFDGTRGVSMGIESVVDKENAKLSNGVGDAACSACEMAVVWIQSQLRQNMTQERILNYVNELCERLPSPMGESAVDCAQLSTMPTVSLTIGGKVFDLAPEEYVLKVGEGPVAQCISGFIALDVAPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAA
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Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity). Possesses aspartic protease activity in vitro. Optimum pH is 5.0-6.0 with insulin B chain as substrate and at 37 degrees Celsius. Located in protein storage vacuoles (PSV) of the embryo. Expressed in roots, leaves, stems, petals, carpels, seed pods and dry seeds. By light and during senescence. Belongs to the peptidase A1 family.
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D6VQW6
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MSIPADIASLISDKYKSAFDNGNLKFIQTETTKTKDPKTSMPYLISHMPSLIEKPERGQTPEGEDPLGKPEEELTVIPEFGGADNKAYKLLLNKFPVIPEHTLLVTNEYQHQTDALTPTDLLTAYKLLCALDNEESDKRHMVFYNSGPASGSSLDHKHLQILQMPEKFVTFQDRLCNGKEHFLPTFNTEPLQDAKVSFAHFVLPMPESEETVDEDLLAMCYISILQRALTFFQDWLNENPELKKSYNLMLTKEWICVVPRSKAFSDEMKIGFNSTGYCGMILTKNDEVFSKITEKPELINDILLECGFPNTSGQKPNEYNY
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Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP. ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate + phosphate ADP + H(+) + sulfate = adenosine 5'-phosphosulfate + phosphate kcat is 81.2 sec(-1) with Ap4A as substrate. Optimum pH is 7.5. Monomer. The N-terminus is blocked. Inactivation of both APA1 and APA2 promotes a great increase in the cellular concentration of bis(5'-nuceleosidyl) tetraphosphate nucleotides. Present with 19600 molecules/cell in log phase SD medium. Belongs to the ATP adenylyltransferase family.
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O04593
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MGVYSRAVAFSVFVSFLLFFTAYSKRNDGTFRVGLKKLKLDPNNRLATRFGSKQEEALRSSLRSYNNNLGGDSGDADIVPLKNYLDAQYYGEIAIGTPPQKFTVIFDTGSSNLWVPSGKCFFSLSCYFHAKYKSSRSSTYKKSGKRAAIHYGSGSISGFFSYDAVTVGDLVVKDQEFIETTSEPGLTFLVAKFDGLLGLGFQEIAVGNATPVWYNMLKQGLIKRPVFSFWLNRDPKSEEGGEIVFGGVDPKHFRGEHTFVPVTQRGYWQFDMGEVLIAGESTGYCGSGCSAIADSGTSLLAGPTAVVAMINKAIGASGVVSQQCKTVVDQYGQTILDLLLAETQPKKICSQIGLCAYDGTHGVSMGIESVVDKENTRSSSGLRDAGCPACEMAVVWIQSQLRQNMTQERIVNYINEICERMPSPNGESAVDCSQLSKMPTVSFTIGGKVFDLAPEEYVLKIGEGPVAQCISGFTALDIPPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAV
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Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles. Expressed in seed pods and dry seeds. Belongs to the peptidase A1 family.
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P49348
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MFPSNLREIVEATYEKAVANGHVKFTESSSKKLKDVDAGISYQVTFAPSLQSKPERLPIAIDENGAPIPKKDPFAEPEPELTILDDCAGDYKLLLNKYPVAANHLILVTKKYLLQTAPLSPKDLLTTYKLLQELDDEDEMLRHLAFYNCGPNSGSSQDHKHLQILPLPYKFVPYQDKLCSGKEHFIPNAKTEPLQDAKIPFAHYAVPLPEDPEKVDEDLLAMTFVSLLQRTLSMFQDWEGSNAEKSNDDEASIPAYNVLMTKEWLCLVPRSKAFAETPSIGFNATGYAGLVLVKWDETLKVLNENPSAVTKLLLECSFPSTAGAKPTEYHY
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Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP. ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate + phosphate ADP + H(+) + sulfate = adenosine 5'-phosphosulfate + phosphate Monomer. Belongs to the ATP adenylyltransferase family.
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D6VTF1
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MIEENLKQKIHDKFVAAKKNGHLKVTHAESKKLKDPQTTTQYWVTFAPSLALKPDANKNSDSKAEDPFANPDEELVVTEDLNGDGEYKLLLNKFPVVPEHSLLVTSEFKDQRSALTPSDLMTAYNVLCSLQGDKDDDVTCERYLVFYNCGPHSGSSQDHKHLQIMQMPEKFIPFQDVLCNGKDHFLPTFNAEPLQDDKVSFAHFVLPLPESSDQVDEDLLAMCYVSLMQRALTFFQDWTNESPELTKSYNVLLTKKWICVVPRSHAKSGPPLMLNINSTGYCGMILVKDREKLENLTEDPHLVDKSLLQCGFPNTAGQKPTEYHY
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Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates, but prefers A-containing substrates. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP. ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate + phosphate ADP + H(+) + sulfate = adenosine 5'-phosphosulfate + phosphate kcat is 93.8 sec(-1) with Ap4A as substrate. Optimum pH is 7.5. Monomer. Inactivation of both APA1 and APA2 promotes a great increase in the cellular concentration of bis(5'-nuceleosidyl) tetraphosphate nucleotides. Present with 1770 molecules/cell in log phase SD medium. Belongs to the ATP adenylyltransferase family.
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Q9XEC4
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MGTRFQSFLLVFLLSCLILISTASCERNGDGTIRIGLKKRKLDRSNRLASQLFLKNRGSHWSPKHYFRLNDENADMVPLKNYLDAQYYGDITIGTPPQKFTVIFDTGSSNLWIPSTKCYLSVACYFHSKYKASQSSSYRKNGKPASIRYGTGAISGYFSNDDVKVGDIVVKEQEFIEATSEPGITFLLAKFDGILGLGFKEISVGNSTPVWYNMVEKGLVKEPIFSFWLNRNPKDPEGGEIVFGGVDPKHFKGEHTFVPVTHKGYWQFDMGDLQIAGKPTGYCAKGCSAIADSGTSLLTGPSTVITMINHAIGAQGIVSRECKAVVDQYGKTMLNSLLAQEDPKKVCSQIGVCAYDGTQSVSMGIQSVVDDGTSGLLNQAMCSACEMAAVWMESELTQNQTQERILAYAAELCDHIPTQNQQSAVDCGRVSSMPIVTFSIGGRSFDLTPQDYIFKIGEGVESQCTSGFTAMDIAPPRGPLWILGDIFMGPYHTVFDYGKGRVGFAKAA
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Involved in the processing and degradation of storage proteins. A number of isoforms are produced. According to EST sequences. Expressed in petals, carpels and seed pods. Belongs to the peptidase A1 family.
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Q9GL23
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ILKKDNYSYISFYNALIHEGYKDLAALLHSGIPVISSSNGGKDSVGGITS
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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase 9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex. Interacts with APIP (By similarity). Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain) (By similarity). Interacts with CIAO2A (By similarity). The CARD domain mediates interaction with APIP. The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization (By similarity). Physiological concentrations of calcium ions negatively affect the assembly of apoptosome by inhibiting nucleotide exchange in the monomeric form.
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Q9I9H8
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MEERARSRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLASLLHSDLPLLSPEGEKSFADGVSPSVQAILSVGGVPQRPVVFVSRPPLLNLIREMLYQLRDTPGWVTVFGMAGSGKSVMAAEVVRDRSLIKECFPDGVHWLSVGQCERADLLVRMQSLCFRLEQCQSSDTSQRPPSTVEEAKERLRFLMLRRFPRSLLILDDVWDSSSLRSFDIQCRVLLTTRNRALTDSVSGVRYEVPVENGLDEEKALEILALYVNGKMHKLPEQARSIVSECKGSPLVVSLIGALLREFPDRWSYYLRQLQQKQFKRIRKSSSYDYEALDQAMDASLQVLEAEHQELYRDLSVMQKDIKVPAKVLSVLWGLELEEVEDVLQEFVNKSLLFRDCNQRPYRYYLHDLQLDFLAEQNRDQIAELHKKMVRQYQRFYSKRPPDSADKDSLYWYQFIPYHMAKAGLSKELYSLMFSLDWVKEKARIMGSAHLINDYVEYGEILDKENSEVRVQFQEFLSLNGHHLEQRPFPDVVQLALSQPDRSEVYRQALMQAQKRASRGQIYLNWVNKNIEEGLSRLVMHPHQGAVYYACFSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIREFEVEHEEQINHCQFTNTGRRVLLATCSNDKFTNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFEVSSANEWKSIDVDSFFPESDEEIKAMVKCSTWSADGSQIICAARNTVFVFDVETSDLLLKLKTSRLSTIQFCHACPNSSLLAVALSHYTVELWNFESSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWETDRVHTSSAVALKRDTDVLSSHSDATIIAPDSSNRLQVLSGSTGAVVLESEELSSRIRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECMVLQGHMEPVRKFHLLSSSSSPHLFSWSFDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRDTKDSMNSYHAGWVTDLHFSPDNRVLVSTAGYIKWWSVESGEALQTFYTMGGNLKKIHVSPDFSTFITVDSIGILYILKRLEGEGT
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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). Monomer. Oligomerizes upon binding of cytochrome c and dATP (By similarity).
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Q9UNC9
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MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE
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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis. Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex. Pro-caspase-3 is recruited into the Apaf-1-pro-caspase-9 complex via interaction with pro-caspase-9. Interacts with APIP. Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain). Interacts with CIAO2A (PubMed:25716227). Ubiquitous. Highest levels of expression in adult spleen and peripheral blood leukocytes, and in fetal brain, kidney and lung. Isoform 1 is expressed in heart, kidney and liver. By E2F and p53/TP53 in apoptotic neurons (PubMed:11389439). Translation is inhibited by HNRPA1, which binds to the IRES of APAF1 mRNAs (PubMed:31498791). The CARD domain mediates interaction with APIP. The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization (By similarity). Physiological concentrations of calcium ions negatively affect the assembly of apoptosome by inhibiting nucleotide exchange in the monomeric form.
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A2RRK8
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MDAKARNCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAALLQSGLPLVSSSSGKDTDGGITSFVRTVLCEGGVPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCMRLDQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKHVVPVESGLGREKGLEILSLFVNMKKEDLPAEAHSIIKECKGSPLVVSLIGALLRDFPNRWAYYLRQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCVLWDLETEEVEDILQEFVNKSLLFCNRNGKSFCYYLHDLQVDFLTEKNRSQLQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHILDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQEGDTGRLYLEWINKKTIKNLSRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFTNKSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSINVKRFFLSSEDPPEDVEVIVKCCSWSADGDKIIVAAKNKVLLFDIHTSGLLAEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETKKVCKNSAIVLKQEIDVVFQENETMVLAVDNIRGLQLIAGKTGQIDYLPEAQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVFLQAHQETVKDFRLLQDSRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPISVEEGTATHGGWVTDVCFSPDSKTLVSAGGYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQVLE
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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex (By similarity). Interacts with UACA. It may also interact with Bcl-XL. Interacts with APIP. Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain) (By similarity). Interacts with CIAO2A (By similarity). Highly expressed in lung and spleen, weakly in brain and kidney and not detectable in liver. High levels in embryonic brain and liver from 11.5 dpc to 17.5 dpc. The CARD domain mediates interaction with APIP. The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization. Physiological concentrations of calcium ions negatively affect the assembly of apoptosome by inhibiting nucleotide exchange in the monomeric form. Major isoform.
