Split (1)

train · 541k rows

UniProt ID stringlengths 6 10	Protein Sequence stringlengths 2 35.2k	Functional Description stringlengths 5 30.7k
P0DKV3	MRLFLSLPVLVVVLLMILEGPGPAQGAPEALDTSSGLDKLKEFGNTLEDKVREFFNRVKESDIPAKTRNWFSETLQKVKEKLRIES	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.
P56595	MRLILSLPVLVVVLSMVLEGPAPAQAAGEISSTFERIPDKLKEFGNTLEDKARAAIESIKKSDIPAKTRNWFSEAFKKVKEHLKTAFS	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. Expressed in the liver. Belongs to the apolipoprotein C1 family.
P0DOA4	MRLFLSLPVLVVVLLMILEGPVPAQGAPEAVDASSGLDKLKEFGNTLENKVREFFSRIKESDIPTKTRNWFSETLQKVKEKLNIES	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.
P0DTG3	MRLILSLPVLAVVLAMVLEGPAPAQAAPDMSSTLESIPGKLKEFGSTVKEKFRTAIDQIQKSDFPEKTRNWFSDVFQKVKEKFETTFS	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.
P0DTG2	MRLILSLPVLAVVLAMVLEGPAPAQATTDVSSTSESILGKLKEFGSTVEEKVRTAIDQIKKSNVPEKTKNWFSEVFQKVKEKFETTFS	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.
P0DUX3	MRLFISLPVLIVVLAMALEGPAPAQATPDLSSTFENLPDKLKEFGNTLEDKARAAIEHIKQKEFLTKTRTWISETFGKMKEKIKTTFA	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). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification (By similarity). Belongs to the apolipoprotein C1 family.
P0DUX2	MRLFISLPVLIVVLAMALEGPAPAQATPDLSSTFENLPDKLKEFGNTLEDKARAAIEHIKQKEFLTKTRTWISETFGKMKEKIKTTFT	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). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification (By similarity). Belongs to the apolipoprotein C1 family.
P0DPG9	MRLFLSLPVLVVVLAMVLEGPAPAQAAPEISSTFERIPDKLKEFGNTLEDKARAAIETIKQSDIPAKTRTWFSETYNKVKERLKTAFS	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.
P0DTG4	MRLILSLPVLAVVLAMVLEGPAPAQAAPDISSAWESIPEKLEEFGRTVKEKVRTAIDHIKKSDFPEKTRKWFSEMFDTLKEKF	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.
P0DTT4	MRLFLSLPVLVVVLAMVLEGPAPAQAAPEISSTLERIPDKLKEFGNTLENKARAAIESIKQSDLPAKTRNWFSETFNKVKEQLKTTFS	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.
P0DM82	MRLILWLPVLVVVLLMVLEGPAPAQGAPAIASTFSNIPNSLKEFGNNLKDAFESIPEATRKLMTSFAEGLKNLRLPLL	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.
P0DUX4	MRLFIALPVLIVVVAMALEGPAPAQAAPDLSSTLERLPDKLKEFGSTLEDKAREAIDHIKQKEILTKTRTWFSETFSKVKEKLKTTFA	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). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification (By similarity). Belongs to the apolipoprotein C1 family.
Q6IB97	MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS	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. Synthesized mainly in liver and to a minor degree in intestine. Also found in the lung and spleen. 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. Apolipoprotein C1 entry
P0DM83	MRLFLSLPVLVVVLAMVLEGPAPTQAAPEISSTLGRIPDKLKEFGNTLEDKARAAIESIKQSDIPAKTRNWFSETFHKVKEQLKTAFS	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.
P0DPH0	MRLILSLPVLVVVLSMVLEGPAPAQAAGEISSTFERIPDKLKEFGNTLEDKARAAIESIKKSDIPAKTRNWFSEAFNKVKEHLKTAFS	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.
P0DPH1	MRLILWLPVLVVVLLMVLEGPAPAQGAPDIAGTFRNIPNSLKEFGNNLKDAFENIPEATRKLMTSFAEGLKNFRIPMV	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.
P0DTT2	MKVLWAALVVALLAGCWADVEPESPLEENLEPELEPKRELEQEVEPEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEEVLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLSQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSTIRERLWPLLEQARTRHAKVDALATQPLRERVNALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQAEAFQARLKGWFEPLVEDMQRQWAVLVEKVQAAVGTSPTTPPVETK	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
Q9GLM8	MKVLWAALLVTFLAGCQAKVEQAVETEPEPELHQQAEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVRGRLAQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAMGTSAAPVPSDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUY9	MKALWAVLLATLLTGCLSEGEPEVTEQLSWQSDQPWEQALNRFWDYLRWVQTLSDQVQEELQNSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLAQYRNEVHTMLGQSTEELRSRLSSHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGVAQPLRDRAQALGDRLRGRLEEVGNQARDRLEEMREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPLVEDMQRQLANLVEKIQASTNSVLSTSVPQENQ	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
G5CBM7	MKALWAVLVVTLLAGCRADVQPELEMQEPALWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLNSQVTQELTVLMEDTMKEVKAYKNELEEELGPVAEDTKARLSKELQGAQARLRADMEEVRNRLAHYSEEMQVMLGQSPDELRARLGSHLRKLRKRLLRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGSLVEQSRVRAALTGQPLRERAQAWGERLRGRLEEVGGRARDRLDEVREQMEEVRAKVEEQAEAFQARLKGWFEPMMEDMRRQWADLIEKVQLAVGASTPVPSEDH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
Q9P2S4	MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:6860692, PubMed:1911868, PubMed:14754908). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:6860692, PubMed:2762297, PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:14754908, PubMed:23620513). Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:6860692, PubMed:2762297, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:6860692, PubMed:1911868). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:2762297, PubMed:1917954, PubMed:7768901, PubMed:8939961, PubMed:12950167, PubMed:20030366, PubMed:2063194, PubMed:8756331, PubMed:20303980, PubMed:1530612, PubMed:7635945). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:9395455, PubMed:9488694, PubMed:23676495, PubMed:7635945). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:23676495, PubMed:29516132). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:2762297, PubMed:1917954, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:9395455, PubMed:14754908, PubMed:23620513). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:8939961, PubMed:25173806). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074). (Microbial infection) Through its interaction with HCV envelope glycoprotein E2, participates in the attachment of HCV to HSPGs and other receptors (LDLr, VLDLr, and SR-B1) on the cell surface and to the assembly, maturation and infectivity of HCV viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). Homotetramer (PubMed:8340399). May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs (PubMed:14754908). May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear (PubMed:8367470, PubMed:23620513). May interact with MAPT (PubMed:7972031). May interact with MAP2 (PubMed:7891887). In the cerebrospinal fluid, interacts with secreted SORL1 (PubMed:30448281). (Microbial infection) Interacts with hepatitis C virus (HCV) envelope glycoprotein E2; this interaction is required for HCV infectivity and production. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner (PubMed:9488694). Lipidation induces the release from the extracellular matrix (PubMed:9488694). Produced by several tissues and cell types and mainly found associated with lipid particles in the plasma, the interstitial fluid and lymph (PubMed:25173806). Mainly synthesized by liver hepatocytes (PubMed:25173806). Significant quantities are also produced in brain, mainly by astrocytes and glial cells in the cerebral cortex, but also by neurons in frontal cortex and hippocampus (PubMed:3115992, PubMed:10027417). It is also expressed by cells of the peripheral nervous system (PubMed:10027417, PubMed:25173806). Also expressed by adrenal gland, testis, ovary, skin, kidney, spleen and adipose tissue and macrophages in various tissues (PubMed:25173806). APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma (PubMed:29516132). The extent of glycosylation and sialylation are tissue and context specific (PubMed:29516132). Plasma APOE undergoes desialylation and is less glycosylated and sialylated than the cellular form (PubMed:2498325, PubMed:19838169, PubMed:20511397, PubMed:23234360). Glycosylation is not required for proper expression and secretion (PubMed:2498325). O-glycosylated with core 1 or possibly core 8 glycans. Thr-307 and Ser-314 are minor glycosylation sites compared to Ser-308 (PubMed:19838169, PubMed:23234360). Glycated in plasma VLDL of normal subjects, and of hyperglycemic diabetic patients at a higher level (2-3 fold). Phosphorylated by FAM20C in the extracellular medium. Undergoes C-terminal proteolytic processing in neurons. C-terminally truncated APOE has a tendency to form neurotoxic intracellular neurofibrillary tangle-like inclusions in neurons. There are three common APOE alleles identified: APOE2/APOE-epsilon2/E2, APOE3/APOE-epsilon3/E3, and APOE4/APOE-epsilon4/E4. The corresponding ApoE2, ApoE3 and ApoE4 isoforms differentially present Cys and Arg residues at positions 130 and 176. The most common allele in the human population is APOE3 which sequence is the one displayed in that entry with a Cys at position 130 and an Arg at position 176. Common APOE variants influence lipoprotein metabolism in healthy individuals. Additional variants have been described and are described relative to the three common alleles. Allele APOE4 is strongly associated with risk for severe COVID-19, increases susceptibility to SARS-CoV-2 infection in neurons and astrocytes (PubMed:33450186). The disease is caused by variants affecting the gene represented in this entry. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD. Disease susceptibility is associated with variants affecting the gene represented in this entry. The APOE4 allele (APOE form E4) is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE4 participates in pathogenesis is not known. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Binds to and activates LILRB4 on acute myeloid leukemia (AML) cells which leads to suppression of T cell proliferation and promotion of AML cell migration and infiltration. Belongs to the apolipoprotein A1/A4/E family. Apolipoprotein E entry Tangled - Issue 83 of June 2007
P0DUZ0	MKILWAALVLTLLAGCRADVEPEVEVRETAVWQSGQPWELALSRFWDYLRWVQTLSDQVQEELLSSQVTQELTLLMEDTMKELKAYKSELEKEVGPMAEDTKARLSKELQGAQARLAGDMEEVRNRLSQYRSEVQAMLGQSSEELRARLASHLRKLRKRLQRDAEELQKRLAVYKAGAQEGAERGVSAIRERLGSLMEQGRLQALTSHPLRERAQAWGEQVRGRLEKVGSQARDRLEEVREQMEEVRVKVEEQTEAFQARLKSWFEPMVEDLRRQWAELIEKVQVAVGASTSPPSQKS	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
Q9GLM6	MKVLWAALLVTFLAGCQAKVEQAVEPEPEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYRSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVRGRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEVGGRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUZ1	MKVLWAVLVVTLLAGCQADVEPALEVGEPAPEVREPAMWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKEVKAYKSELEQELGPMAEDTKARLSKELQAAQARLGADMEEVRNRLTQYRSEVQTMLGQSAEELRARLASHLRKLRKRLLRDAEDLQKRLAVYKAGAQEGAERGVSAIRERLGSLVEQGRLRAAQTSQPLRERAQAWGERLRGRLEEVGGQARDRLDVVREQMEEVRAKVEEQAEAFQARLKGWFEPVVEDMRRQWAELIEKVQVAVGASTPAPSEKH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUZ2	MKVLWAVLVVTLLAGCQADVEPALEVGEPAPEVREPAMWQSGQPWELALGRFWDYLRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKEVKAYKSELEQELGPMAEDTKARLSKELQAAQARLGADMEEVRNRLTQYRSEVQTMLGQSAEELRARLASHLRKLRKRLLRDAEDLQKRLAVYKAGAQEGAERGVSAIRERLGSLVEQGRLRAAQTSQPLRERAQAWGERLRGRLEEVGGQARDRLDVVREQMEEVRAKVEEQAEAFQARLKGWFEPVVEDMRRQWAELIEKVQVAVGASTPAPSEKH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DML8	MKVLWVALVITLLAGCQAEVEPEPEPEVQLGQEWPGWQDSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLAPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P10517	MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEGQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPIDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
G7NMA9	MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEGQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLARLGPLVEQGRVRAATVGSLASQPLQERAQAKLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DO94	MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEGQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUZ3	MKALWAVLLVTLLTGCLAEGEPEVADELAWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSSEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKSGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQALGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPLLEDMQRQWANLVEKIQASVATNPITSTPMPEEN	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUZ4	MKALWAVLVVTLLAGCLAEGDPELEPEVTDQLGWQTNQPWEQALGRFWDYLRWVQTLSDQVQQELQTSQVTQELTVLMEDTMTELKAYKKELEEQMGPMAEETRARLAKEVQAAQSRLGADMEDLRNRLGLYRNEVQTMLGQSTEELRARLTTHLRKLRKRLMRDAEDLQKRLAVYKAGAREGAERGVGAIRERLGPLVEQGRQRTANLGAGAAQPLRERAQALGARIRGRLEEVGNQARDRLEEVREQMEEVRAKVEEQAQQMRLQAEIFQTRLKGWFEPLVEDMQRQWANLMEKIQASVATNPIPPSSVPQESQ	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P08226	MKALWAVLLVTLLTGCLAEGEPEVTDQLEWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTALMEDTMTEVKAYKKELEEQLGPVAEETRARLGKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQAFGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPIVEDMHRQWANLMEKIQASVATNPIITPVAQENQ	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (By similarity). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:23676495). Homotetramer (By similarity). May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs (By similarity). May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear (By similarity). May interact with MAPT (By similarity). May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1 (By similarity). In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. APOE knockout mice display severe hypercholesterolemia associated with impaired clearance of dietary fats (PubMed:1423598). Excess cholesterol is more particularly associated with the atherogenic very low and intermediate density lipoproteins in the plasma (PubMed:1423598). These mice are therefore prone to atherosclerosis (PubMed:1423598). Mice lacking both Cx3cr1 and Apoe show decreased atherogenesis (PubMed:12569158). Animals with a double knockout of APOE and CD36, fed a Western diet for 12 weeks, exhibit much lower levels of CXCL1, CXCL2 and CCL5 mRNA expression in the descending aorta and a corresponding decrease in atherosclerotic lesion formation, compared to APOE single knockout mice (PubMed:23812099). Animals with a double knockout of APOE and TLR4 or TLR6 also have less aortic plaque formation than single knockout mice. All 3 double knockout show lower serum concentrations of IL1A, ILB and IL18 (PubMed:20037584). Belongs to the apolipoprotein A1/A4/E family.
P0DUZ5	MKALWAVLLVTLLAGCLAEGEPEVTDQLEWQSSQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSALRERLGPLVEQGRQRTANLGAGAAQPLRDRAQAFGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPIVEDMHRQWANLMEKIQASVATNPIISTPMPQENQ	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
A0A2Y9GHM3	MKVLWAALVVALLAGCWADVEPESPLQGKPEPELEPELEPKRELEQEVEAEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEDMLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLTQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSSIRERLWPLLEQARTRHANLATQPLRERVDALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQVEAFQARLKSWFEPLVEDMQRQWAGLVEKVQVAVGTSPTTPPLETK	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
A0A6P6DKR7	MKVLCTVLVVTLLAGCRADVEPEPEVLEPAVWKSGQPWELALGRFWDYVRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKAVKAYKSELEQELVPMAEDTKARLSKELQAAQARLGADMEEVRNRLAQYRNEMQAMLGQSADELRARLASHLRKLRKRMLRDAEDLQKRLAVYKDGASEGAERGVSAIRERLGSLVEQSRVRAALTGQPLQERAQAWGKQLRGRLEEVRGQAQDRLEEMREQMEEVRVKIEEQAEAFQTRLKGWFEPMVEDMRRQWADLIEKVQAAVGASTPVPSQKP	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
P0DUZ6	MKALWAVLVVTLLAGCLAEGEPELEPEVTDRLAWQSGQPWELALGRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTELKAYKKELEEQLGPMAEETRARLAKEVQAAQSRLGADMEDLRNRLGQYRNEVQTMLGQSTEELRARLSTHLRKLRKRLMRDAEDLQKRLAVYKAGAREGAERGVGAIRERLGPLVEQGRQRTANLGAGAGKPLQDRAQALGARIRGRLEEVGNQARDRLEEVREQMEEVRAKVEEQAQQMRLQAEIFQARLKGWFEPLVEDMQRQWANLVEKIQASVAANPIPPSSVPQESQ	APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. Homotetramer. May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear. May interact with MAPT. May interact with MAP2. In the cerebrospinal fluid, interacts with secreted SORL1. In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. Glycated in plasma VLDL. Phosphorylated by FAM20C in the extracellular medium. Belongs to the apolipoprotein A1/A4/E family.
B1YJG1	MEFKQHIKEVENWPKEGISFKDITSLMQNGPAYKQSVDALIDYARKQGADVIAGPEARGFVVGCPAAYAMEIGFVPVRKEGKLPRETVRVEYGLEYGKDVLTMHHDAIQPGQRVVILDDLLATGGTIEATIKMIEQLGGTVAGIGFLIELDGLGGREKLEGYDILSLIRYAD	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
C4L531	MDFKQHIKEVADYPKEGISFKDITSLMQNGEVYKKSVDELVAYARERGAELIAGPEARGFVVGCPAAYALELGFVPVRKEGKLPRETVRVSYGLEYGTDILTMHKDSIQPGQQVVILDDLLATGGTIEATIKMIEQLGGVVAGIGFLIELDGLGGRERLEGYDVFSLIRYED	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A7HLE2	MELKNFIRDIPDFPQKGVMFRDITPLVKNPEAFKYAIDTIAEELGKYDFDLIVCPEARGFIIAAPLAYKLDKGLVPVRKPGKLPYKTISDVYELEYGKAELHMHEDAIQPNQKVVIIDDVLATGGTAMALKRLVEKAGGIVVASAFLIELTYLNPRNIIKDLPIIAPIKY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B0S0M3	MELKEKIRVIDGFPKEGISFKDITTLLNDKDAYKYAVDLMVDDLKDKGITAIAAPEARGFLFGSAVAYALGVRFIPVRKPGKLPGEVSEYSYDLEYGTDKLEVHRDAIKKGDKVAIVDDLLATGGTVNAVAKLIEKNGGEITAMEFLIELTELGGRDINKNYYINTLVQYES	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A5FFL9	MKIENYIRDIQGFPKEGILFKDITPLLNNVEARQECLSILVNSLKGQKIDKVVGAESRGFFFGMLLAQELKAGFIPVRKPKKLPFDIISASYELEYGTDSLEMHIDAIKKGDRVLIHDDVLATGGTAKAVCELVEKLGGEIVQCNFLMELTFLNGRKKIKEYPVFAALTY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q0RNU1	MTSIDEAAPGRSAASDAAADVLRGHIRDIQDWPQPGVVFKDITPLLSTPAAFGVVVGALVDVARERGATTIAGIEARGFLLAAPVADRLGAALVPIRKQGKLPGPTRSATYDLEYGTATIEIHADAVRPDERVLLVDDVLATGGTAAAAHGLLAGVGAEVVGLAVLMELSFLPGRERVAPLDVVPLLTI	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q2JD90	MTSIDDAPQRSAAHDAVAEVLRGHIRDIPDWPQPGVVFKDITPLLATPTAFGVVIGALADAARALGATTIAGIEARGFLLAAPVADRLGTGLVPIRKQGKLPGPTRSASYDLEYGAATIEIHADAVHDGDRVLLVDDVLATGGTAAAAHSLLAAGGGEVVGLAVLMELSFLPGRDRVAPLDVVSLLTI	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B0TWU0	MNLDFIKDRIVAVPDFPKPGIVFRDITPLLADPQGLKMTAKAMAEELKSKGIKPTVIAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRETYKVSYQLEYGSDSLEIHKDAFKPTDKVLVVDDLLATGGTAKATVQLIEKTQASVAGLIFVIELEDLNGRKVLEGHNVSALVKY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A8KZE2	MTSVDSQPDLSAAEAVLGAHVRDVMDFPKPGVVFKDITPLLSTPAAFGVVVGALADLARGLGATTIAGIEARGFLLAAPVADRVGAGIVPIRKQGKLPGRTRSEAYALEYGTAVLEIHEDAVPTGERVLIVDDVLATGGTAAAAHTLLRGCGADVVGLAVLMELTFLSGRDRTGTLDVTSIMKI	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q14JZ2	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIVAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDGLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A7NEG0	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIIAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDSLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q2A1J5	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIIAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDSLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B2SEZ5	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIVAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDGLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A0Q8C6	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIVAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDGLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q0BK98	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIIAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDSLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q5NII9	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIVAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDGLGGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A4IW38	MNLDFIKSKIAAVPDFPKPGIMFRDITPLLADPQGLRKTAEAMAQELKNKGIQPTIVAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRATYSVKYDLEYGSDSLEIHQDAFKVTDEVLVVDDLLATGGTAKATVDLIEKTQAKVAGLIFVMELDGLSGREVLAGYNVSALIKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q8RDM9	MDLKNYVASIENYPKEGIIFRDITPLMNDGEAYKYATEKIVEFAKDHHIDIVVGPEARGFIFGCPVSYALGVGFVPVRKPGKLPREVIEYAYDLEYGSNKLCLHKDSIKPGQKVLVVDDLLATGGTVEATIKLVEELGGVVAGLAFLIELVDLKGRERLDKYPMITLMQY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B9M4Z1	MEELKSIIRDIPDFPKKGIIFKDITTLLSDAASYQRMIDLLSHRYIGKRIDKVVGVEARGFIIGAALAYKLGAGIVLVRKPGKLPSETFKKTYDLEYGTDTLEMHTDAIKKGERVLIADDLLATGGTMSAVVDMVDSMGGELVECCFMAELEFLNGRTKLPVERVFSLLKF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q5KWS2	MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIEIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDILTLMQF	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A2BRV3	MKKLEDLILTYKDFPKKGIEFKDVLEILQYPDIFQDIILKMSSNQFLKKAEAIISIDARGFIFGSAVALESSKPMIVARKPGKLPGQLLTREYDLEYGKNSLSIQVNALKKFNSFVIVDDLLATGGTVKSVSRLIRDQKKKILGLITVVELKSLKGKSKLDFPVHSIVTL	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q46KW1	MDHLKKYITEINDYPKKGIVFKDLNPIYKEPKIWKELMFPLQNLISTKKPDYIAGIESRGFISASALAFKLEIGLITIRKPNKLPGEVIGTNYKLEYGEDRLEIQQNIMEKDSKIMLFDDLLATGGTAGAAGNLIKKAGGNLIGYAFLVELTELKGRENLDSNLFVETLIKY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q48GH3	MTFDQSNFKSLIRPVIDFPKPGVVFRDITPLFQSPKATRQVIDSFVQRYIEADFSHIGVMDARGFLIGSVVAYQLNKPLVLFRKQGKLPADVLSEAYQTEYGEAYLEVHADSLCEGDSVIMFDDLIATGGTLIAAANLIRRMGAEVHEAVAIIDLPELGGSKRLNDLKIPTFCLTEFALDEQ	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q15RT2	MPAAYIKSVIKTVPDYPKPGILFRDVTSILEDHKAYTTSIELLVKEFAPYNFDKVAGTEARGFLFGAPLAIELGIGFIPVRKPNKLPRKVISESYDLEYGTDCLEIHEDAVKPGEKVLMLDDLLATGGTMIATANLIRRLGGIVEHAGFVISLPDLGGEAKLQEIGVQSHSICEFEGE	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A6V7V8	MIFDEFTLKSQIRAVPDFPKAGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLILFRKQGKLPADVLAEAYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGIATFSLTAFALDER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B7UVH9	MIFDEFTLKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGISTFSLTAFALDER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q02K26	MIFDEFTLKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGISTFSLTAFALDER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q04633	MIFDEFTLKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGISTFSLTAFALDER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q1ICH9	MYSDTFDLKALIRPVVDFPKPGVIFRDITPLFQSPRGLRYVADQFIERYVEADFTHIGAMDARGFLIGSIIAHQLNKPLILFRKQGKLPADVLSEGYQTEYGEAFLEVHADSLCDGDSVLIFDDLIATGGTLLAAANLVRRTGAKVFEAAAIIDLPELEGSRRLQAAGVPTFCLTEFSLSEY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q4KFF5	MAFDSFDIKSLIRPVIDFPKPGVIFRDITPLFQSPRALRLVADSFAQRYVEEDFSHIGAMDARGFLIGSIIAYQLNKPLILFRKQGKLPADILAEGYRTEYGEAFIEVHADSLCEGDSVLLIDDLIATGGTLIAAANLVRRMGAKVYEAAAIIDLPELGGSQKLQDMGIPTFCLTQFSLTER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
C3K148	MTFDSFDIKSLIRPVIDFPKPGVIFRDITPLFQSPRALRLVADSFAQRYVEADFTHIGAMDARGFLIGSIIAYQLNKPLILFRKQGKLPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLMFDDLIATGGTLIAAANLVRRMGAKIFEAAAIIDLPELGGSQRLEEMGIPTFCLTQFALTER	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A8F7S9	MDLRKFIRDIPDFPFEGIIFRDVTPLLKNPQAFQAAIDKMAETVSDIDFDLIVAPEARGFIFGSALAYKLHKGFIPVRKPGKLPYETTSIEYDLEYGTAKLQIHSDAIDKGEKILLVDDVLATGGTANAIAQLVKKLGGEVAGTCFLVELTYLNPRERLRDYLIRTVISY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A4XVK6	MIFDEFSIKTLIRPVPDFPKPGVVFRDITPLFQSPRALRMVADSFIQRYVEAEFSHIGAMDARGFLIGSIIAYELNKPLILFRKQGKLPADVLSESYQTEYGEAFLEVHSDSLCEGDSVLIFDDLIATGGTLIAAANLVRRMRASVFEAAAIIDLPELGGSQKLQDAAIPTFTLTAFALDDR	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
A5W0U8	MHSDAFDLKALIRPVVDFPKPGVIFRDITPLFQSPRGLRYVADQFIERYVEAEFSHIGAMDARGFLIGSIIAHQLNKPLILFRKQGKLPADVLSEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAANLVRRTGAQVFEAAAIIDLPELDGSRRLQAAGVPTFCLTEFSLSEY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q3KFA3	MVFDSFDIKSLIRPVIDFPKPGVIFRDITPLFQSPKALRLVMDSFAHRYVEADFTHIGAMDARGFLIGSVLAYQLNKPLVLFRKQGKLPADVLAEGYATEYGEAFLEVHADSLCEGDSVVMFDDLIATGGTLIAAANLIRRMGARVHEAAAIIDLPELGGSQRLEDMGIPTFCLTQFALTDK	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B0KPW6	MHSDAFDLKALIRPVVDFPKPGVIFRDITPLFQSPRGLRYVADQFIERYVEAEFSHIGAMDARGFLIGSIIAHQLNKPLILFRKQGKLPADVLSEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAANLVRRTGAQVFEAAAIIDLPELDGSRRLQAAGVPTFCLTEFSLSEY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q88F33	MHSDAFDLKALIRPVVDFPKPGVIFRDITPLFQSPRGLRYVADQFIERYVEAEFSHIGAMDARGFLIGSIIAHQLNKPLILFRKQGKLPADVLSEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAANLVRRTGAQVFEAAAIIDLPELDGSRRLQAAGVPTFCLTEFSLSEY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
B1JBZ0	MHSEAFDLKALIRPVVDFPKPGVIFRDITPLFQSPRGLRYVADQFIERYVEAEFSHIGAMDARGFLIGSIIAHQLNKPLILFRKQGKLPADVLSEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAANLVRRTGAQVFEAAAIIDLPELDGSRRLQAAGVPTFCLTEFSLSEY	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Q884U6	MTFDQSNFKSLIRPVVDFPKPGVVFRDITPLFQSPKATRQVIDSFVQRYIDADFSHIGVMDARGFLIGSVVAYQLNKPLVLFRKQGKLPADVLSEAYQTEYGEAYLEVHADSLCEGNSVIMFDDLIATGGTLIAAANLIRRMGAQVHEAAAIIDLPELGGSKRLNDLNIPTFCLTEFALDEQ	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
P47202	MIFDEFSIKTLIRPVQDFPRPGVVFRDITPLFQSPKALRMVADSLIQRYVEADFTHIGALDARGFLVGSILAYELNKPLVLFRKQGKLPADVLSQAYSTEYGEAHLEIHADSLCEGDSVLLFDDLIATGGTLLAAAQLVRRMRANIHEAAAIIDLPELGGSQKLQDIGIPTFTLTAFALSDR	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family.
O49676	MVFGRITELFTAASSRLPAGSQSSVPYMPTGSSPDVGTSVSDSISIGNGGRKNCLRHSASLQDFSSYHGFDPEESILPREAISWGQNGSSFSKEKGSVPNGTNPSTRRKLIRAVMIVMCLFLFAFLVYIVSMYIYTNWSRGASRYYVVFDCGSTGTRAYVYQASINYKKDSSLPIVMKSLTEGISRKSRGRAYDRMETEPGFDKLVNNRTGLKTAIKPLIQWAEKQIPKNAHRTTSLFVYATAGVRRLRPADSSWILGNVWSILAKSPFTCRREWVKIISGTEEAYFGWTALNYQTSMLGALPKKATFGALDLGGSSLQVTFENEERTHNETNLNLRIGSVNHHLSAYSLAGYGLNDAFDRSVVHLLKKLPNVNKSDLIEGKLEMKHPCLNSGYNGQYICSQCASSVQGGKKGKSGVSIKLVGAPNWGECSALAKNAVNSSEWSNAKHGVDCDLQPCALPDGYPRPHGQFYAVSGFFVVYRFFNLSAEASLDDVLEKGREFCDKAWQVARTSVSPQPFIEQYCFRAPYIVSLLREGLYITDKQIIIGSGSITWTLGVALLESGKALSSTLGLKSYETLSMKINPIALISILILSLLLLLCALSRVSNCLPRFFRKSYLPLFRHNSTSASSVLNIPSPFRFQRWSPMSTGVKTPLSPTVRGSPRRPFSFGSSIQLMESSLYSSSSCVMHSCSSDSLGDIQYDSTGSFWSSPRRSQMRLQSRRSQSREDLSSSLADSHMLKM	Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (By similarity). Involved in the regulation of pollen and anther development. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate Detected in mature pollen grains. Also expressed in more diverse tissues such as roots, leaves, stems, pistils and sepals. More particularly expressed in the vascular bundle. By wounding and drought stress. No visible phenotype. Apy6 and dapy7 double mutant exhibits late anther dehiscence and low male fertility. Pollen grains of double mutant are largely deformed in shape and in most cases, the cell walls of the pollen grains are interconnected. Belongs to the GDA1/CD39 NTPase family. The predicted gene has been split into 2 genes: At4g19180 and At4g19185. The predicted gene has been split into 2 genes: At4g19180 and At4g19185.
Q5B865	MALHRLKGHGANVGNRVGIQLDKDFVLFQGSEQEALAVYLSGILSLRLKETTTIKYIRLHLRGVRRVSSDTQSSLPARTGRKRFCSENEFYSRTWNFFDGYREAPMTVPAGEYKYPFDVVMEGSLPASVEGMKEASISYLFTVEIGRRHGRDITFDKPLRVIRVPDLEPCSHDFALDEVWANKIAYRIGIQNRTVALGTRIDVDYVFAPLLRDMKIAFIESQLLEVRDLSVEPNDGGSAHAARTETIVCSDRYTLGEEYSSKALESYQFSRTLQLPQALGHCVQDTEDMGVRVSHKLKIHVRMHNPDGHESELRLAIPVLIYLSPYYRVWEDSFCGETIPLPETLNPSDECPPAYGMHELDQLYMPQD	May be involved in signaling by recognizing appropriately phosphorylated substrates via its arrestin domains and then recruit a HECT-type ubiquitin ligase such as hulA, leading to ubiquitination of the substrate, providing a link between ubiquitination and phosphorylation in protein regulation and stability. Interacts with hulA. Belongs to the arrestin family.
P83481	VYINKLTPPCGTMYYACEAV	Has antiviral activity against Tobacco mosaic virus and antitumor activity against stomach cancer cells in vitro.
Q176L2	MAGRPGYSEVIFLYVVSVAVIARATDNMPVNKDVSKLFPLTLIHINDLHARFEETNMKSNVCTQKDQCIAGIARVYQKIKDLLKEYESKNPIYLNAGDNFQGTLWYNLLRWNVTADFIKKLKPAAMTLGNHEFDHTPKGLAPYLAELNKEGIPTIVANLVMNNDPDLKSSKIPKSIKLTVGKRKIGIIGVLYDKTHEIAQTGKVTLSNAVEAVRREAAALKKDNIDIIVVLSHCSYEEDKKIAAEAGDDIDVIVGAHSHSFLYSPDSKQPHDPKDKVEGPYPTLVESKNKRKIPIVQAKSFGKYVGRLTLYFDEEGEVKNWEGYPVFIDHKVQQDPQILKDLVPWRAKVEAIGSTVVGETMIELDRDSCRDQECTLGVLYADGFADQYTNDTFRPFAIIQAGNFRNPIKVGKITNGDIIEAAPFGSTADLIRLKGADIWDVAEHSFALDDEGRTNCLQVSGLRIVIDISKPVRSRVKKIEVMDYTNPKSDKLKPLDKEAEYYIVVPSYLADGKDGFSAMKRATARRTGPLDSDVFKNYVEKIKKVDNLKLGRVIVCKGSKCT	Facilitates hematophagy by preventing ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate Salivary gland specific. Not detectable in females on the first day after eclosion, but is detectable on the second day. It is maximally expressed by day 4. The N-terminus is blocked. Causes an allergic reaction in human. Belongs to the 5'-nucleotidase family.
Q5MIX3	MAGKPGIQLFVIFLLLSSFAAVVWAMDNMPADKDVSKLFPLTLIHINDLHARFDETNMKSNACTAKDQCIAGIARVYQKIQDLLKEYKSKNAIYLNAGDNFQGTLWYNLLRWQVTADFITKLKPTAMTLGNHEFDHTPKGLAPYLAELDKAGIPTLVANLVMNDDPDLKSSKIQKSIKVTVGGKTIGIIGVLYDKTHEIAQTGKVTLSNAVETVKREAAALKKDKVDIIVVLSHCSYDEDKKIAKEAGQDIDVIVGAHSHSFLYSKESNKPYDQKDKIEGPYPTIVESNNKRKIPIVQAKSFGKYVGRLTLYFDNEGEVKHWEGYPEFIDNKVKQDPKILEALIPWRKKVQEIGSTKVGETTIELDRDSCRDKECTLGVLYADAFADHYTNSSFRPFAIIQAGNFRNPIKVGKITNGDIIEAAPFGSTADLIRLKGDNLWAVAEHSLALDDENRTNCLQVSGLRIVIDPSKSVGSRVVKIDVMDNRNPKSEDLKPLDRNAEYFIALPSYLADGKDGFSAMKEATARWTGPLDSDVFKSYVEKIKKVDKLKLDRVIVCKAGSPCT	Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood. Platelet aggregation was inhibited by 6% when 0.4 uM recombinant apyrase was added and by 9.5% when the concentration of recombinant apyrase was 0.8 uM. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate Salivary gland specific. Causes an allergic reaction in human. Belongs to the 5'-nucleotidase family.
F6C6C1	MSESTYPSVKDLTLEEKASLTSGGDAWHLQGVESKGIPGYMITDGPHGLRKSLASSAGETDLDDSVPATCFPPAAGLSSSWNPELIHKVGEAMAEECIQEKVAVILGPGVNIKRNPLGGRCFEYWSEDPYLAGHEAIGIVEGVQSKGVGTSLKHFAANNQESDRLRVDARISPRALREIYFPAFEHIVKKAQPWTIMCSYNRINGVHSAQNHWLLTDVLRDEWGFEGIVMSDWGADHDRGASLNAGLNLEMPPSYTDDQIVYAVRDGRITPAQLDRMAQGMIDLVNKTRAAMSIDNYRFDVDAHDEVAHQAAIESIVMLKNDDAILPLNAGPVANPSAMPQKIAVIGEFARTPRYQGGGSSHITPTKMTSFLDTLAERGIKADFAPGFTLDLEPADPALESEAVETAKNADVVLMFLGLPEAAESEGFDRDTLDMPAKQITLLEQVAAANQNVVVVLSNGSVITVAPWAKNAKGILESWLLGQSGGPALADVIFGQVSPSGKLAQSIPLDINDDPSMTNWPGEEGHVDYGEGVFVGYRYYDTYGKAVDCPFGYGLSYATFEITGVAVAKTGANTATVNATVTNTSDVDAAETVQVYVAPGKADVARPKHELKGFTKVFLKSGESKTVTIDLDERAFAYWSEKYNDWHVESGEYAIEVGTSSRDIAETVTVALEGDGKTQPLTEWSTYGEWEADPFGAKIVAAVAAAGEAGELPKLPDNAMMRMFLNSMPINSLPTLLGEGGKKIAQFMVDEYAKLSK	Catalyzes the hydrolysis of a non-reducing terminal alpha-L-arabinopyranosidic linkage in ginsenoside Rb2 (alpha-L-arabinopyranosyl-(1->6)-alpha-D-glucopyranosyl) to release alpha-D-glucopyranosyl (Rd). It is not able to hydrolyze alpha-L-arabinofuranosyl-(1->6)-alpha-D-glucopyranosyl (Rc). Completely inhibited by Cu(2+) and Fe(2+). Optimum pH is between 5.5 and 6. Optimum temperature is 40 degrees Celsius. Homotetramer. Belongs to the glycosyl hydrolase 3 family.
E7CY69	MSESTYPSVKDLTLEEKASLTSGGDAWHLQGVESKGIPSYMITDGPHGLRKSLASSAGETDLDDSVPATCFPPAAGLSSSWNPELIHKVGEAMAEECIQEKVAVILGPGVNIKRNPLGGRCFEYWSEDPYLAGHEAIGIVEGVQSKGVGTSLKHFAANNQETDRLRVDARISPRALREIYFPAFEHIVKKAQPWTIMCSYNRINGVHSAQNHWLLTDVLRDEWGFDGIVMSDWGADHDRGASLNAGLNLEMPPSYTDDQIVYAVRDGLITPAQLDRMAQGMIDLVNKTRAAMSIDNYRFDVDAHDEVAHQAAIESIVMLKNDDAILPLNAGPVANPSATPQKIAVIGEFARTPRYQGGGSSHITPTKMTSFLDTLAERGIKADFAPGFTLDLEPADPALESEAVETAKNADVVLMFLGLPEAVESEGFDRDTLDMPAKQIALLEQVAAANQNVVVVLSNGSVITVAPWAKNAKGILESWLLGQSGGPALADVIFGQVSPSGKLAQSIPLDINDDPSMLNWPGEEGHVDYGEGVFAGYRYYDTYGKAVDYPFGYGLSYATFEITGVAVAKTGANTATVTATVTNTSDVDAAETVQVYVVPGKADVARPKHELKGFTKAFLKAGESKTVAIDLDERAFAYWSEKYNDWHVEAGEYAIEVGVSSRDIADTVAVALDGDGKTQPLTEWSTYGEWEADPFGAKIVAAVAAAGEAGELTKLPDNAMMRMFLNPMPINSLPTLLGEGGKKIAQFMLDEYAKLSK	Catalyzes the hydrolysis of a non-reducing terminal alpha-L-arabinopyranosidic linkage in ginsenoside Rb2 (alpha-L-arabinopyranosyl-(1->6)-alpha-D-glucopyranosyl) to release alpha-D-glucopyranosyl (Rd). It is not able to hydrolyze alpha-L-arabinofuranosyl-(1->6)-alpha-D-glucopyranosyl (Rc). Completely inhibited by Cu(2+) and activated by Co(2+). Optimum pH is 6.8. Optimum temperature is 48 degrees Celsius. Homotetramer. Belongs to the glycosyl hydrolase 3 family.
O96559	MRSSYRVGNPIRFQPTNVVGLLLLSLVLSFMLVQSYELGHASGETNANSKYPLTTPVEENLKVRFKIGVISDDDKNAVSKDESNTWVSTYLTGTLEWEKSTDKITVQWDKGNEKKVKSKYSYGGRGMELSELVTFNGNLLTFDDRTGLVYILKDDKVYPWVVLADGDGKNSKGFKSEWATEKAGNLYVGSSGKEWTTKEGTIENYNPMWVKMINKNGEVTSLNWQTNYEKIRSSMNITFPGYMWHEAACWSDKYNKWFFLPRALSQEAYDSKKFETQGANVIISCDDKFEKCEPTQIQGKTEDKRGFSNFKFVPTSEDKIIVGLKTVEADDTTETYFTAFDLEGKVLLEETKIDDHKYEGVDFV	Inhibits platelet aggregation by the calcium-dependent hydrolysis of ATP and ADP. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate Belongs to the apyrase family.
Q43164	MLNQNSHFIFIILAIFLVLPLSLLSKNVNAQIPLRRHLLSHESEHYAVIFDAGSTGSRVHVFRFDEKLGLLPIGNNIEYFMATEPGLSSYAEDPKAAANSLEPLLDGAEGVVPQELQSETPLELGATAGLRMLKGDAAEKILQAVRNLVKNQSTFHSKDQWVTILDGTQEGSYMWAAINYLLGNLGKDYKSTTATIDLGGGSVQMAYAISNEQFAKAPQNEDGEPYVQQKHLMSKDYNLYVHSYLNYGQLAGRAEIFKASRNESNPCALEGCDGYYSYGGVDYKVKAPKKGSSWKRCRRLTRHALKINAKCNIEECTFNGVWNGGGGDGQKNIHASSFFYDIGAQVGIVDTKFPSALAKPIQYLNAAKVACQTNVADIKSIFPKTQDRNIPYLCMDLIYEYTLLVDGFGLNPHKEITVIHDVQYKNYLVGAAWPLGCAIDLVSSTTNKIRVASS	Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate The N-terminus is blocked. Belongs to the GDA1/CD39 NTPase family.
B3A0N5	MFKITVFIYVLQLILPSKVHSSPVPDSDNGLREFPLSIVHINDFHARFEQTDELGGQCKPTAKCVGGYARLVTTVKKLKEEGQNTIFLNAADNYQGTLWYNLGKWNVTAYFMNLLPADAMTLGNHEFDDKIEGIVPFLEVIKTPIVVANIDDSLEPTFKGKYTKSVVLERGGRKIGIVGVIAQNTDNISSPGKLRFLDEIQSVKNESKRLREEEKVDIVIVLSHIGLDHDYDLAEQAGDYIDAIIGGHSHSFLWTGDNPPGKEKVVDAYPVEIVQTSGKKVLIVQASAFARYVGNITLYFGENNNLIRYAGAPVYLDSDVPEVPQIVEEMKAWEEFVHEKGNEIIAESRVVLSRENCRVSDCNIGNFFTDAYVHEYVTSHTGPYWTPVSVGLMNVGGIRASVDRGNITFSQLITMAPFENTVDTFDLSGKHLLEAFEHAVTVPNRLGFNGQNMLQVSGVKLVYDVTKCEGQRVVSAKIRCQKCDIPKYEPLDPEETYRIVTASFLANGGDGFTMIRDNKKNYKVGRKDYDVLINYAKYSSPITIGEEGRIRIIQ	Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity. May reduce probing time by facilitating the speed of locating blood. a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate Salivary gland specific. Causes an allergic reaction in human. Binds to IgE. Belongs to the 5'-nucleotidase family.
W5X2N3	MGWVWKDDDEQGGHVNPSAADISPRLDGDRCSTRKVVRTQCKTEEVEPGKFIRKCEKTEEVLRDCVGRPIEVVQSNKEYTEDDVTDQVMKGSVSFGSADNGAFNFPGLQHDIDEIEHNFLGGLSRFFEAAEDMKNGFFSSFGIPHIFDEGPSTSLPSPRREIPIDSPRQLEAFQKAYGTKSGEVDLSGLARDV	Interacts with FRAA1E, FRAA2 AND FRAA3.
B3EWK7	GSGASGSMPATTS	Up-regulated in CNS of active, non-hibernating snails suggesting involvement in the regulation of hibernation and maintenance of the active state.
Q8IXF9	MAGLNVSLSFFFATFALCEAARRASKALLPVGAYEVFAREAMRTLVELGPWAGDFGPDLLLTLLFLLFLAHGVTLDGASANPTVSLQEFLMAEQSLPGTLLKLAAQGLGMQAACTLMRLCWAWELSDLHLLQSLMAQSCSSALRTSVPHGALVEAACAFCFHLTLLHLRHSPPAYSGPAVALLVTVTAYTAGPFTSAFFNPALAASVTFACSGHTLLEYVQVYWLGPLTGMVLAVLLHQGRLPHLFQRNLFYGQKNKYRAPRGKPAPASGDTQTPAKGSSVREPGRSGVEGPHSS	Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. Restricted to the pancreas. Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily.
A4QPB9	MAGLNVSLSFFFATFTLCEAARRASKALLPVGAYEVFAREAMRTLVELGPWAGDFGPDLLLTLLFLLFLAHGVTLDGASANPTVSLQEFLMAEESLPGTLLKLAAQGLGMQAACTLTRLCWAWELSDLHLLQSLMAQSCSSALRTSVPHGALVEAACAFCFHLTLLHLRHSPPAYSGPAVALLVTVTAYTAGPFTSAFFNPALAASVTFACSGHTLLEYVQVYWLGPLTGMVLAVLLHQGRLPHLFQRNLFYGQKNKYRAPRGKPAPASGDTQTPAKGSSVREPGRSGVEGPHSS	Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily.
A0A0G3FWY4	MTANGDVRQPDARTYFTHQHPADYHADWKGYYERALVSRARSMERFAHELDIRYGTDPHQILNVFRAADTRSAPVIIYFHGGRWREGHPAFYDHLADTWAADGAVFVSAGYRLTPEHSIADSVADAWAVTDWVVRNIAAYGGDPSRITVAGHSSGGHLASMVALTDNCAVSIVGLVCMSAPVDLRTLGFWDDDTLSPHLQISRVPRRVVVSFGDPEPNRKGDDALRLTREGQMLADSLVAYGASLRTVVLPNADHVRTATAFADRQSPLFGAAHSVIFGDSTEDRSAPRSPHFQEEKQSCPE	Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid. H2O + N-octanoylanthranilate = anthranilate + H(+) + octanoate Up-regulated by PQS. Belongs to the AB hydrolase superfamily.
A0A0E4AET8	MFQTVTAPTGVWRGRVTGDVTVFHGIQYARADRFAPPQRCEPQLQHLVEVPEPGPIAPQSPSRLEGVMGAPSSLKQSEACLTVTVTTPHLAQPGSLPVLVWLHGGAFLSGSGAWEQYGAEQLVRETGIVVVSVNYRLGVLGYLCAPGISSGNLGLLDQITALEWVRDNIEAFGGDNGRVTLDGQSAGAHSIVAMLGIDRARSLFSRAIIQSAPLGLGFHSVEQARRAAEIFEEELGSDPRRAVVTDILAAQARTAHRLAGRGAMNSAPPFLPVHGMAPLPFVGEWNGKVAANAARRKILIGNTRDEMAAFFGPHPVFSAMRRVPLAGPQLAGAIQRRVQKVVFDNPVQEFADRFASAGASVWRYGIGPLHPDNPFGACHCIDIPLLFGDGDTWRDAPMLRPLSPKEIGESGTRTRRYWGEFVHTGRISDPAWPMHRPKSRYAHLLTDETIGGSA	Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid. H2O + N-octanoylanthranilate = anthranilate + H(+) + octanoate Up-regulated by PQS. Belongs to the type-B carboxylesterase/lipase family.
