APOA1
entrez
335
canonical
uniprot
P02647
canonical
ensembl
ENSG00000118137
resolver
ensp
ENSP00000236850
resolver
ensp
ENSP00000352471
resolver
ensp
ENSP00000364469
resolver
ensp
ENSP00000364472
resolver
ensp
ENSP00000525356
resolver
ensp
ENSP00000525357
resolver
ensp
ENSP00000525358
resolver
ensp
ENSP00000525359
resolver
ensp
ENSP00000525363
resolver
ensp
ENSP00000525367
resolver
ensp
ENSP00000525369
resolver
ensp
ENSP00000525370
resolver
ensp
ENSP00000525374
resolver
ensp
ENSP00000525377
resolver
ensp
ENSP00000525379
resolver
ensp
ENSP00000525380
resolver
enst
ENST00000236850
resolver
enst
ENST00000359492
resolver
enst
ENST00000375320
resolver
enst
ENST00000375323
resolver
enst
ENST00000855297
resolver
enst
ENST00000855298
resolver
enst
ENST00000855299
resolver
enst
ENST00000855300
resolver
enst
ENST00000855304
resolver
enst
ENST00000855308
resolver
enst
ENST00000855310
resolver
enst
ENST00000855311
resolver
enst
ENST00000855315
resolver
enst
ENST00000855318
resolver
enst
ENST00000855320
resolver
enst
ENST00000855321
resolver
genesymbol
APOA1
resolver
hgnc
HGNC:600
resolver
uniprot
A0A024R3E3
resolver
uniprot
A8K866
resolver
uniprot
Q6LDN9
resolver
uniprot
Q6Q785
resolver
uniprot
Q9UCS8
resolver
uniprot
Q9UCT8
resolver
uniprot_entry
A0A024R3E3_HUMAN
resolver
uniprot_entry
APOA1_HUMAN
resolver
uniprot_sec
A8K866
resolver
uniprot_sec
Q6LDN9
resolver
uniprot_sec
Q6Q785
resolver
uniprot_sec
Q9UCS8
resolver
uniprot_sec
Q9UCT8
resolver
amino_acid_sequence
MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
uniprot
proteins
disease_involvement
DISEASE: Hypoalphalipoproteinemia, primary, 2 (FHA2) [MIM:618463]: An 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. {ECO:0000269|PubMed:1898657, ECO:0000269|PubMed:1901417, ECO:0000269|PubMed:8282791}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hypoalphalipoproteinemia, primary, 2, intermediate (FHA2I) [MIM:619836]: An 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. {ECO:0000269|PubMed:8240372}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Familial apolipoprotein gene cluster deletion syndrome (FAPLDS) [MIM:620058]: An 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. {ECO:0000269|PubMed:6800349}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Amyloidosis, hereditary systemic 3 (AMYLD3) [MIM:620657]: A 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. {ECO:0000269|PubMed:10198255, ECO:0000269|PubMed:10487826, ECO:0000269|PubMed:12050338, ECO:0000269|PubMed:1502149, ECO:0000269|PubMed:2123470, ECO:0000269|PubMed:3142462, ECO:0000269|PubMed:8208902}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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. {ECO:0000269|PubMed:1909888}.
uniprot
proteins
mass_dalton
30778
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-53, F-124, F-139, F-190, F-216 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 53; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-124, F-139, F-190, F-216 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 124; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-139, F-190, F-216 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 139; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-190, F-216 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 190; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-139, F-216 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 216; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-139, F-190 and F-260."; /evidence="ECO:0000269|PubMed:16091367"; MUTAGEN 260; /note="Y->F: Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-139, F-190 and F-216."; /evidence="ECO:0000269|PubMed:16091367
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000269|PubMed:3005308}.; PTM: Phosphorylation sites are present in the extracellular medium.; PTM: Some tyrosine residues are chlorinated and nitrated: chlorination and nitration takes place when the lipid-free form of APOA1 is exposed to hypochlorous acid and peroxynitrite oxidants, respectively, which are generated by myeloperoxidase (MPO) (PubMed:15314690, PubMed:15326314, PubMed:15498770, PubMed:15574409, PubMed:16091367). Chlorinated and nitrated at Tyr-53, Tyr-190, Tyr-216 and Tyr-260; Tyr-216 constitutes the major site of chlorination and nitration (PubMed:15498770). According to a report, chlorination of Tyr-216 inactivates APOA1 and impairs cholesterol transport (PubMed:15574409). According to another report, however, other sites, such as tryptophan residues, can be modified by oxidants generated by MPO in absence of tyrosine residues (PubMed:16091367). {ECO:0000269|PubMed:15314690, ECO:0000269|PubMed:15326314, ECO:0000269|PubMed:15498770, ECO:0000269|PubMed:15574409, ECO:0000269|PubMed:16091367}.
uniprot
proteins
protein_family
Apolipoprotein A1/A4/E family
uniprot
proteins
pubmed
10198255
uniprot
proteins
pubmed
10487826
uniprot
proteins
pubmed
11991719
uniprot
proteins
pubmed
12050338
uniprot
proteins
pubmed
12562854
uniprot
proteins
pubmed
12576517
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12847263
uniprot
proteins
pubmed
12966036
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1502149
uniprot
proteins
pubmed
15108119
uniprot
proteins
pubmed
15314690
uniprot
proteins
pubmed
15326314
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498770
uniprot
proteins
pubmed
15574409
uniprot
proteins
pubmed
15922294
uniprot
proteins
pubmed
16091367
uniprot
proteins
pubmed
164450
uniprot
proteins
pubmed
1742316
uniprot
proteins
pubmed
1898657
uniprot
proteins
pubmed
1901417
uniprot
proteins
pubmed
1909888
uniprot
proteins
pubmed
204308
uniprot
proteins
pubmed
2107878
uniprot
proteins
pubmed
2108924
uniprot
proteins
pubmed
2111322
uniprot
proteins
pubmed
2123470
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22028381
uniprot
proteins
pubmed
23719382
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24755625
uniprot
proteins
pubmed
2506184
uniprot
proteins
pubmed
2512329
uniprot
proteins
pubmed
26073399
uniprot
proteins
pubmed
2673706
uniprot
proteins
pubmed
2995392
uniprot
proteins
pubmed
3005308
uniprot
proteins
pubmed
3047170
uniprot
proteins
pubmed
3120314
uniprot
proteins
pubmed
3129297
uniprot
proteins
pubmed
3142462
uniprot
proteins
pubmed
6198645
uniprot
proteins
pubmed
6207999
uniprot
proteins
pubmed
6294659
uniprot
proteins
pubmed
6304641
uniprot
proteins
pubmed
6328445
uniprot
proteins
pubmed
6401735
uniprot
proteins
pubmed
6405383
uniprot
proteins
pubmed
6406984
uniprot
proteins
pubmed
6409108
uniprot
proteins
pubmed
6412234
uniprot
proteins
pubmed
6413973
uniprot
proteins
pubmed
6432779
uniprot
proteins
pubmed
6489332
uniprot
proteins
pubmed
6800349
uniprot
proteins
pubmed
7895732
uniprot
proteins
pubmed
7918609
uniprot
proteins
pubmed
7981179
uniprot
proteins
pubmed
8208902
uniprot
proteins
pubmed
8240372
uniprot
proteins
pubmed
8261628
uniprot
proteins
pubmed
8282791
uniprot
proteins
pubmed
8664326
uniprot
proteins
pubmed
9356442
uniprot
proteins
pubmed
9514407
uniprot
proteins
sequence_length
267
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins