P02647 · APOA1_HUMAN
- ProteinApolipoprotein A-I
- GeneAPOA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids267 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameApolipoprotein A-I
- Short namesApo-AI; ApoA-I
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP02647
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Hypoalphalipoproteinemia, primary, 2 (FHA2)
- Note
- DescriptionAn autosomal recessive disorder of lipoprotein metabolism, biochemically characterized by severe apoA-I deficiency and severely reduced serum high-density lipoprotein cholesterol (HDL-C). Affected individuals have undetectable serum levels of apoA-I, and develop xanthomas and corneal opacities. The disease is generally associated with atherosclerosis and markedly increased cardiovascular risk.
- See alsoMIM:618463
Natural variants in FHA2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083307 | 23-267 | missing | in FHA2; no protein expression | |
VAR_083309 | 108-267 | missing | in FHA2; missing protein expression |
Hypoalphalipoproteinemia, primary, 2, intermediate (FHA2I)
- Note
- DescriptionAn autosomal dominant disorder of lipoprotein metabolism, biochemically characterized by partial apoA-I deficiency and reduced serum high-density lipoprotein cholesterol (HDL-C). Affected individuals have half the normal plasma apoA-I and HDL-C levels, and may develop xanthomas and corneal opacities. Most patients do not have increased cardiovascular risk.
- See alsoMIM:619836
Familial apolipoprotein gene cluster deletion syndrome (FAPLDS)
- Note
- DescriptionAn autosomal dominant disorder of lipoprotein metabolism. Affected individuals do not produce ApoA-I, ApoC-III and ApoA-IV lipoproteins, have marked plasma high density lipoprotein (HDL) deficiency, and manifest premature atherosclerosis and coronary artery disease.
- See alsoMIM:620058
Amyloidosis, hereditary systemic 3 (AMYLD3)
- Note
- DescriptionA form of hereditary systemic amyloidosis, a disorder characterized by amyloid deposition in multiple tissues resulting in a wide clinical spectrum. AMYLD3 clinical features include amyloid neuropathy, nephropathy, hepatopathy, and cardiomyopathy. Inheritance is autosomal dominant.
- See alsoMIM:620657
Natural variants in AMYLD3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_000609 | 50 | G>R | in AMYLD3; dbSNP:rs28931574 | |
VAR_000610 | 84 | L>R | in AMYLD3; dbSNP:rs121912724 | |
VAR_083310 | 173 | R>P | in AMYLD3; uncertain significance | |
VAR_083311 | 198 | L>S | in AMYLD3; plasma level of HDL and apoA-I protein were significantly lower in the patient | |
VAR_083312 | 199 | A>P | in AMYLD3; uncertain significance |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_083307 | 23-267 | in FHA2; no protein expression | |||
Sequence: Missing | ||||||
Natural variant | VAR_000605 | 27 | in Munster-3C; dbSNP:rs121912720 | |||
Sequence: P → H | ||||||
Natural variant | VAR_000606 | 27 | in dbSNP:rs121912720 | |||
Sequence: P → R | ||||||
Natural variant | VAR_000607 | 28 | in Munster-3B; dbSNP:rs121912721 | |||
Sequence: P → R | ||||||
Natural variant | VAR_000608 | 34 | in Baltimore; dbSNP:rs28929476 | |||
Sequence: R → L | ||||||
Natural variant | VAR_000609 | 50 | in AMYLD3; dbSNP:rs28931574 | |||
Sequence: G → R | ||||||
Natural variant | VAR_083308 | 56-267 | in HDL deficiency; with periorbital xanthelasmas; decreased protein abundance | |||
Sequence: Missing | ||||||
Natural variant | VAR_025445 | 61 | in dbSNP:rs12718465 | |||
Sequence: A → T | ||||||
Natural variant | VAR_000610 | 84 | in AMYLD3; dbSNP:rs121912724 | |||
Sequence: L → R | ||||||
Natural variant | VAR_017017 | 92 | confirmed at protein level; dbSNP:rs766422306 | |||
Sequence: T → I | ||||||
Natural variant | VAR_083309 | 108-267 | in FHA2; missing protein expression | |||
Sequence: Missing | ||||||
Natural variant | VAR_000611 | 113 | in dbSNP:rs150243849 | |||
Sequence: D → E | ||||||
Natural variant | VAR_000612 | 119 | in Hita | |||
Sequence: A → D | ||||||
Natural variant | VAR_016189 | 126 | in dbSNP:rs5077 | |||
Sequence: D → H | ||||||
Natural variant | VAR_000613 | 127 | in Munster-3A; dbSNP:rs921646982 | |||
Sequence: D → N | ||||||
Natural variant | VAR_000615 | 131 | in dbSNP:rs4882 | |||
Sequence: K → M | ||||||
Natural variant | VAR_000614 | 131 | in Marburg/Munster-2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_000616 | 132 | in Tsushima | |||
Sequence: W → R | ||||||
Natural variant | VAR_000617 | 134 | in Fukuoka | |||
Sequence: E → K | ||||||
Natural variant | VAR_000618 | 160 | in Norway; dbSNP:rs121912718 | |||
Sequence: E → K | ||||||
Natural variant | VAR_000619 | 163 | in dbSNP:rs758509542 | |||
Sequence: E → G | ||||||
Natural variant | VAR_000620 | 167 | in Giessen; dbSNP:rs121912719 | |||
Sequence: P → R | ||||||
Natural variant | VAR_000621 | 168 | in Zaragoza | |||
Sequence: L → R | ||||||
Natural variant | VAR_000622 | 171 | in dbSNP:rs1015066427 | |||
Sequence: E → V | ||||||
Natural variant | VAR_083310 | 173 | in AMYLD3; uncertain significance | |||
Sequence: R → P | ||||||
Natural variant | VAR_074073 | 173 | in Boston; correlated with decreased levels of HDL cholesterol; correlated with decreased serum cellular cholesterol efflux; correlated with decreased lecithin-cholesterol acyltransferase (LCAT) activity | |||
Sequence: R → S | ||||||
Natural variant | VAR_021362 | 180 | in Oita; 60% of normal apoA-I and normal HDL cholesterol levels; rapidly cleared from plasma; dbSNP:rs121912727 | |||
Sequence: V → E | ||||||
Natural variant | VAR_014609 | 184 | in dbSNP:rs5078 | |||
Sequence: R → P | ||||||
Natural variant | VAR_000623 | 189 | in dbSNP:rs121912722 | |||
Sequence: P → R | ||||||
Natural variant | VAR_000624 | 197 | in Milano; correlated with decreased HDL levels and moderate increase in triglycerides; allows the formation of disulfide-linked homodimers via the introduced cysteine; assembles properly in HDL; alters protein structure; has no tendency to form fibrils and aggregates; dbSNP:rs28931573 | |||
Sequence: R → C | ||||||
Natural variant | VAR_083311 | 198 | in AMYLD3; plasma level of HDL and apoA-I protein were significantly lower in the patient | |||
Sequence: L → S | ||||||
Natural variant | VAR_083312 | 199 | in AMYLD3; uncertain significance | |||
Sequence: A → P | ||||||
Natural variant | VAR_000625 | 222 | in Munster-4; dbSNP:rs121912717 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 396 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue (large scale data), modified residue, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-18 | UniProt | |||||
Sequence: MKAAVLTLAVLFLTGSQA | |||||||
Chain | PRO_0000425323 | 19-267 | UniProt | Proapolipoprotein A-I | |||
Sequence: RHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | |||||||
Chain | PRO_0000001940 | 25-266 | UniProt | Truncated apolipoprotein A-I | |||
Sequence: DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNT | |||||||
Chain | PRO_0000001939 | 25-267 | UniProt | Apolipoprotein A-I | |||
Sequence: DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 110 | UniProt | Methionine sulfoxide | ||||
Sequence: M | |||||||
Modified residue | 136 | UniProt | Methionine sulfoxide | ||||
Sequence: M | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 263 | UniProt | N-linked (Glc) (glycation) lysine | ||||
Sequence: K |
Post-translational modification
Glycosylated.
Palmitoylated.
Phosphorylation sites are present in the extracellular medium.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (By similarity).
Interacts with NAXE and CLU (PubMed:11991719, PubMed:1742316).
Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin (PubMed:1909888).
Interacts with NDRG1 (PubMed:15922294).
Interacts with SCGB3A2 (PubMed:12847263).
Interacts with NAXE and YJEFN3 (PubMed:23719382).
Interacts with NAXE and CLU (PubMed:11991719, PubMed:1742316).
Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin (PubMed:1909888).
Interacts with NDRG1 (PubMed:15922294).
Interacts with SCGB3A2 (PubMed:12847263).