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Q9EPV5
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MDAKARNCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGLLHSGLPLVSSSSGKDTDGGNTSFVRTVLCEGGVPQRPVIFVTRKKLVSAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHALLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCTRLGQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKYVIPVESGLGKEKGLEILSLFVNMKKEDLPVEAHSIIKECKGSPLVVSLVGALLRDFPNRWAYYLRQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCVLWDLETEEVEDILQEFVNKSLLFCNRNGKSFCYYLHDLQVDFLTEKNRSQLQDLHRKMVTQFQRYHQPHTLSPGQEDCMYWYNFLAYHMASAGMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDTGRLYLEWINKKTIKNLSRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHTYEEHSEQVNCCHFTNKSNHLLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWDVRSANEKKSINVKRFFLSSEDPPEDVEVIVKCCSWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETRKVCKNSAIVLKQEIDVVFQENEMMVLAVDNIRGLQLIAGKTGQIDYLPEAQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVFLQAHQETVKDFRLLRDSRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLCAPISIEEGTATHGGWVTDVCFSPDRKMLVSAGGYLKWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQVLE
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Regulates programmed cell death; necessary for normal brain development. Participates with pro-caspase-9 (Apaf-3) in the cytochrome c-dependent activation of caspase-3, leading to apoptosis. This activation requires ATP (By similarity). Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains. Interacts with UACA. Interacts with APIP (By similarity). Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain) (By similarity). Interacts with CIAO2A (By similarity). Highly expressed in brain cortex in embryos (E17) and newborn rats up to day 7. Very low expression thereafter. By brain injury. The CARD domain mediates interaction with APIP. The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization (By similarity). Physiological concentrations of calcium ions negatively affect the assembly of apoptosome by inhibiting nucleotide exchange in the monomeric form.
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Q4K4X3
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MATYAVGDLQGCLEPLQCLLEQVAFDPARDRLWLVGDLVNRGPQSLETLRYLYSIRDSLVCVLGNHDLHLLAVWRNVERLKKSDTLREILEAPDCEELLQWLRQQKLMHYDEARNIAMVHAGIAPQWSLKKAQKCAAEVEEALRDDNLFDPFLDGMYGNDPAKWDSDLKGVTRLRVITNYFTRMRFCTSDGKLDLKSKEGLDTAPPGYAPWFSHKERKTRDLKIIFGHWAALEGHCNEPGIFALDSGCVWGGAMTLLNVDSGVRLTCDCDAQGRTAALSPDPLPAPAKR
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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C3K329
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MATYAVGDLQGCLEPLKCLLDRVAFDPAKDRLWLVGDVVNRGPESLETLRYLYSLRDSLVCVLGNHDLHLLAASNTIERLKKGDTLREILEAPDRAELLDWLRRQKIMHYDQGRNMALVHAGIPPQWTLKKALKCAAEVESALADDTLYTAYLDGMYGNDPVKWDNDLTGVARLRVITNYFTRMRFCTAEGKLDLKSKEGADTALPGYKPWFAHKERKTRDTKIVFGHWAALEGKCDEPGVFALDTGCVWGGAMTLMNIDTGERYSCQCESPLPVTLPATAKP
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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A4XZJ6
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MAVYAVGDLQGCLQPLKCLLEQVAFDPAQDQLWLVGDLVNRGPQSLETLRFLYSIRHALTCVLGNHDLHLLAVAHNIERLKKGDTLREILDAPDRDDLLDWLRLQKLVHHDAERQITLVHAGIPPQWSLAKALKRAAEVEEVLRDDARLPLFLDGMYGNEPAKWNKDLHGVTRLRVITNYFTRMRFCTADGTLDLKSKEGVGSAPPGFAPWFSHPQRKMRGEKIIFGHWAALDGNCQEPGLYALDTGCVWGGAMTLLNVDSGALHRCTCPKQ
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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A5VXJ3
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MATYAVGDLQGCLQPLKCLLDRVSFNPAVDRLWLVGDLVNRGPESLETLRFLYSIRHSLVCVLGNHDLHLLAAWHNVERLKKSDTLREIIEAPDADQLFDWLRQQKLLHYDEPRGIALVHAGIPPQWTLGKALELAAEVEEVLRDDTRLQLYLDGMYGNEPNKWSKNLAGVERLRVITNYFTRMRFCTADGKLDLKSKEGLGSAPKGYKAWYAHKDRRSRHVKIIFGHWAALQGEVTEPDVIALDTGCVWGGAMTLYNVDSGEYHRCDCADDGTLRQPAQPTTLNDHT
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q3K5T0
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MATYAVGDLQGCLEPLKCLLQQVAFDPALDRLWLVGDLVNRGPQSLETLRFLYGMRESLVCVLGNHDLHLLAAAKNIERLKKSDTLREILEAPDCAELMEWLRQQKLMHYDEQREVAMVHAGIPPQWSLRKALKYAEEVETALRDDNLLPPFLDGMYGNEPAKWDSDLKGVTRLRVITNYFTRMRFCTAEGKLDLKSKEGLDTAPPGYKPWFQHKERKTRGLRIIFGHWAALEGNVHEPGICALDTGCVWGGSLTLMNVDSGERLSCKCDEHGAALPTVAPLITESSPVSAPR
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B0KJ91
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MATYAVGDLQGCLQPLKCLLERVSFNPAVDRLWLVGDLVNRGPESLETLRFLYSIRQSLVCVLGNHDLHLLAAWHNVERLKKSDTLREIIEAPDADPLFDWLRQQKLLHYDEARGIAMAHAGIPPQWTLGQALGYAAEVEEALRDDSRLKLYLDGMYGNEPNKWSKNLTGVERLRVITNYLTRMRFCTAEGKLDLKSKEGLGTAPKGYKPWFAHKGRRSRHVTIIFGHWAALEGRVDEPGIIALDTGCVWGGAMTLYNVDSGEYHRCDCADDGTLRQPAQPTTLNDHT
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q88QT8
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MATYAVGDLQGCLQPLKCLLDRVSFNPAVDRLWLVGDLVNRGPESLETLRFLYSIRHSLVCVLGNHDLHLLAAWHNVERLKKSDTLREIIEAPDADQLFDWLRQQKLLHYDEPRGIALVHAGIPPQWTLGKALELAAEVEEVLRDDTRLQLYLDGMYGNEPNKWSKNLAGVERLRVITNYFTRMRFCTADGKLDLKSKEGLGSAPKGYKAWYAHKDRRSRHVKIIFGHWAALQGEVTEPDVIALDTGCVWGGAMTLYNVDSGEYHRCDCADDGTLRQPAQPTTLNDHT
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B1JE09
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MATYAVGDLQGCLQPLKCLLERVKFDPAVDRLWLVGDLVNRGPESLQTLRYLYSIRHSLTCVLGNHDLHLLAAWQNVERLKKSDTLREIIEAPDADQLLDWLRQQKLLHYDEPRGIALVHAGIPPQWTLGKALELAGEVEEVLRDDERLKLYLDGMYGNEPNKWSKNLGGVERLRVITNYLTRMRFCTGTGKLDLKSKEGLGTAPKGYKPWFAHKDRRSRHVKIIFGHWAALEGRVDEPGIIALDTGCVWGGTMTLYNVDSGEYLRCDCADDGTLRPPAQPTKLIDQP
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q88A48
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MAVYAVGDLQGCLEPLQCLLEHVRFDPVQDRLWLVGDLVNRGPQSLQTLRYLYSIRESLVCVLGNHDLHLLAVARKNELLKKGDTLREILEAPDRDELLRWVRQQKLMHYDAERNIAMVHAGIAPQWSVKKALKQAAEVEHALQDDQLYGAFLDGMYGNEPAKWNNDLQGVTRLRVITNYFTRMRFCTSDGKLDLKSKEGVGTAIPGYAPWFSHQNRKTRDVKIIFGHWAALEGRCDEPGVFALDSGCVWGGAMTLLNVDTLERHQCNCDAVGNAATGIIASAQPGNAHIQQIPAQEPKQ
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q4ZMG3
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MAVYAVGDLQGCLEPLQCLLEHVHFNPEQDRLWLVGDLVNRGPQSLETLRYLYSLRESLVCVLGNHDLHLLAVARKKELLKKGDTLLEILEAPDRDDLLGWVRRQKLMHYDAQRNVAMVHAGIAPQWTLKKALKHAAEVEHALQDEQLYGAFLDGMYGNEPTRWDNDLQGVTRLRVITNYFTRMRFCTSDGKLDLKSKEGVGTAIPGYAPWFSHQSRKTRDVKIIFGHWAALEGRCDEPDVFALDSGCVWGGSMTLLNVDTLERHQCNCDAMGNAADGLVTRVQPGATPLP
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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A4VHH8
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MTTYAVGDLQGCLEPLTCLLERVDFSPSRDCLWLAGDLVNRGPQSLEALRFVRDLESSAITVLGNHDLHLLAVAHNIERMRKSDTLQAILDAPDRADLIDWLRQQKLIHYDAERHTAMVHAGIPPQWSLEKALRRAAEVEQALQDDALLLPFLDGMYGNQPAKWNKELHGVPRLRLITNYFTRMRFCKADGTLDLDAKEGADSAPAGYAPWFSHASRKTRNVKLIFGHWAALEGQCDEPNVFALDTGCVWGNAMTLMNLDSGEMHRCECEHGKPA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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A1STS0
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MATYIVGDVHGCFDELQALLELAQFKKNKDQLWITGDLVGRGPKSLETLRFVKSLGDSAKIVLGNHDLHLLAIHQGIHSDKESDKLSALLNAPDCDELLTWLRFQPLFRRHPEFNFVMVHAGISPQWTIQQAQGYAQEVQNILQGNEFKKLLKNMYGNHPASWNDSSQGIKRLRFIINALTRMRYCLLDGSLEFYSKLAPEQTDSTIIKPWFEINTLDQSSDIIFGHWAALLGTGTKQGIYALDTGCVWGNSLSMLRWQDKKMFSFACQRQRVHSK
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q8Y1K9
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MTVASIPPHAIGDLQGCCSPLQTLLTALPANAPLRFVGDLVNRGPDSLGTLRRVIMLCEGGRARAVLGNHDIHLLAVAAGVRKLGKRDTLDDILGAPDCDALIHWLRHQPLAIFENGFLMVHAGVLPQWTTGDVLELAGAVERELRSPHWKTFLTDAFGNQPAKWSSDLIGIDRLRLTINALTRLRFCTPDGAMEFETTDADGAPDGHVPWFDVPGRRTRGTPIAFGHWSTRGLVMRDDLLGLDTGCVWGGKLTAARMTLAPAGREVIQVACEQAQDPLAHKK
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q21MT2
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MATYAVGDIQGCYRALKLLLKKVKFNADNDHLWVAGDLVNRGPESLKSLRYIKKLGPSATLVLGNHDLHLLAHAYGVRTLNPKDTLAPILTAKDSDELLEWLQAQPLLHYDAEFDAVLVHAGIPPIWSIENALNYALEVEQALSTTQTAAAFFVDMYGNQPDVWQPSLEGTARLRLITNYLTRMRFCSPTGKLELQTKNAPSLPPTGFAPWYTHKHNKWGNTKILFGHWAALMGETRSKQFIGLDTGCVWGGALTMMRLEDGQFFAVDCPC
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B5F769
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MATYLIGDVHGCYDELIALLQQVEFTPDTDTLWLTGDLVARGPGSLDVLRYVKSLGNSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLEGKGTPEGIYALDTGCCWGGELTCLRWEDKQYFVQPSNRQMDMGEGEAVNA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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A9MQG4
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MATYLIGDVHGCYDELIALLQQVEFTPETDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLDGKGTPDGIYALDTGCCWGGKLTCLRWEDKQYFVQPSNRQMDMGEGEAINA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q57TH2
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MATYLIGDVHGCYDELIALLQQVEFTPDTDTLWLTGDLVARGPGSLDMLRYVKSLGNSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLIMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLEGKGTPEGIYALDTGCCWGGELTCLRWEDKQYFVQPSNRQMDMGEGEAVNA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B5FI32
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MATYLIGDVHGCYDELIALLQQVEFTPDTDTLWLTGDLVARGPGSLDVLRYVKSLGNSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLEGKGTPEGIYALDTGCCWGGELTCLRWEDKQYFVQPSNRQMDMGEGEAVNA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B5R1S6
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MATYLIGDVHGCYDELIALLQQVEFTPDTDTLWLTGDLVARGPGSLDVLRYVKSLGNSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLEGKGTPEGIYALDTGCCWGGELTCLRWEDKQYFVQPSNRQMDMGEGEAVNA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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B5RGC0
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MATYLIGDVHGCYDELIALLQQVEFTPDTDTLWLTGDLVARGPGSLDVLRYVKSLGNSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQVDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELSGLARLRFITNAFTRMRYCFPNGQLDMYSKASPENAPAPLKPWFAIPGPVSEAYSIAFGHWASLEGKGTPEGIYALDTGCCWGGELTCLRWEDKQYFVQPSNRQMDMGEGEAVNA
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Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Belongs to the Ap4A hydrolase family.
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Q9SJ93
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MEALGSSDCNLEILETLSDDAIQEITESYDGFFTTVESLIAGTGDSLVEDEFVSHVYCLCKYGLDSLVRDHFLRSLEQAFEKGGASSFWQHFDAYSEKKHHNYGEEIQIVLCKALEEISIEKQYHEKCLSIVVHALQSFKEQSSDDRQNSDTERVHLFSRFQSMLSSTLMTTLPQHFPEILHWYFKERLEELSAIMDGDGIEEQEDDCMDLDEKLRYKNGEMDVDEGCSQGKRLGHDKLVKNIGKVVRDLRSIGFTSMAENAYASAIFLLLKAKVHDLAGDDYRTSVLESIKEWIQTVPLQFLNALLSYLGDSVSYGTTSSGLTSPLACCPSPSFSRVVTPSEGIVRWKLRLEYFAYETLQDLRIAKLFEIIVDYPESSPAIEDLKQCLEYTGQHSKLVESFISSLKYRLLTAGASTNDILHQYVSTIKALRAIDPAGVFLEAVGEPIRDYLRGRKDTIKCIVTMLTDGSGGNANGSGNPGDSLLEELMRDEESQENVGFDDDFHTDDKQAWINASRWEPDPVEADPLKGSLSQRKVDILGMLVDIIGSKEQLVNEYRVMLAEKLLNKTDYDIDTEIRTVELLKIHFGEASMQRCEIMLNDLIDSKRVNTNIKKASQTGAELRENELSVDTLTSTILSTNFWPPIQDEPLELPGPVDKLLSDYANRYHEIKTPRKLLWKKNLGTVKLELQFEDRAMQFTVSPTHAAIIMQFQEKKSWTYKDLAEVIGIPIDALNRRVNFWISKGVLRESTGANSNSSVLTLVESITDSGKNEGEELLTGEEEGETSIASVEDQLRKEMTIYEKFIMGMLTNFGSMALERIHNTLKMFCVADPSYDKSLQQLQSFLSGLVSEEKLEFRDGMYLLKK
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. Protein modification; protein ubiquitination. The APC/C is composed of at least 10 subunits. Interacts with APC8, APC11, CDC27A and CDC27B. Highly expressed in immature flowers. Expressed in stems, leaves and flowers. Gametophytic lethal phenotype. Belongs to the cullin family.
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Q8T129
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MFQNKEQTESILVWEKIVSIFSIPSQNEILNFKQKSPNNIDNNLKQLFNFVKLYKLESLVLDWYFESIKKYFKSTLSNEFWKFFNNVNLAELDSSTTSGRQLKFINHQFALSINLLHKVFSFFKSNLFLFYELLFKKESYNFNFLIKKLQDLLITNIMHTTNQQTKYFNTILFMFFERDFISFTKSFYHSKKQILKDEEENNNNSKDLEFNDQQQEEEEEEEENEEESKSYIIMEMSFEDSITDINIKEDSFMDLCKKLQDLNFIVISEEIFTQILFKKVFEYIETRCKGVFEKSFLKSILEWADQVIFKWLAMILLSSTTTTKINNYNDIINNNDDDNDDDDDDENKENSLKIFNQWKKRLEFSIYENYSQQRISELFDMIVQYPDSLPSLEDLSICFQKIPIEKTMITNLKRVLHNRLLHPGANTSDIITQYISTIHAMDIIDPSGMVMEKVGKPIREYLSQREDTIRCIISSFTEESNEIYQELCNYDPQDNGGDDDSNNSLLAFGNCDLYVDEGDNFSSIDDFKFWIPNKIDGSSTTISIGNAKANNNNKKKKKKDTISHLVNIYDGIDLFINEYRSMLSDRLLSVVDFDLDKEIKNIELLKLRFGDSVLFNCEIMIKDMVDSKRLNLQIKNSQGVNNNNNNNNNNNNELKEFETLILSQLFWPTLKGDEFKYPKSIEKKMQIYSKEYERIKTPRQLIWKQHLGLVDLDLEIGNNIQSFQVSPIHATLIMLFESDDGDDDDEKELTLEYLSKQLEISKDLVKKKLIFWLNNQIIKETSHETYKINNKEKEEQKQRQQQIENDDQDESSSDDDDDDNNIVVEEEEEEKSTSAKEKEEQMRVVESFIIGMLINFKTLPLERIHSMLTMFNSELYTSTIHELKAFLSKLVNEEKIELVGNDFKIKK
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: anapc1, anapc2, anapc3, anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26 and cdh1. Belongs to the cullin family.
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Q874R3
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MNDTDLSTFTGRSLLIDQLSSVTQGTPVLDFIDKLRIHFYTTIRQNLLKIDLKNICSLHDLTDQLSDFWLVYEQSVLESPILSPELDRILTCFRCLCRRYLPISVIESVLTEYLDQVLKVWLESKTNPCLDMEKFFQLCEKFKQLGLSSVLKERFVYVLQLHVGSLLTTRYAMSWEQSVYHEALEWIRTEFGVLVEHVFSLSNPAVLVQLDHLVSQILAHLRSDNILDIVLHYPNSLGAIEDLRLVARQKQQRQYLTETFVKDCTSSILTASSDSSYILLFYVSTIRCFVALDPPGVLLDKAAKPIRSFLNEREDAYKCLVSLLFVDGEKGLRSELSQIPTENIDSTTDRFDNYHWMPDPIDAAPDFKKPTDRDVVGSLISIFKSKEPLVKELQLLLADRLLQLTDYHYEVEAKNIEFLKYRFGETVLQMCSVMLNDIENSRFIDQSIHMENYVSKGLHVTILSRLFWPTLSVRYFHLPGPLKKELDAYAEEYRERKRKRELVFLPNLGSVELEIELEDRTLTLTVTPEQAAFISLFEETSTLHIEKAAELLDQPKEIVERHLKFWLHHRVLTDIGDDRYRVRETEAETATETVLDEIQGVSAVQSEAESSAAEMRVYWSFVVGMLTNLGALELERIHNMLTMFIPPPNGYTRTQSELREFLALMIKEEKLEFTGGAYKLK
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Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. The APC/C is composed of at least 13 subunits: apc1, apc2, nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and apc15. Belongs to the cullin family.
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Q7LGV7
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MSFQITPTRDLKVITDELQTLSSYIFHTNIVDDLNSLLTWMSPNDAKSNHQLRPPSLRIKNIIKVLFPNNATTSPYSMINTSQANNSIVNEGNTNKELQLQLFSTLKEFYIFQVRYHFFLHFNNINYLKDIQRWENYYEFPLRYVPIFDVNVNDWALELNSLRHYLLNRNIKFKNNLRTRLDKLIMDDDFDLADNLIQWLKSANGSLSSTELIVNALYSKINKFCEDNMSRVWNKRFMIMETFNKFINQYWSQFSKLVGCPEDDHELTTTVFNCFESNFLRIRTNEIFDICVLAYPDSKVTLLELRKIMKDFKDYTNIVTTFLSDFKKYILNPSVTTVDALLRYVKTIKAFLVLDPTGRCLHSITTFVKPYFQERKHLVNVLLYAMLDLPEEELKEKINFNVDMKALLSLVDTLHDSDINQDTNITKRDKNKKSPFLWNLKVKGKRELNKDLPIRHAMLYEHILNYYIAWVPEPNDMIPGNIKSSYIKTNLFEVLLDLFESREFFISEFRNLLTDRLFTLKFYTLDEKWTRCLKLIREKIVKFTETSHSNYITNGILGLLETTAPAADADQSNLNSIDVMLWDIKCSEELCRKMHEVAGLDPIIFPKFISLLYWKYNCDTQGSNDLAFHLPIDLERELQKYSDIYSQLKPGRKLQLCKDKGKVEIQLAFKDGRKLVLDVSLEQCSVINQFDSPNDEPICLSLEQLSESLNIAPPRLTHLLDFWIQKGVLLKENGTYSVIEHSEMDFDQAQKTAPMEIENSNYELHNDSEIERKYELTLQRSLPFIEGMLTNLGAMKLHKIHSFLKITVPKDWGYNRITLQQLEGYLNTLADEGRLKYIANGSYEIVKNGHKNS
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC2 interacts directly with APC11 thereby anchoring APC11 to the core complex. Present with 432 molecules/cell in log phase SD medium. Belongs to the cullin family.
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Q54J83
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MEEIMIQSIDESIHCGLIKNALFLSERLYASTANEDNLFKIAQIYYQMGKINQCLLILQQHPQITMIKNLYLLALSNYDLGNIQEAESSIIKCCIYFEKYFQPNNNNNNNNNNNNNNNNNNNNNNNNNKDKCNNSNKNNDSNNNSNSNNNENEYYGIYSDILCEFDDIVDINSISYGFDSPCSIGSVYYLMGLISKRKNQKEKAIKYLKKSVYTYPFLWVAFEQLCNICPDEIDISDLFSHTNLIHQINHLNQQQHQQHQQFQQYLSNSLNQNKVNNNNNNNNNNNNNINNNNSSNKNNEQTITSTVATGTTNITTNTIKPNNFIKPPYHPNHRVGLTPSSFYDSSIHITPINFKASIQQTNQQQQQQQQQQPQQPSQQNLQKYNNRYFVTPQTPLSHITPILSNRFSQNVVDPIPMVMDTPDSKGSQHPPSSNSQTPYTPSTPGVHHHQKQQPHQHKKSAPPSQMIKKSMSNEFDTPMSLDLKSPIFTTSTSSDVHGFTSSTSKQQQQQQQTKQQTTTTTTTTTSITDKEVLLTKTKKQVNFGKTEEFSLKSLSSSLSDDDYDEENHHYQQHHHLHHHNKSIDELELEEDDQLNITDNSVQPNFYEFDESSILDFNGGDLYEGLIELHKGQTQLLELFFILADSYRLLCLYLCKEAIESFKRLSEEQYRTGWVLTKVAKAYHELIDYKEARSIFQEVSQMEPYRLEGMELYSTLLWQMNEDAELSYIAHKYSEFDRLSPYSWVVVGNCFSLQRDHEAAIKLFRRAIQLDPDMTYAYTLCGHEYLANDELELALNAFRMAIRCDPRHYNAFYGIGLIYYRQEKYNLAEYHFRKALSINESSSVLCCYLGMTLQHNPNKIQDGIDMLYRSIEIQPKNTFAKFKLAAFLFANQQYHHAIDQLLEFKEIEPKETPIYILLGKCYKQLGELDKALDSLNTALDLDPKNSNYIRSLIDKLPLEDEDDNQDYFQLN
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: anapc1, anapc2, anapc3, anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26 and cdh1. Belongs to the APC3/CDC27 family.