A0A0E4AFG7	MSGVAGHAEVVGGGIGGLSAAIALGKRGWTVRLHERNDEIRASGSGIYLWDNGLAALDYLGALDSTLVGAHFGARMQTRDAHNALVASSEVNRAGGPRVVTVARERLINALLASADAVGVEVVTGSTVTRVDAAGRIEFDNGHADADLIVVADGIGSRSRDQLGVKTRRRQLNQKCARVLLPREPGMVPSEWVDEYVTFYSGQRFLLYTPCSADLLYLALVCPSDDAPATGDPLPREAWIASFPQLAPLIDRIGPTPRWDEFEMLTLDSWSSGRVAILGDAAHAQPPSLGQGGGCAMLSALGLAHSLSKNYDLTTALGEWESSERSVIQRTQWFSYWLARANKLPDRPRSLLLSAAGHSSLYRNNRMRAALTTPTGITSSK	Could be involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to anthranilic acid. May catalyze the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4-quinolone). 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+) Up-regulated by PQS. Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
A0A0E4AFH6	MTQRNAIVVGGGIGGLTAASALARQGWRVQLHERQPEIRAVGAGIYIWDNGLFALDAVHAYSEAIEGAHEPPSIDMRGQSGKTLMRIKINGESQPRCLTLLRDQLIKALVNAAKDAGVELVTNSSVVAVRPEGEVHFEHGDHSTTDLVVVADGVHSRLRDSVDLSYSRIRMSQGAARIMIPQSSHELPAEDRGRILESFHGSRRLLYTPCTPELVYLAFTCDSDDPAISGAYINTSEWSRSFPTLSDALRATEGVPATRWDTFEYVRLASWSRGKVAFLGDAAHAQPPYLGQGGGTAMTNAIALANAVSSDMELSEALATWERITRPGIESTQRTSYQQRLLNYVPDRVRNPLVRIAGLTSNVAKSQLKATEIRPTLGSTGGSR	Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to anthranilic acid. Probably catalyzes the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4-quinolone). 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+) Up-regulated by PQS. Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
B1MFK1	MSSGHAEVVGGGIGGLTAATALALRGWTVRLHERDTRIRTVGAGIYVWDNGLEALDTIGAAAEGLDDAYEAPAITVRASDGRPLYRIDVNQPGGARCVTLLRDRLIGALHVAAEHAGVEVCTGSAAVSATADGTVEFSTGTSTRADLVVAADGVHSLLRDRLGISYRRIRMRQGAARVMVSGERPFIPGMDVDQHHEFLGGRRRLLYTPCTATQTYLAFVADNDDTATVGPELDLAAWARAFPLLVPVFDAARGRALIRWDNFELIRLSTWSHGRVAVLGDAAHAQPPYVGQGGGTAMNSAVGLAAAVSESADVEDGLNRWEQALRPPIEKAQTTSYRMRLIGSVPEVLRGPLLGALGRSRSSATSQLIKKRSAA	Involved in the degradation pathway of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4(1H)-quinolone) to anthranilate. Catalyzes the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4(1H)-quinolone). 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+) Up-regulated by PQS. Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
A0A0E4AE72	MNMPQLSTIQIGDHELAYLDNKLTSAVTPTIVMLPGWCGDHHSFSELIPQLNDTHRVVAVNWRGHAPVPHDVSDFGYAEQAQDALAILDAIGVDEFLPVSASHGGWALVQLLVDAGPARARAGVVLDWLMRRPTPEFTAALLSLQDPEGWVDSCRALFHTWRPNDSDWVESRVERAKEFGFDMWARSGRVISGAYGEHGTPLEFMKTITPERHIRHLFSTPSDSDYVAPQEAFASENEWFSYALLGGTSHFPHLEMPDRVAAHIVELAKNTYQAGAMR	Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Catalyzes the cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide. 2-heptyl-3-hydroxy-4(1H)-quinolone + O2 = CO + H(+) + N-octanoylanthranilate kcat is 20.5 sec(-1). Up-regulated by PQS. Belongs to the AB hydrolase superfamily.
A4IFR7	MDALEEESFALSFSSASDAEFDAVVGYLEDIIMDDEFQLLQRNFMDKYYQEFEDTEENKLTYTPIFNEYISLVEKYIEEQLLERIPGFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSVPASQNNLRP	Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity). Interacts with GTP bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to SLC25A4/ANT1. Interaction with ARL2 may be required for targeting to cilia basal body (By similarity). Interacts with STAT3; interaction is enhanced with ARL2. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Found in a complex with ARL2BP, ARL2 and SLC25A6. Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. Expressed in brain. Belongs to the ARL2BP family.
Q5ZKW5	METSEEENFGVAVSSPSDAEFDAVVGYLEDIIMDDDFQSIQRTFMEKHYQEFDDSEENKLIYTSIFNEYISLIEKYIEEKLLDRIPGFNMTAFTMSLQQHKDEMAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRSLDLSGGLVVTSLNKSSVSSS	Plays a role as an effector of the ADP-ribosylation factor-like protein 2, ARL2. Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Belongs to the ARL2BP family.
Q6NYS0	MVDMQSLDEEDFSVSKSSDADAEFDIVIGNIEDIIMEDEFQHLQQSFMEKYYLEFDDSEENKLSYTPIFNEYIEILEKHLEQQLVERIPGFNMDAFTHSLKQHKDEVSGDILDMLLTFTDFMAFKEMFTDYRAEKEGRGLDLSTGLVVKSLNSSSASPLTPSMASQSI	Plays a role as an effector of the ADP-ribosylation factor-like protein 2, ARL2. Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Belongs to the ARL2BP family. It is uncertain whether Met-1 or Met-4 is the initiator. Truncated N-terminus. Truncated N-terminus.
Q504R0	MDALEGESFALSFSSASDAEFDAVVGYLEDIIMDDEFQLLQRNFMDKYYLEFEDTEENKLIYTPIFNEYISLVEKYIEEQLLQRIPEFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSLPASQNNLRH	Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2. Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Interacts with GTP-bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to SLC25A4. Interaction with ARL2 may be required for targeting to cilia basal body. Interacts with STAT3; interaction is enhanced with ARL2. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization. Expressed in retina pigment epithelial cells (at protein level). Widely expressed. The disease is caused by variants affecting the gene represented in this entry. Belongs to the ARL2BP family.

Subsets and Splits

No community queries yet

The top public SQL queries from the community will appear here once available.