Interacts with NAXE and YJEFN3 (PubMed:23719382).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P02647 | ABCA1 O95477 | 8 | EBI-701692, EBI-784112 | |
BINARY | P02647 | APOA1 P02647 | 28 | EBI-701692, EBI-701692 | |
BINARY | P02647 | APP P05067 | 8 | EBI-701692, EBI-77613 | |
BINARY | P02647 | C1QBP Q07021 | 2 | EBI-701692, EBI-347528 | |
BINARY | P02647 | CMTM5 Q96DZ9 | 3 | EBI-701692, EBI-2548702 | |
BINARY | P02647 | CMTM5 Q96DZ9-2 | 6 | EBI-701692, EBI-11522780 | |
BINARY | P02647 | HP P00738 | 3 | EBI-701692, EBI-1220767 | |
BINARY | P02647 | LAMP2 P13473-2 | 3 | EBI-701692, EBI-21591415 | |
BINARY | P02647 | LCAT P04180 | 2 | EBI-701692, EBI-9104464 | |
BINARY | P02647 | MAPK6 Q16659 | 3 | EBI-701692, EBI-1384105 | |
BINARY | P02647 | SH3GLB1 Q9Y371 | 3 | EBI-701692, EBI-2623095 | |
BINARY | P02647 | SNCA P37840 | 3 | EBI-701692, EBI-985879 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 68-89 | 1 | ||||
Sequence: LKLLDNWDSVTSTFSKLREQLG | ||||||
Region | 68-267 | 10 X approximate tandem repeats | ||||
Sequence: LKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | ||||||
Repeat | 90-111 | 2 | ||||
Sequence: PVTQEFWDNLEKETEGLRQEMS | ||||||
Repeat | 112-122 | 3; half-length | ||||
Sequence: KDLEEVKAKVQ | ||||||
Repeat | 123-144 | 4 | ||||
Sequence: PYLDDFQKKWQEEMELYRQKVE | ||||||
Repeat | 145-166 | 5 | ||||
Sequence: PLRAELQEGARQKLHELQEKLS | ||||||
Repeat | 167-188 | 6 | ||||
Sequence: PLGEEMRDRARAHVDALRTHLA | ||||||
Repeat | 189-210 | 7 | ||||
Sequence: PYSDELRQRLAARLEALKENGG | ||||||
Repeat | 211-232 | 8 | ||||
Sequence: ARLAEYHAKATEHLSTLSEKAK | ||||||
Repeat | 233-243 | 9; half-length | ||||
Sequence: PALEDLRQGLL | ||||||
Repeat | 244-267 | 10 | ||||
Sequence: PVLESFKVSFLSALEEYTKKLNTQ |
Sequence similarities
Belongs to the apolipoprotein A1/A4/E family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length267
- Mass (Da)30,778
- Last updated1986-07-21 v1
- Checksum1A28B8366E620310
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8W696 | F8W696_HUMAN | APOA1 | 245 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 32 | in Ref. 25; AA sequence | ||||
Sequence: W → P |
Mass Spectrometry
Apolipoprotein A-I
Molecular mass is 28,081 Da. Determined by Electrospray. Without methionine sulfoxide.Apolipoprotein A-I
Molecular mass is 28,098 Da. Determined by Electrospray. With 1 methionine sulfoxide, oxidation at Met-110.Apolipoprotein A-I
Molecular mass is 28,095 Da. Determined by Electrospray. With 1 methionine sulfoxide, oxidation at Met-136.Apolipoprotein A-I
Molecular mass is 28,114 Da. Determined by Electrospray. With 2 methionine sulfoxides, oxidation at Met-110 and Met-136.Polymorphism
Genetic variations in APOA1 can result in APOA1 deficiency and are associated with low levels of HDL cholesterol [MIM:107680].
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J00098 EMBL· GenBank· DDBJ | AAB59514.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X01038 EMBL· GenBank· DDBJ | CAA25519.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02162 EMBL· GenBank· DDBJ | CAA26097.1 EMBL· GenBank· DDBJ | mRNA | ||
X00566 EMBL· GenBank· DDBJ | CAA25232.1 EMBL· GenBank· DDBJ | mRNA | ||
M11791 EMBL· GenBank· DDBJ | AAA35545.1 EMBL· GenBank· DDBJ | mRNA | ||
X07496 EMBL· GenBank· DDBJ | CAA30377.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M27875 EMBL· GenBank· DDBJ | AAA62829.1 EMBL· GenBank· DDBJ | mRNA | ||
M29068 EMBL· GenBank· DDBJ | AAA51747.1 EMBL· GenBank· DDBJ | mRNA | ||
AY422952 EMBL· GenBank· DDBJ | AAQ91811.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY555191 EMBL· GenBank· DDBJ | AAS68227.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
A14829 EMBL· GenBank· DDBJ | CAA01198.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292231 EMBL· GenBank· DDBJ | BAF84920.1 EMBL· GenBank· DDBJ | mRNA | ||
EF444948 EMBL· GenBank· DDBJ | ACA05932.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF444948 EMBL· GenBank· DDBJ | ACA05933.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF444948 EMBL· GenBank· DDBJ | ACA05934.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF444948 EMBL· GenBank· DDBJ | ACA05935.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF444948 EMBL· GenBank· DDBJ | ACA05936.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471065 EMBL· GenBank· DDBJ | EAW67274.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005380 EMBL· GenBank· DDBJ | AAH05380.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110286 EMBL· GenBank· DDBJ | AAI10287.1 EMBL· GenBank· DDBJ | mRNA |