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Q9US21
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MTDRLKCLIWYCIDNQNYDNSIFYSERLHAIEDSNESLYLLAYSHFLNLDYNIVYDLLDRVISHVPCTYLFARTSLILGRYKQGISAVEACRSNWRSIQPNINDSISSRGHPDASCMLDVLGTMYKKAGFLKKATDCFVEAVSINPYNFSAFQNLTAIGVPLDANNVFVIPPYLTAMKGFEKSQTNATASVPEPSFLKKSKESSSSSNKFSVSESIANSYSNSSISAFTKWFDRVDASELPGSEKERHQSLKLQSQSQTSKNLLAFNDAQKADSNNRDTSLKSHFVEPRTQALRPGARLTYKLREARSSKRGESTPQSFREEDNNLMELLKLFGKGVYLLAQYKLREALNCFQSLPIEQQNTPFVLAKLGITYFELVDYEKSEEVFQKLRDLSPSRVKDMEVFSTALWHLQKSVPLSYLAHETLETNPYSPESWCILANCFSLQREHSQALKCINRAIQLDPTFEYAYTLQGHEHSANEEYEKSKTSFRKAIRVNVRHYNAWYGLGMVYLKTGRNDQADFHFQRAAEINPNNSVLITCIGMIYERCKDYKKALDFYDRACKLDEKSSLARFKKAKVLILLHDHDKALVELEQLKAIAPDEANVHFLLGKIFKQMRKKNLALKHFTIAWNLDGKATHIIKESIENLDIPEENLLTETGEIYRNLET
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Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Interacts with spindle apparatus, chromosomes, or nuclear envelope, and interconnect nuclear and cytoskeletal functions in mitosis, so the elongation of the spindle in anaphase is blocked. The APC/C is composed of at least 13 subunits: apc1, apc2, nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and apc15. Interacts with apc10 and cut9. Belongs to the APC3/CDC27 family.
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O65418
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MSEMASDEEENIIPFQLQFDKPIPFQIKIAEWNPEKDLLAMVTEDSKILLHRFNWQRLWTISPGKPVTSLCWRPDGKAIAVGLEDGTISLHDVENGKLLRNLKPHDVAVVCLNWEEDGQSNTDESGNFSVYEDRTSRFFPPAPRPPKMPGLVAGDSSFMDDGEDSLAELSNTSFRKFNILCTGDRDGNICFSIFGIFQIGKINIHELSLPVPHLDEHASCKLFNASIYKVALSKDLCRLVVMCTGELKDCDIKPREEKINVQDLPGLHCLAMDTSIFWKRKYELHQVAQQASNIEDLTEVIRASLSVMNKQWADAMKTFHEKFHSLSTLIIDNGLESSPQEEFLSLLGGARISPALNQFLVNSLGEVGVKRVLKSVCGTGKELQQVVLDHLQPAAEIIGFRIGELRGLSRWRARYQGIGLDEMLLNEATENTGLLLVQVQRFMMVLSSVVQQFSNFFNWLVRSIKYLMQEPNDQLLSYNSELLVVFLKFLYDQDPVKDLLELSEAGDDIEIDLKTIGRVKELLQFGGFSECDFLQRTLAKEFQHMESSFKMAFQMPFTTISRKISCMKLLPLCPLQLSTTQTPTTIPMSLSFYKNELSDDTPCQSGYTDYISFQVPDETFPEISNCIGIAKGYKQNSNNEKNGYTSLEAVLLSVPNGYTCVDLSLYKDKELVLLLNKTNTDSEGSGEACMMVVQTGDLAFISISGSSSLNQWELEDLKGSIVNLEMENEKVRKVPHSVIAPLAVSASRGVACVFAERRRALVYILEEDEDEEISDEK
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication (By similarity). Protein modification; protein ubiquitination. The APC/C is composed of at least 10 subunits. Belongs to the APC4 family.
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Q54NI1
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MKDFVLLNDKILPNDVKCYSCCTTMDLIALVTKDDQIVIHRFLTWQKLFTINHMSTTINDNNTNNNNNNNNNNNNNNNDNNNDNDKSNKSIVSIQWSPNGKMISIGCEDGSIFIYNIENAKLINKSHNHKHPIHKLAWIKEVSQQRSQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNKNGSTKCNNNYVSPPLFLSQIKQNMNLFPSISYYFENSKEENIYLGGDIYDRPFDILICCDSIGVISLLAFGLFKIVTIDLLSLLKQKYSNTHFLIKPSKSLKILDITLTESLNKLSVMIETDNGLFLSVTIDTSILLEKRNEIHEISLQYFLLFQLQQSLDIHIKEITEKWKETQQQLSTKWVEFEKVLSDYGFSSSIEQELIDLLMCGVPSPPTNQFIVNNINIKKLKLTESNCNSIREILIKYILPSFLNIFHIITVLHNNSLENDGYKGLLDTNTVKNILDYCGSFGMRLQSLETLICGIESHYTSFFSWLYKVQCTLNEIQPDRKLSLPFNELSIMSLLKKGLKFDLLFSTSTLFSSSSSSSPSSPPSNNNSPTFSSSSSINNNNNNNNNELNQSGNIGFSNNNENLEFQYKDLKGNFHDLFKDFSSKIFETFNEITIVLPSLFKFENVIPFCLYDKNDTSVSHKFNCSLISHPNDTIYLSIYTTLSNSNRLFICKREDKLNWSFTCYQLNEKYSILDCKFYNNSSLMALVSEDIIKANQKKSTRKNTYLKQYQYKTDDNDDSDNREYIKLDVNIPQSTILLDLLDSFKSREIILKSRISPITFELSTSRKISATFIGKRRVALYDLAEDEEEEEEGEEEDICLVR
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: anapc1, anapc2, anapc3, anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26 and cdh1. Belongs to the APC4 family.
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Q9NSH6
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MLRFPTCFPSFRVVGEKQLPQEIIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTGKEVTCLAWRPDGKLLAFALADTKKIVLCDVEKPESLHSFSVEAPVSCMHWMEVTVESSVLTSFYNAEDESNLLLPKLPTLPKNYSNTSKIFSEENSDEIIKLLGDVRLNILVLGGSSGFIELYAYGMFKIARVTGIAGTCLALCLSSDLKSLSVVTEVSTNGASEVSYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKFVQEKNTTTSVQDEFMHLLLWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEEAITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTEDHVLPELNKMTQKDITFVAEFLTEHFNEAPDLYNRKGKYFNVERVGQYLKDEDDDLVSPPNTEGNQWYDFLQNSSHLKESPLLFPYYPRKSLHFVKRRMENIIDQCLQKPADVIGKSMNQAICIPLYRDTRSEDSTRRLFKFPFLWNNKTSNLHYLLFTILEDSLYKMCILRRHTDISQSVSNGLIAIKFGSFTYATTEKVRRSIYSCLDAQFYDDETVTVVLKDTVGREGRDRLLVQLPLSLVYNSEDSAEYQFTGTYSTRLDEQCSAIPTRTMHFEKHWRLLESMKAQYVAGNGFRKVSCVLSSNLRHVRVFEMDIDDEWELDESSDEEEEASNKPVKIKEEVLSESEAENQQAGAAALAPEIVIKVEKLDPELDS
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Protein modification; protein ubiquitination. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:25043029, PubMed:27259151, PubMed:9469815, PubMed:26083744). In the context of the APC/C complex, directly interacts with UBE2S (PubMed:27259151). Belongs to the APC4 family.
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Q9CZZ0
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MLRFPTCFPSFRVVGEKQLPQEIIFLAWSPKRDLIALANTTGEVLLHRLASFHRVWSFPPNESTGKEVTCLAWRPDGKLLAFALADTKKIILCDVEKPESLHSFSVEAPVSCMHWTEVTVESSVLTSFYNAEDESNLLLPKLPTLPKNYNSTSKIFSEENSDEIIKLLGDVRLNILVLGGSSGFIELYAYGMFKIARVTGIAGTCIALCLSSDLKSLSVVTEVSSGGESEVSYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKFVQEKPTTTSVQDEFMHLLLWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEDAITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTEDHVLPELNKMTQKDITFVAEFLTEHFNEAPDLYNRKGKYFNVERVGQYLKDEDDDLVSPPNTEGNQWYDFLQNSTHLKESPLLFPYYPRKSLHFVKRRMENVIDQCLQKPADVIGRSMNQAICIPLYKDARSMDCARRLLKFPFLWNNKTSNLHYLLFTILEDSVYKMCILRRHTDISQSVSNGLIGIKFGSFTSASADKVRRSSYSCLDAQFYDDETVTVILKDSMGREGRDRILVQLSLSLVYNSEDSDEYEFTGSYSTRLDEQGSIIPTRTMHFEKHWRLLESMRAQYVAGNGLRKVSCVLSSNLRHVRVFEMDIDDEWEIDESSDDEEEAGGKPVKIKEEVLSESETEAHQDAAALDPDVVIKVEKLDPELDS
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Protein modification; protein ubiquitination. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. In the context of the APC/C complex, directly interacts with UBE2S. Belongs to the APC4 family.
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Q5RAQ5
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MLRFPTCFPSFRVVGEKQLPQEIIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTGKEVTCLAWRPDGKLLAFALADTKKIVLCDVEKPGSLHSFSVEAPVSCMHWMEVTVESSVLTSFYNAEDESNLLLPKLPTLPKNYSSTSKIFSEENSDEIIKLLGDVRLNILVLGGSSGFIELYAYGMFKIARVTGIAGTCLALCLSSDLKSLSVVTEVSTNGASEVSYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKFVQEKNTTTSVQDEFMHLLLWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGLASWKQKYEPLGLDAAGIEEAITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTEDHVLPELNKMTQKDITFVAEFLTEHFNEAPDLYNRKGKYFNVERVGQYLKDEDDDLVSPPNTEGNQWYDFLQNSSHLKESPLLFPYYPRKSLHFVKRRMENIIDQCLQKPADVIGKSMNQAICIPLYRDTRSEDSIRRLFKFPFLWNNKTSNLHYLLFTILEDSLYKMCILRRHTDISQSVSNGLIAIKFGSFTYATTEKVRRSIYSCLDAQFYDDETVTVVLKDTVGREGRDRLLVQLPLSLVYNSEDSAEYQFTGTYSTRLDEQCSAIPTRTMHFEKHWRLLESMKAQYVAGNGFRKVSCVLSSNLRHVRVFEMDIDDEWELDESSDEEEEASNKPVKIKEEVLSESEAENQQAGAAALAPEIVIKVEKLDPELDSQSSLPLLCV
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Protein modification; protein ubiquitination. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. In the context of the APC/C complex, directly interacts with UBE2S. Belongs to the APC4 family.
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Q9P545
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MVSKSFKYPKKHKFEWINETNRVERVGSGLKRVILCPSMELIAILTCSNHLICCRSNSQRIWDVDFHDLEATELCWNHDGNLIVVGFKNGELKIIDSSTGHLVEQRPASRDLAVLMITWAMQETIVNEKRNDFLFDATAYMPLLGTLPSSAKEERIFSSKAIAQFFEPRKREGENNKKVELLSILDERGIRYINMFSSYKIGESDSLKSALNLGVPISHSITNDLAYHVLICKGGTNISLKTLYMPLLKNDLGSIVDIATMSTRMQHLVRYLEEVLNAMYEEFDNVFKSEASFIKTFDALVSKYSDTTFFSLQLELYQFIMNGIPSDLLKEWINERVGDRVLKNWERAMVNSYTSLIIFCQEFVIPACERLTVLLSSARGKSIWGHMKGNTLLDAKLVEDCLATLGYLQNNVFSFLNCLFEEKKYMKHFISWLNYAIVEFNTSEPSSIPPQEIIEHINETVIYIRHSLFRSKLTSYFMGTKPLQLRDPDYYSLKDFANQDDSNSVDDFVSFKTLKESLRDSFNVIFSYPSLTCQKQWLKTGDLVLFEGTDWNVSSLIPKSCNEKNQLFSLFFRKDTPNIFLIISQLMENTMLPVSGCHFGLDYAELLGSSLLDFQPATVLDMKLLNGSSILILGKLKEKCFLCEICLADVPLTFFEHQQKNSYLDAISHLPFIPLNSCLWLHEFEKDFLPSTLEYALSENSDYGVLISRESSRYRLFSF
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Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates. The APC/C is composed of at least 13 subunits: apc1, apc2, nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and apc15. Interacts with apc1 and dim1.
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D6VSA3
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MSSPINDYFIDYNPLFPIFATRIAKGLAIYRVSDHARLAVIPIRNINLVANYDWDTTTGKFLSIFFKDGTIRIHDIFKDGRLVSFLRIPSTKISKGIWDRIPLRYEPNNRDFACNIIDDLPKLIRFVKDSKRINIVPYTQPNSLWRGPDEDDLDSNEKLDVHVVFNEGNDKITVFFNGDYAVFLSVDNIENENSLKSIIKVQDGFYQCFYEDGTVQTLNLGPLLQSKSSVNLLNYIMVIKELIGYMLTHLEFINRELATPYLDFVKRLCDEAYGYGKLKSELEALFLLGEISCDLEDWLCNSVGEKNFKRWKYLGCEAYQKTVQILTLIFVPACERIIIYVEKLRAILQAFSIQNKLSYTSDLTAVEVLLKSSQKLLTMTLNSIIGLGRDETLFEKFFIWFNDRLHEALDEDYKLKFQFEDDLYFGYDLLSYFDRILSKKGTEPSSIIDVKLYRDLINSMSDMEKDIAQSNVNSHIQQHILVDLKTDVFAQKYPSSQINLLDAIKLPKHNYIVYLIQVTKHNSAQEPFSEENKKKLYIGTLKDENLGIISKESSVKIPALFKSYRLSSTRFVPNRVHSLLRDIGLSDSNYHSSHVTDYRGENYENEEDDGTIAIPAYIRENRENDDFIACTAKVSVDGRSASLVFPKEKQNV
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. Present with 1332 molecules/cell in log phase SD medium.
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Q68FI4
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MAKNTVSARFRKVDVDEYDENKFVDEEEAGEGQQGPDEGEVDSAIRGGNMMGALQAALKNPPINTKNQSAKDRAENLVLKVLISFKANEIEKAVQSLDKNSTDLLMKYIYKGFESPSDNSSAVLLQWHEKALAVAGVGSIVRVLTARKTV
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Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:17178911). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:17178911). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (By similarity). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity). Component of the Arp2/3 complex composed of actr2/arp2, actr3/arp3, arpc1 (arpc1a or arpc1b), arpc2, arpc3, arpc4 and arpc5. Belongs to the ARPC5 family.
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Q6DE18
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MAKNTLSSRFRKVDIDEYDENKFVDDQLQEEPAEPQGPDEAEVDSLIRQGELLRAFQSALRNSPVNSKNQVAKERTQAIVLKVLTSFKSNEIEKAVNTLDPNGIDLLMKYIYKGFEKPTENSSAILLQWHEKAFVIGGLGSIVRVLTSRKTV
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Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (By similarity). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity). Component of the Arp2/3 complex composed of actr2/arp2, actr3/arp3, arpc1 (arpc1a or arpc1b), arpc2, arpc3, arpc4 and arpc5. Belongs to the ARPC5 family.
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Q641B9
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MAKNTVSARFRKVDVDEYDENKFVDEEEAGEGQQGPDEGEVDSAIRGGNMMGALQAVLKNPPINTKNQSAKDQAEHLVLKVLISFKANEIEKAVQSLDKNSMDLLMKYIYKGFESPSDNSSAVLLQWHEKALAVAGVGSIVRVLTARKTV
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Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (By similarity). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity). Component of the Arp2/3 complex composed of actr2/arp2, actr3/arp3, arpc1 (arpc1a or arpc1b), arpc2, arpc3, arpc4 and arpc5. Belongs to the ARPC5 family.
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Q9SHK3
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MAGLTRTAGAFAVTPHKISVCILLQIYAPSAQMSLPFPFSSVAQHNRLGLYLLSLTKSCDDIFEPKLEKLINQLREVGEEMDAWLTDHLTNRFSSLASPDDLLNFFNDMRGILGSLDSGVVQDDQIILDPNSNLGMFVRRCILAFNLLSFEGVCHLFSSIEDYCKEAHSSFAQFGAPNNNLESLIQYDQMDMENYAMDKPTEEIEFQKTASGIVPFHLHTPDSLMKATEGLLHNRKETSRTSKKDTEATPVARASTSTLEESLVDESLFLRTNLQIQGFLMEQADAIEIHGSSSSFSSSSIESFLDQLQKLAPELHRVHFLRYLNKLHSDDYFAALDNLLRYFDYSAGTEGFDLVPPSTGCSMYGRYEIGLLCLGMMHFRFGHPNLALEVLTEAVRVSQQLSNDTCLAYTLAAMSNLLSEMGIASTSGVLGSSYSPVTSTASSLSVQQRVYILLKESLRRADSLKLRRLVASNHLAMAKFELMHVQRPLLSFGPKASMRHKTCPVSVCKEIRLGAHLISDFSSESSTMTIDGSLSSAWLKDLQKPWGPPVISPDSGSRKSSTFFQLCDHLVSIPGSVSQLIGASYLLRATSWELYGSAPMARMNTLVYATLFGDSSSSSDAELAYLKLIQHLALYKGYKDAFAALKVAEEKFLTVSKSKVLLLKLQLLHERALHCGNLKLAQRICNELGGLASTAMGVDMELKVEASLREARTLLAAKQYSQAANVAHSLFCTCHKFNLQIEKASVLLLLAEIHKKSGNAVLGLPYALASISFCQSFNLDLLKASATLTLAELWLGLGSNHTKRALDLLHGAFPMILGHGGLELRARAYIFEANCYLSDPSSSVSTDSDTVLDSLRQASDELQALEYHELAAEASYLMAMVYDKLGRLDEREEAASLFKKHIIALENPQDVEQNMA
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication (By similarity). Protein modification; protein ubiquitination. The APC/C is composed of at least 10 subunits (By similarity). Interacts with PYM. Belongs to the APC5 family.
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Q5ZKK3
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MASVHESLYFNPMMTNGVVHANVFGIKDWVTPYKMALLVLLSELGRAGSQLDQLERRRLNRLLLPLLQGPDMPLSRLRKAIEECCPNLAGSVHIRLKLIAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVIGLFLRHMILAYNKLSFSQVYKLYTALQQYFLNDEKKCGIDENDMELTNTEELDGKMEKEELDVPLREEEISCSGPLSQKQAEYFLSQQASLLKNDETKALSPVSLQKELNNLLKFNPDFAEAHYLSYLNSLRVHDVFSSTHSLLHYFDRLILTGAESKSNGDEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESNDHVCLQHCLSWLHISEQKIFDSCVLLEHSVNKSLHFGLPYLASLGIQSLVQQRAFAGKAANKLMDALKDSDLLHWKHSLSELIDISIAQKTAIWRLYGRSTMALQQAQTLLSMNSLEAVNVGVQQNNTEAFAVVLCHLAELHAEQGYFAAASEILKHLKERFPPNSQHAQLWMLFDQKIQFERAMNDGRYHIADSLVAGITALNSIEGMYRKAIVLKAQNQMLEAHKLLQKLLIHCQEIKNTEIVISVLLSVAELYWRSSCHTIALPVLLQALAFSREYSLQYLASETVLNLAFSQLILGVPEQVLNILHMAIEPGLAHGAVLDKGCAMFLVAKCQVASTASYSQQKKAEALESAILNLNEAKTYLAKVDCKEQLRDVLYFQARLFHTLGKTQERNKCAMLFRQLHQELPAHGVPLINAFK
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Protein modification; protein ubiquitination. The APC/C is composed of at least 12 subunits. Belongs to the APC5 family.
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Q54VV5
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MDKYRLTPHKITICVLVEYYLNGTIKYHQKQSLSHLLIRHIKENNYQDTVKEVSLYDFIEKELKYVLPIQFINNEFLRMIQFDSVDDIYQFMSSLKELFNGSNDHESINSKQMQLLDSKSILGIFIKKVILNFNQILFDGLIKLYDQLDQYLNDFYNEINKIQQQQQQQQQKEHCENDNSIDMSMDQEQQQQQQEDYNEISNYENKIKFLSPLDEERFIYEETIRINSLIGIETPLEIENQVNRLKASLPNVKRVHLISLLFNIGYQDYDQSLEDLHRYFDYVNGQMTSSQWSSSASSFLFTPNDNYQSGNSNSSNYYYNNYNFIGGSGDTTNLMLPYAVLNLVRLHYHFGHYEESYLALREAIRIAQERADHSCLALADHWLARLLKKSVYNSMESSNLLQYLLASHSDSEILKKSIERSRDLEMPDLLALNHTAFSKYKLENGEFSTNINSNNYNSNNNNNNNNSNTNNNTNNNNNTNNANNNNNNNNNNTNNTNNNNNNNNNNNNNNNNNNNNNNSSNSNNNGGVNMFGKSFHLWNDIFQPIEISRLLDKSSSTAMIAHHLYSSSWELLGNNDLAQFFTELAMKSYHSNDLSLQHDPLRAVSSQNTIIYNIGTNNNNNNNNNNNQIKQQQQQNQQPPDLLSFCKLALLYSKKSKYNEAIQILIKCFSIYKTQHLCGNLLTFTVLSILFDHLMINIDNNNNNNNNNNNNNNNNNNNNNNDNELLISIVIESLINITNRFQSEDSVDGSGWSQIVICYQKIIKYYCNVRGMYEKSMNLIVKGIQISRDFGLDSQITHFYSLLSKIYEKSSPYRFSGLSDTLSALSLSNSYHLANSIADSNIALIKIHLSTDRLDKAITLIKETLPMVLSDKLLNSQLYLLWAKSLISTSTKQSIDYLNRSEQLFLQLFSNQSNNNNNNNNNNNNNNELLKEIYYLKSIIYNDLGDIENRNLYAKKFKSILVPSSSIQQQQQQQQQQQQQQQQQQQQQQQSNQSPVINSVQPTPKICLVPPILMKIR
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: anapc1, anapc2, anapc3, anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26 and cdh1. Belongs to the APC5 family.
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Q9BQD4
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MASVHESLYFNPMMTNGVVHANVFGIKDWVTPYKIAVLVLLNEMSRTGEGAVSLMERRRLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMELTSRDEGERKMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQASLLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESKSNGEEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESNDHVCLQHCLSWLYVLGQKRSDSYVLLEHSVKKAVHFGLPYLASLGIQSLVQQRAFAGKTANKLMDALKDSDLLHWKHSLSELIDISIAQKTAIWRLYGRSTMALQQAQMLLSMNSLEAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEVLKHLKERFPPNSQHAQLWMLCDQKIQFDRAMNDGKYHLADSLVTGITALNSIEGVYRKAVVLQAQNQMSEAHKLLQKLLVHCQKLKNTEMVISVLLSVAELYWRSSSPTIALPMLLQALALSKEYRLQYLASETVLNLAFAQLILGIPEQALSLLHMAIEPILADGAILDKGRAMFLVAKCQVASAASYDQPKKAEALEAAIENLNEAKNYFAKVDCKERIRDVVYFQARLYHTLGKTQERNRCAMLFRQLHQELPSHGVPLINHL
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Protein modification; protein ubiquitination. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. The TPR repeats are six to seven residues longer than a canonical TPR motif. Belongs to the APC5 family.
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C4KIC4
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MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKSSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYVKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVKDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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C3MQZ8
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MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVRDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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C3MWY6
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MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKSSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYVKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVKDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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C3NGG9
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MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVVGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNARDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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C3N766
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MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVRDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q975P3
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MKQYKILFFIADGLGDRPVRKLQGKTPLEYVDKPNIRELLKNSIIGLMDPISPGVVAGSDTSHLSMFGLDPHKYYRGRGAFEAIGAGARLKASDVAFRGNFATVNNEFIVVDRRAGRKIEEADDLVKELNEKIGEIDGVKVRFYHGTEHRVAVVLSGKGLTDKVSDTDPHEVNKKVLESKPLDNSPESQFTANIINKLTRKIYEILNSSEINKIRVSKGELPANIILLRGAAEFVELPQFESYTKLKAAAVSATALIKGICEQIGMRVVTPPGATGGLDTNYLGKADAAVELLKEYDFVFLHLKATDAASHDGNVDGKVYAINKMDEMIGRILDKLGSELVIAISGDHTTPVEVKEHTGDPVPFLLYVPYDIINDVVNDFNEREARRGSLRIRGLDVINLLLNYSNRAEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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B7IDT4
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MIDRQKVISELISPNTSKIVLLVMDGIGDIPNEEGLTPLQKANTPNLDALAKKSDLGQTIPVLPGITPGSGPGHLGLFGYDPLKYQIGRGILEALGINVEVGENDLVARGNFATIDGDIIVDRRAGRPSSEESAKVVEILNENIKEIEDVKITFYPGKEHRFVVKFTGEGLMDKLEDADPQKEGKPIKYTKALDESSKKSERIVNILLDKIKEVLKDQPKMNFALLRGFSKHPDMPKFGDVFKLKPAAVAVYPMYKGLAKLVGMEVVEAGQTIEDEFNTVKKLWNEYDFFYVHIKKTDSYGEDGNFDSKVKVIEEVDKFLPILLELNPDVLIVTGDHSTPCVMKGHSFHPVPLMIYAKNTRRGLSKLFNEFECARGSLGTIHAVDVMPLALAYAGRLEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q9HL27
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MMKSIILIVLDGLGDRPGSDLQNRTPLQAAFRPNLNWLASHGINGIMHPISPGIRCGSDTSHMSLLGYDPKVYYPGRGPFEALGLGMDIRPGDLAFRANFATNRDGVIVDRRAGRENKGNEELADAISLDMGEYSFRVKSGVEHRAALVVSGPDLSDMIGDSDPHREGLPPEKIRPTDPSGDRTAEVMNAYLEEARRILSDHRVNKERVKNGRLPGNELLVRSAGKVPAIPSFTEKNRMKGACVVGSPWLKGLCRLLRMDVFDVPGATGTVGSNYRGKIEKAVDLTSSHDFVLVNIKATDVAGHDGNYPLKRDVIEDIDRAMEPLKSIGDHAVICVTGDHSTPCSFKDHSGDPVPIVFYTDGVMNDGVHLFDELSSASGSLRITSYNVMDILMQLAGRSDKFGS
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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C5A4S1
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MKKRKGLLIILDGLGDRPIKEFGGKTPLEYAKTPNMDKLAKLGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEALGVGLDLDEDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAIQENVKLPVDFIFVGATGHRAVLVLKGMAKGYRVGENDPHEAGKPPHRFTWEDEESKRVAEILEEFVRQAHEVLERHPINEKRRKEGKPVANYLLIRGAGTYPDIPMKFTEQWKVRAGAVIAVSLVKGVARAIGFDVYTPEGATGEYNTDEMAKAKKTVELLKEYDFVFLHFKPTDAAGHDNNPKLKAEMIEKADRMIGYIIEHINLEDVVIAITGDHSTPCEVMNHSGDPVPLLIVGGGVRPDHTESFGERECMRGGLGRIRGHDIVPVMMDLMNRSEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q5JI21
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MKKRKGLLIILDGLGDRPIKEFGGKTPLEYANTPNMDRLAKMGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEALGVGLDLNEDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAVQENVKLPVDFIFVGATGHRAVLVLRGMAKGYRVGENDPHEAGKPPQEFTWEDEESKKVAEILEEFVQKAHEVLDKHPINEKRRKEGKPPANYLLIRGAGTYPDIPMKFTEQWKVKAGAVIAVSLVKGVARAIGFDVYTPEGATGEYNTDVMAKAKKTVELLKDYDFVFLHFKPTDAAGHDNNPKLKAEMIEKADRMIGYILEHIDLEDVVIAITGDHSTPCEVMNHSGDPVPLLIAGGGVRPDHTESFGERECMRGGIGRIKGHDIVPIMMDLMNRSEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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A6LMV5
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MIDRQQILNELISPNSSKIVLLVMDGIGDIPGEDGLTPLQKANTPKLDELAKQSDLGQTIPVLPGITPGSGPGHLGIFGYDPLKYQIGRGILEALGIDVEVGEKDLVARGNFATLEGDIIVDRRAGRPSSEESAKVVEILNENIHKIEDVEVKFYPGKEHRFVVKLTGEGLYDKLEDADPQKEGKPIKYTKALDESSKKSEKIINILIDRIKEVLKDQQKMNFALLRGFSKYPNLPSFGDVYKLRPAAIAVYPMYKGLAKLVGMEILKTGQTIEDEFKTVKENWEKYDFFYVHVKKTDSYGEDGNFESKVKVIEEVDKNLGLLLELKPDVLIVTGDHSTPCAMKGHSFHPVPLMIYSKFTRKGLSKLYNEFECARGTLGTIPAVDVMSLALAYAGRLEKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q9X295
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MFDKQEFVSKLVTEEKAKIVLLVMDGLGDIPVNGKTPLQAANTPNLDNLAKESDLGQTIPVLPGITPGSGPGHLSLFGYDPIKYQIGRGILEALGIGVEVGEKDVVARANFATWDGKVVLDRRAGRPATEESAKVVQLLSEKIKKIEDVEITFYPGKEHRFVVKFTGEGLGDKVTDADPQKEGHPMVWAEGLDEPSKKTARIVNELIKKIAEVLKDNPKINFALIRGFSKYPDLPKFPQVYKMKAGAIATYPMYRGLAKLVGMEIIETGQTVADEIKTLKEKWNDYDFFYVHVKKTDSYGEDGKFEEKVKVIEEVDAIIPEIVSLNPDVLVITGDHSTPVPLKAHSWHPVPLLIWSKYTRRGLSQAFNEFECARGTLGTIHASDVMTLALAYAGKLEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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B9K857
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MLDKQKFVSKLVTTNDTKIVLLVMDGLGDIPVNGKTPLQAASTPNLDSLAKESDLGQTVPVLPGITPGSGPGHLSLFGYDPIKYQIGRGILEALGIGVEVGEKDVVARANFATWDGNVVLDRRAGRPATEESAKVVQLLSEKIKKIEDVEITFYPGKEHRFVVKFTGEGLGDRVTDADPQKEGHPMVWAEGLDEPSKKTARIANELIRKIAEVLKDNPKINFALIRGFSKYPDLPKFPEIYKLRAGAIATYPMYRGLAKLVGMEIIETGQTVEDEINTLKEKWNDFDFFYVHVKKTDSYGEDGKFDEKVKVIEEVDRVIPEILALKPDVLVITGDHSTPVPLKAHSWHPVPLLIWSRYTRRGLSQAFNEFECARGTLGTIHASDVMTLALAYAGRLEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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A5ILK6
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MFDKQEFVSKLVTEEKAKIVLLVMDGLGDIPVNGKTPLQAANTPNLDSLAKESDLGQTIPVLPGITPGSGPGHLSLFGYDPIRYQIGRGILEALGIGVEVGEKDVVARANFATWDGKVVLDRRAGRPATEESAKVVQLLSEKIKKIEDVEITFYPGKEHRFVVKFTGEGLGDNVTDADPQKEGHPMVWAEGLDEPSKKTARITNELIKKIAEVLKDNPKINFALIRGFSKYPDLPKFPQVYKMKAGAIATYPMYRGLAKLVGMEIIETGQTVADEIKTLKERWNDYDFFYVHVKKTDSYGEDGKFEEKVKVIEEVDALIPEIVSLNPDVLVITGDHSTPVPLKAHSWHPVPLLIWSKYTRRGLSQAFNEFECARGTLGTIHASDVMTLALAYAGKLEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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B1LAP9
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MFDKQEFVSKLVTEEKAKIVLLVMDGLGDIPVNGKTPLQAANTPNLDNLAKESDLGQTIPVLPGITPGSGPGHLSLFGYDPIKYQIGRGILEALGIGVEVGEKDVVARANFATWDGKVVLDRRAGRPATEESAKVVQLLSEKIKKIEDVEITFYPGKEHRFVVKFTGEGLGDKVTDADPQKEGHPMAWAEGLDEPSKKTARIVNELIKKIAEVLKDNSKINFALIRGFSKYPDLPKFPQVYKMKAGAIATYPMYRGLAKLVGMEIIETGQTVADEIKTLKEKWNDYDFFYVHVKKTDSYGEDGKFEEKVKVIEEVDAIIPEIVSLNPDVLVITGDHSTPVPLKAHSWHPVPLLIWSKYTRRGLSQAFNEFECARGTLGTIHASDVMTLALAYAGRLEKFGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q72GG0
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MDLFPVLKELAQKTPSKILLIVLDGVGGLPLEPGGPTELEAAKTPNLDRLAEESALGLLTPVYPGLAPGSGPGHLALFGYDPFRYVVGRGALSALGLGADFREGDVALRGNFATLDPEGKVVDRRAGRPPTEENQRVVAKLKEAIPRIEDVEVHFYTESEHRFLVVLRGEGLGDAVTDTDPQKTGLPPLKAKALDEASERTARLVNLLSERIREVLKDEPRMNGALFRGASKKPSFPRMQEVYKLTPAAIASYPMYKGLASLVGMEVLPVEGEGDALEGKLKALKENWGRYDFFYFHVKKTDAMGEDGNFHGKVEKVELFDALLPEILALGPDVLAITGDHSTPALLKAHSWHPVPLLLKAPYLRADEARRFTEREAQRGSLGHLRGMELMPLLLAHAGKLLKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q5SM27
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MDLFPVLKELAQKTPSKILLIVLDGVGGLPLEPGGPTELEAAKTPNLDRLAEESALGLLTPVYPGLAPGSGPGHLALFGYDPFRYVVGRGALSALGLGADFREGDVALRGNFATLDPEGKVVDRRAGRPPTEENQRVIAKLKEAIPRIEDVEVLFYTESEHRFLVILRGEGLEDKVTDTDPQKTGLPPLKAKALDEASERTARLVNLLSERIREVLKDEPRMNGALFRGASKKPSFPRMQEVYKLTPAAIASYPMYKGLASLVGMEVLPVEGEGDALEGKLKALKENWGRYDFFYFHVKKTDAMGEDGNFHGKVEKVELFDALLPEILALGPDVLAITGDHSTPALLKAHSWHPVPLLLKAPYLRADEARRFTEREAQRGSLGHLRGVELMPLLLAHAGKLLKYGA
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q979H8
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MIDVKSIILIVLDGLGDRPGEILGYRTPLQAAYHPNMNRMASLGMTGLMHPISPGIRSGSDTSHMSLLGYDPRVYYQGRGPFEALGLHMDMKPGDLAFRANFATNRDGKIIDRRAGRINAGNDQLASAISIDIGNYKFRVKSGVEHRAALVVSGPNLSDKISDSDPHSEGKPPEPIRPLDPSADSTAKIMNEYLKRIREILRDHPVNVEREKNGQIPGNELLIRSAGKVPDIPSFQEKNGITGACVVGSPWLKGLCRLLGMAVIDVPGAAGTINSNYTGKIKTAIDASKRYDFVLVNIKATDVAGHDGDYELKRRVIEDIDIAMEPLLGQSDRIVVAITGDHSTPCSVKDHSGDPVPIVFYTDGIYSDDVKLFDEVSAMKGALRITTQDVLNILMEMAGRAEKFGS
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
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Q9LNT8
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MKRSSLVDSCSYSRIFRSIFCLLSFCIFFLTTTNAQVMHRRLWPWPLWPRPYPQPWPMNPPTPDPSPKPVAPPGPSSKPVAPPGPSPCPSPPPKPQPKPPPAPSPSPCPSPPPKPQPKPVPPPACPPTPPKPQPKPAPPPEPKPAPPPAPKPVPCPSPPKPPAPTPKPVPPHGPPPKPAPAPTPAPSPKPAPSPPKPENKTIPAVFFFGDSVFDTGNNNNLETKIKSNYRPYGMDFKFRVATGRFSNGMVASDYLAKYMGVKEIVPAYLDPKIQPNDLLTGVSFASGGAGYNPTTSEAANAIPMLDQLTYFQDYIEKVNRLVRQEKSQYKLAGLEKTNQLISKGVAIVVGGSNDLIITYFGSGAQRLKNDIDSYTTIIADSAASFVLQLYGYGARRIGVIGTPPLGCVPSQRLKKKKICNEELNYASQLFNSKLLLILGQLSKTLPNSTFVYMDIYTIISQMLETPAAYGFEETKKPCCKTGLLSAGALCKKSTSKICPNTSSYLFWDGVHPTQRAYKTINKVLIKEYLHVLSK
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A number of isoforms are produced. According to EST sequences. Found in sporophytic and gametophytic cell types in the anther, only in male fertile plants. Expressed in male gametogenesis, during microspore development. Higher expression is found during microspore mitosis with a dramatic decline during pollen maturation. Belongs to the 'GDSL' lipolytic enzyme family.
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P40603
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PPKPQPKPPPKPQPKPPPAPTPSPCPPQPPKPQPKPPPAPTPSPCPPQPPKPQPKPPPAPGPSPKPGPSPSPPKPPPSPAPKPVPPPSPSPKPSPPKPPAPSPKPSPPKPPAPSPPKPQNKTIPAVFFFGDSIFDTGNNNNLDTKLKCNYRPYGMDFPMGVATGRFSNGRVASDYISKYLGVKEIVPAYVDKKLQQNNELQQSDLLTGVSFASGGAGYLPQTSESWKVTTMLDQLTYFQDYKKRMKKLVGKKKTKKIVSKGAAIVVAGSNDLIYTYFGNGAQHLKNDVDSFTTMMADSAASFVLQLYGYGARRIGVIGTPPIGCTPSQRVKKKKICNEDLNYAAQLFNSKLVIILGQLSKTLPNSTIVYGDIYSIFSKMLESPEDYGFEEIKKPCCKIGLTKGGVFCKERTLKNMSNASSYLFWDGLHPSQRAYEISNRKLVKKYIHFI
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Found in anther, only in male fertile plants. Expressed in male gametogenesis, during microspore development. Higher expression is found during microspore mitosis with a dramatic decline during pollen maturation. Belongs to the 'GDSL' lipolytic enzyme family.
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Q7T0X4
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MESEGFSATTEQYEYYDYANETGLQPCDETDWDFSYSLLPVFYMIVFVLGLSGNGVVIFTVWKAKPKRRSADTYIGNLALADLAFVVTLPLWATYTALGFHWPFGSALCKLSSYLVLLNMFASVFCLTCLSFDRYLAIVHSLSSAKLRSRSSILVSLAVIWLFSGLLALPSLILRDTRVEGNNTICDLDFSGVSSKENENFWIGGLSILTTVPGFLLPLLLMTIFYCFIGGKVTMHFQNLKKEEQKKKRLLKIIITLVVVFAICWLPFHILKTIHFLDLMGFLELSCSAQNIIVSLHPYATCLAYVNSCLNPFLYAFFDLRFRSQCFFFFGFKKVLQGHLSNTSSSLSAQTQKSEIHSLATKV
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Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity (PubMed:17412318). Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively (By similarity). Promotes angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone (PubMed:17412318). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility, and heart failure. Acts upstream of the i/o type of G-alpha proteins in the differentiation of endothelium, erythroid cells, myeloid cells and cardiomyocytes (By similarity). Internalized to the cytoplasm after exposure to apelin (apln) (PubMed:17412318). After exposure to apelin receptor early endogenous ligand (apela), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). Expressed in all blood vessels including the posterior cardinal vein, intersomitic veins and the vitelline vein network. Belongs to the G-protein coupled receptor 1 family.
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P35414
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MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFFCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVLRTTGDLENTTKVQCYMDYSMVATVSSEWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNIFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD
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Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity (PubMed:11090199, PubMed:25639753, PubMed:28137936). Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone (By similarity). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (PubMed:25639753, PubMed:28137936). (Microbial infection) Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia (PubMed:11090199). After exposure to apelin (APLN), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). After exposure to apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (PubMed:25639753). Expressed in heart, brain, kidney, stomach, spleen, thymus, lung, ovary, small intestine and colon, adipose tissues and pancreas (PubMed:8294032, PubMed:25639753). Expressed in glial cells, astrocytes and neuronal subpopulations (PubMed:8294032). Expressed in embryonic (ESCs) and induced (iPSCs) pluripotent stem cells (PubMed:25639753). Belongs to the G-protein coupled receptor 1 family.
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O97666
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MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVFRTTGDLENTTKVQCYMDYSMVATVSSDWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD
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Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure. (Microbial infection) Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia. After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. Belongs to the G-protein coupled receptor 1 family.
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Q3TZS9
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MEDDGYNYYGADNQSECDYADWKPSGALIPAIYMLVFLLGTTGNGLVLWTVFRTSREKRRSADIFIASLAVADLTFVVTLPLWATYTYREFDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAVPVMVFRSTDASENGTKIQCYMDYSMVATSNSEWAWEVGLGVSSTAVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDIFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCDQSGCKGTPHSSSAEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVD
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Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone (PubMed:28854362, PubMed:28890073, PubMed:28663440). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (PubMed:28890073). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (PubMed:28371822). After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. Expressed in coronary endothelial cells (at protein level) (PubMed:28890073). Expressed in the embryo, allantoic and endothelial precursor cells of the yolk sac at 8 days post-coitum (dpc) (PubMed:28663440). Expressed in the secondary heart field and somite at 8.25 dpc (PubMed:28854362). Expressed in fetal allantoic endothelial cells at 9 dpc (PubMed:28663440). Expressed in the allantoid and the invading fetal vasculature of the placenta at 9.5 dpc (PubMed:28854362). Expressed in endothelial cells adjacent to syncytiotrophoblast cells at 10.5 dpc (PubMed:28663440). Expressed weakly in the embryonic heart at 11.5 dpc (PubMed:26611206). Expressed in the adult heart (PubMed:26611206). Expressed in endothelial cells and cardiomyocytes and weakly expressed in fibroblasts (PubMed:10473142, PubMed:26611206). Expressed from embryonic 8 days post-coitum (dpc) throughout the subsequent stages of formation of the cardiovascular system (PubMed:10473142). Up-regulated following myocardial infarction (MI) (at protein level) (PubMed:26611206). Mice lacking APLNR are not represented at Mendelian ratios. Mutant embryos exhibit incomplete penetrance of embryonic lethality (PubMed:28854362, PubMed:28663440). Mutant embryos display improper establishment of the fetal-maternal circulation, such as underdeveloped yolk sac vasculature, embryonic vascular malformations and impaired cardiac tube looping at 10.5 dpc (PubMed:28854362, PubMed:28663440). Mice heart of embryos show reduced coronary vessel growth at 13.5 dpc (PubMed:28890073). The heart of mutant adult mice induced by pressure overload display no improvement in cardiac dysfunction, hypertrophy and fibrosis in response to peptide hormone APELA treatment (PubMed:28371822). Conditional knockout in heart endothelial cells leads to delayed progression of vessel growth onto the heart and reduced branching of the developing coronary plexus in both the subepicardial and intramyocardial layers at 13.5 and 15.5 dpc (PubMed:28890073). Conditional endothelial-specific knockout adult mice, despite severe embryonic coronary vessel defects recover normal cardiac functions; endocardial-derived coronary vessels expand to rescue defective sinus venosus development in a APELA-APLNR-independent manner (PubMed:28890073). Double knockout mice of APLNR and APELA genes exhibited the same penetrance and embryonic lethality as single APELA knockout mice (PubMed:28854362). Belongs to the G-protein coupled receptor 1 family.
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Q9ESK2
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MEDDGYNYYGADNQSECDYADWTPSGALIPAIYILVFLLGTTGNGLVLWTVFWSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYREFDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAVPVMVFRSTDIPENSTKTQCYMDYSMVATSNSEWAWEVGLGVSSTAVGFVVPFIIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGNLLHWPCDFDSFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRRACTSMLCCDQSGCKGSPHSSSAEKSASYSSGHSQGPGPNMCKGGEPMHEKSIPYSQETLVD
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Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity (PubMed:11359874). Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (By similarity). After exposure to apelin (APLN), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (PubMed:11359874). After exposure to apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). Widely expressed. Highest expression in the lung, lower in the heart, placenta, ovary, skeletal muscle, mammary gland, kidney and several structures in the brain as the hypothalamus (supraoptic and periventricular nuclei), pituitary, olfactory bulb and pineal gland. Higher expression in neonates than in adult. Belongs to the G-protein coupled receptor 1 family.
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Q4VA82
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MATDEFSSSTTPSYDYYDYTNESGLPPCDETDWDLSYSLLPVFYMIVFVLGLSGNGVVIFTVWKAKPKRRSADTYIGNLALADLAFVVTLPLWATYTALGFHWPFGSALCKLSSYLVLLNMFASVFCLTCLSFDRYLAIVHSLSSAKLRSRSSILVSLAVIWLFSGLLALPSLILRDTRVEGNNTICDLDFSGVSSKENENFWIGGLSILTTVPGFLLPLLLMTIFYCFIGGKVTMHFQNLKKEEQKKKRLLKIIITLVVVFAICWLPFHILKTIHFLDLMGFLELSCSTQNIIVSLHPYATCLAYINSCLNPFLYAFFDLRFRSQCFFFFGFKKALQGHLSNTSSSLSAQTQKSEIHSLATKV
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Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively. Promotes angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Required for cardiovascular development, particularly for intersomitic vein angiogenesis. Plays also a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility, and heart failure. Acts upstream of the i/o type of G-alpha proteins in the differentiation of endothelium, erythroid cells, myeloid cells and cardiomyocytes. Internalized to the cytoplasm after exposure to apelin (apln). After exposure to apelin receptor early endogenous ligand (apela), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. Belongs to the G-protein coupled receptor 1 family.
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Q8LES2
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MIAAGAKSLLGLSMASPKGIFDSNSMSNSRSVVVVRACVSMDGSQTLSHNKNGSIPEVKSINGHTGQKQGPLSTVGNSTNIKWHECSVEKVDRQRLLDQKGCVIWVTGLSGSGKSTLACALNQMLYQKGKLCYILDGDNVRHGLNRDLSFKAEDRAENIRRVGEVAKLFADAGIICIASLISPYRTDRDACRSLLPEGDFVEVFMDVPLSVCEARDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEISLGREGGTSPIEMAEKVVGYLDNKGYLQA
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Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates. adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+) Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3. Homodimer; disulfide-linked. Interacts with APK2. Expressed in root vasculature, root tips, leaf epidermal and guard cells, pollen grains and funiculus of developing seeds. No visible phenotype under normal growth conditions. Apk1 and apk2 double mutant exhibits a semi-dwarf phenotype. Belongs to the APS kinase family.
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O49196
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MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG
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Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates. adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+) Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3. Interacts with APK1. Expressed in root vasculature, root tips, leaf epidermal cells and funiculus of developing seeds. No visible phenotype under normal growth conditions. Apk1 and apk2 double mutant exhibits a semi-dwarf phenotype. Belongs to the APS kinase family.
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Q9SQR9
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MSTVGNSTNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELKEKEGECPSPVAMAEEVISYLEDKGFLQNE
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Catalyzes the synthesis of activated sulfate for the sulfation of secondary metabolites, including the glucosinolates (PubMed:19304933). Essential for plant reproduction and viability (PubMed:19903478). adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+) Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3. Expressed in root vasculature, root tips, leaf epidermal and guard cells, pollen grains and radicle of immature seeds. No visible phenotype under normal growth conditions. Belongs to the APS kinase family.
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Q9FJX1
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MDVAAMARCVGRCYVSPAFGESESHRLSERRFLKLSSSTNSDPAGSKSLKLRGKIHRRMSYFRPIMAKDESISSRSGETKQINGKQKNIVWHDCPVTKSDRQELIKQKGCVIWITGLSGSGKSSLACALSRALHNRGKLSYILDGDNVRHGLNSDLSFEADDRAENIRRVGEVAKLFADSGIICIASLISPYRIERAACRALLPQGDFIEVFMDVPLHVCEARDPKGLYKRARAGKIKGFTGVDDPYEAPLDCEIVIQNSRDKGLSSSSSSSSSPSSSSSSLCEMADIVVSYLDQNGYLKKHSTKSRNCM
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Catalyzes the phosphorylation of adenosine 5'-phosphosulfate to 3'-phosphoadenylyl sulfate, which is the activated sulfate form for sulfation reactions. Essential for plant reproduction and viability. adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+) Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3. Homodimer; disulfide-linked. Expressed in root vasculature, root tips, leaf epidermal and guard cells, pollen grains and radicle of immature seeds. No visible phenotype under normal growth conditions. Belongs to the APS kinase family. Truncated N-terminus.
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Q9GSZ3
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MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTPSRLFFVIEFVRGGDLMYHMQRQRRLPEEHARFYAAEISLALNFLHEKGIIYRDLKLDNVLLDHEGHIKLTDYGMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLLYEMLAGRSPFDLAGASENPDQNTEDYLFQVILEKTIRIPRSLSVRAASVLKGFLNKNPADRLGCHRESAFMDIVSHPFFKNMDWELLERKQVTPPFKPRLDSDRDLANFPPEFTGEAVQLTPDDDHVIDNIDQSEFEGFEYVNPLLMSLEDCV
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Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification factors and for the posterior establishment of the microtubule organizing center within the presumptive oocyte. Phosphorylates l(2)gl which restricts l(2)gl activity to the oocyte posterior and regulates posterior enrichment of par-1, leading to establishment of correct oocyte polarity. Essential for apical localization of l(2)gl and par-6 in neuroblasts and for exclusion of mira from the apical cortex. Phosphorylates baz which is required for targeting of baz to the postsynaptic region where it is involved in actin organization, and for apical exclusion of baz which is necessary for establishment of the apical/lateral border in epithelial cells. Phosphorylates yrt which prevents its premature apical localization and is necessary for correct epithelial cell polarization. Required for the establishment of mitotic spindle orientation during symmetric division of epithelial cells and for apical exclusion of raps/Pins. Involved in symmetric adherens junction positioning during embryogenesis. Required for polarization of the spermatid cyst which is necessary for sperm differentiation. Required for stimulation of the Toll signaling pathway which activates Dif and dl and plays a role in innate immunity. Plays a role in memory enhancement. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with baz; the interaction is required for apical localization of aPKC in neuroblasts and epithelial cells. Interacts with Dap160; the interaction promotes aPKC apical localization and kinase activity. Interacts with and phosphorylates l(2)gl and yrt. Interacts with crb and ref(2)P. Forms a complex with baz, fz and Patj. Cytoplasmic at interphase but localizes to the apical cell cortex during mitosis. Expressed in the testis. In spermatid cysts, localizes near the tips of spermatid flagellar axonemes (at protein level). Detectable in freshly laid eggs before onset of zygotic transcription so is deposited in the egg during oogenesis. At the cellular blastoderm stage, present in all cells except the pole cells. During gastrulation, strongly expressed in tissues undergoing morphogenetic movements such as invaginating mesoderm, proctodeum and cephalic furrow. Strongly expressed in neuroblasts. Zygotes survive to mid-larval stages where they exhibit defects in neuroblast and epithelial cell polarity. Mutant neuroblasts lack apical localization of l(2)gl and par-6, and fail to exclude mira from the apical cortex. Oocytes do not differentiate and display failure of BicD and ORB to translocate from the anterior to the posterior crescent, accumulation of Dhc64C in the two posterior-most presumptive pre-oocytes instead of in a single cell as normal, and defective posterior assembly of the microtubule organizing center. Adherens junctions form atypical planar-polarized puncta at gastrulation. Reduced yrt phosphorylation. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
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P07095
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MKLHVAALATLAVVCILAAGSEAAPKAMSDPAVVKAQLFPDAFWESFKNVSMEFKKMVHGLQTSNIGEHAKSLYTDTVAVLTPYLQKIRENVTKMYQVYVESKQH
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Plasma.
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B8AVJ9
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MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGTGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPLPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT
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Transcription factor (PubMed:22408071). Involved in spikelet transition and development (PubMed:22408071). Prevents lemma and palea elongation as well as grain growth (PubMed:22408071). Required for seed shattering through specifying abscission zone (AZ) development (PubMed:22408071). May form homodimer. Expressed in seedlings, leaves, stems, nodes, sheaths, panicles and young spikelets. Accumulates in the spikelet abscission zone (AZ) via a positive regulation by the transcription factor SH4. In developing panicles, highly expressed in the spikelet abscission zone (AZ) and the inner floral organs of 2 mm long spikelets. Later present at weak levels in the apiculus as well as in the palea and lemma to progressively fades out in 8 mm long spikelets. Several spikelet and inflorescence developmental defects, including altered florets palea and lemma structures, abnormal numbers, size, appearance, and identities of floral organs, reduced primary branches number, and longer and fewer grains associated with a loss of grain shattering. Crook-neck-like rachilla between the sterile lemmas and the rudimentary glumes in place of the spikelet abscission zone (AZ). Belongs to the AP2/ERF transcription factor family. AP2 subfamily.
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Q7XT53
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MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGAGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPHPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT
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Transcription factor (PubMed:22408071). Involved in spikelet transition and development (Probable) (PubMed:22408071). Prevents lemma and palea elongation as well as grain growth (PubMed:28066457, PubMed:22408071). Required for seed shattering through specifying abscission zone (AZ) development (PubMed:22408071). May form homodimer. Expressed in seedlings, leaves, stems, nodes, sheaths, panicles and young spikelets (PubMed:22408071). Accumulates in the spikelet abscission zone (AZ) via a positive regulation by the transcription factors SH4 and SH5 (PubMed:22408071, PubMed:24923192). In developing panicles, highly expressed in the spikelet abscission zone (AZ) and the inner floral organs of 2 mm long spikelets. Later present at weak levels in the apiculus as well as in the palea and lemma to progressively fades out in 8 mm long spikelets. Target of miR172 microRNA mediated cleavage, particularly during floral organ development (Probable). Induced by SH5 in spikelets abscission zones (AZ). Triggered by cold stress (PubMed:24923192). Several spikelet and inflorescence developmental defects, including altered florets palea and lemma structures, abnormal numbers, size, appearance, and identities of floral organs, reduced primary branches number, and longer and fewer grains associated with a loss of grain shattering. Crook-neck-like rachilla between the sterile lemmas and the rudimentary glumes in place of the spikelet abscission zone (AZ). Belongs to the AP2/ERF transcription factor family. AP2 subfamily. Extended N-terminus.
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P07096
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MLSTKMTHAAGLLLLVLTAYVQADETQLVPATGKTYLETALERLHSYGEAVSGDKADGIMTEARELVEQFMEEFQAKALPEGVTTHKLAEEMAEAANAKLVPILQAAKAGIERVTAHLHESAPLIIKVRGFIESKRGVMWAYLAALAERAKKAKLDDTLKGVRDGLTALTLSSIGLMKEVKEIASAPPPAQ
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Plasma.
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P81471
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DAPSTTPPQDXEKKAAEFQKTFTEQXNQLANK
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Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3 (By similarity). Hemolymph. Belongs to the insect apolipophorin-3 family. Lipid freight - Issue 59 of June 2005
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P86356
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DAPASPLADIEKHAAEFQKTISEQFNSLVNSKNTQ
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Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects (By similarity). Has hemagglutinating activity towards rabbit erythrocytes. Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3 (By similarity). Hemolymph. By bacterial infection. Belongs to the insect apolipophorin-3 family.
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Q6VU70
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MAAKFIILLALFALSQASVVRRDAPLANFLQDLEKRAADIQKTFSEQFQAISNSKNVQDVNKAVKESSDVVLKQLSTLSSSLQSALTDANGKAKEALEQTRQNLEKTAEELRRAHPDVEKQANQLRDKLQAAVQSTLQETQKLAKEVAANMEQTNEKLAPKIKEAFEDFVKQAEAVQKKVHDAATKQ
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Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects (By similarity). Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3 (By similarity). Hemolymph. Belongs to the insect apolipophorin-3 family. Lipid freight - Issue 59 of June 2005
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P10762
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MNTLLAVLMLAVAAQARPDAAGHVNIAEAVQQLNHTIVNAAHELHETLGLPTPDEALNLLTEQANAFKTKIAEVTTSLKQEAEKHQGSVAEQLNRFARNLNNSIHDAATSAQPADQLNSLQSALTNVGHQWQTSQPRPSVAQEAWAPVQSALQEAAEKTKEAAANLQNSIQSAVQKPAN
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Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 14 molecules of apolipophorin-3 in L.migratoria (5 molecules of apolipophorin-3a and 9 of apolipophorin-3b). Hemolymph. Two isoforms of apolipophorin-3 (a and b) have been found and occur in a ratio of 5a:9b in the hemolymph. Belongs to the insect apolipophorin-3 family. Lipid freight - Issue 59 of June 2005
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P13276
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MAAKFVVVLAACVALSHSAMVRRDAPAGGNAFEEMEKHAKEFQKTFSEQFNSLVNSKNTQDFNKALKDGSDSVLQQLSAFSSSLQGAISDANGKAKEALEQARQNVEKTAEELRKAHPDVEKEANAFKDKLQAAVQTTVQESQKLAKEVASNMEETNKKLAPKIKQAYDDFVKHAEEVQKKLHEAATKQ
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Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3. Hemolymph. Belongs to the insect apolipophorin-3 family. Lipid freight - Issue 59 of June 2005
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P0DPG8
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MRLFLSLPVLVVVLAMVLEGPAPAQAAPEISRTFERIPDKLKEFGNTLEDKAREVLETIKQSDIPAKTRNWFSETYNKVKEQLKTAFS
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Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. Belongs to the apolipoprotein C1 family.
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P0DMT8
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MRPAVSIALALVALLVLADSARSEPGEPTLMQKLEQFKENVKVFADNIGEKTKAALQELHDSEFSTKTRNWFSEHFKKVKEKLKDTFA
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Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. Belongs to the apolipoprotein C1 family.
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P0DKV2
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MRLFLSLPVLVVALLMILEGPGPAQGAPEAVDTSSGLDKLKEFGTTLEDKVREFFNRVKESDIPAKTRNWFSETLQKVKEKLRIES
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Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. Apolipoprotein C-I is present in acidic (APOC1A) and basic (APOC1B) forms in P.paniscus, P.abelii and P.troglodytes and perhaps also in baboons and macaques. The two genes for ApoC-I arose through a duplication process that occurred after the divergence of New World monkeys from the human lineage. In human, the acidic form has become a pseudogene sometime between the divergence of bonobos and chimpanzees from the human lineage and the appearance of the Denisovans. Pseudogenization resulted when the codon for the penultimate amino acid in the signal sequence was changed to a stop codon. Belongs to the apolipoprotein C1 family.
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P0DTT3
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MRLFLSLPVLVVVLAMVLEGPAPAQAAPEISSTLERIPDKLKEFGNTLENKARAAIESIKQSDLPAKTRNWFSETFNKVKEQLKTTFS
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Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. Belongs to the apolipoprotein C1 family.
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