APOA1_BOVIN
ID APOA1_BOVIN Reviewed; 265 AA.
AC P15497; A5D7M9; Q3SZD9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Apolipoprotein A-I;
DE Short=Apo-AI;
DE Short=ApoA-I;
DE AltName: Full=Apolipoprotein A1;
DE Contains:
DE RecName: Full=Proapolipoprotein A-I;
DE Short=ProapoA-I;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-I;
DE Flags: Precursor;
GN Name=APOA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2117227; DOI=10.1093/oxfordjournals.molbev.a040608;
RA O'Huigin C., Chan L., Li W.H.;
RT "Cloning and sequencing of bovine apolipoprotein A-I cDNA and molecular
RT evolution of apolipoproteins A-I and B-100.";
RL Mol. Biol. Evol. 7:327-339(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Fetal pons, and Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-265.
RX PubMed=1739745; DOI=10.1016/0005-2760(92)90104-4;
RA Sparrow D.A., Lee B.R., Laplaud M.P., Auboiron S., Bauchart D.,
RA Chapman J.M., Gotto A.M. Jr., Yang C.Y., Sparrow J.T.;
RT "Plasma lipid transport in the preruminant calf, Bos spp: primary structure
RT of bovine apolipoprotein A-I.";
RL Biochim. Biophys. Acta 1123:145-150(1992).
RN [4]
RP PROTEIN SEQUENCE OF 25-70.
RX PubMed=2105728; DOI=10.1016/0006-291x(90)90885-q;
RA Auboiron S., Sparrow D.A., Beaubatie L., Bauchart D., Sparrow J.T.,
RA Laplaud M.P., Chapman J.M.;
RT "Characterization and amino-terminal sequence of apolipoprotein AI from
RT plasma high density lipoproteins in the preruminant calf, Bos spp.";
RL Biochem. Biophys. Res. Commun. 166:833-839(1990).
CC -!- FUNCTION: Participates in the reverse transport of cholesterol from
CC tissues to the liver for excretion by promoting cholesterol efflux from
CC tissues and by acting as a cofactor for the lecithin cholesterol
CC acyltransferase (LCAT). As part of the SPAP complex, activates
CC spermatozoa motility.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with APOA1BP and CLU.
CC Component of a sperm activating protein complex (SPAP), consisting of
CC APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and
CC albumin. Interacts with NDRG1. Interacts with SCGB3A2 (By similarity).
CC Interacts with NAXE and YJEFN3 (By similarity).
CC {ECO:0000250|UniProtKB:G5BQH5, ECO:0000250|UniProtKB:P02647,
CC ECO:0000250|UniProtKB:P04639}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC chylomicrons.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; M35870; AAA30381.1; -; mRNA.
DR EMBL; BC102941; AAI02942.1; -; mRNA.
DR EMBL; BC140619; AAI40620.1; -; mRNA.
DR PIR; I45853; A56858.
DR RefSeq; NP_776667.2; NM_174242.3.
DR AlphaFoldDB; P15497; -.
DR SMR; P15497; -.
DR IntAct; P15497; 1.
DR STRING; 9913.ENSBTAP00000002914; -.
DR PaxDb; P15497; -.
DR PeptideAtlas; P15497; -.
DR PRIDE; P15497; -.
DR Ensembl; ENSBTAT00000002914; ENSBTAP00000002914; ENSBTAG00000002258.
DR GeneID; 281631; -.
DR KEGG; bta:281631; -.
DR CTD; 335; -.
DR VEuPathDB; HostDB:ENSBTAG00000002258; -.
DR VGNC; VGNC:26022; APOA1.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P15497; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR TreeFam; TF334458; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000002258; Expressed in anterior segment of eyeball and 99 other tissues.
DR ExpressionAtlas; P15497; baseline and differential.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0051180; P:vitamin transport; IEA:Ensembl.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Direct protein sequencing; Glycoprotein; HDL;
KW Lipid metabolism; Lipid transport; Lipoprotein; Oxidation; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1739745"
FT CHAIN 19..265
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425319"
FT CHAIN 25..265
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001935"
FT CHAIN 25..264
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416571"
FT REPEAT 67..88
FT /note="1"
FT REPEAT 89..110
FT /note="2"
FT REPEAT 111..121
FT /note="3; half-length"
FT REPEAT 122..143
FT /note="4"
FT REPEAT 144..165
FT /note="5"
FT REPEAT 166..187
FT /note="6"
FT REPEAT 188..209
FT /note="7"
FT REPEAT 210..230
FT /note="8"
FT REPEAT 231..241
FT /note="9; half-length"
FT REPEAT 242..265
FT /note="10"
FT REGION 67..265
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 185..186
FT /note="QL -> HV (in Ref. 1; AAA30381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 30276 MW; 06A2681EA2ABA50F CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDDPQSS WDRVKDFATV YVEAIKDSGR DYVAQFEASA
LGKQLNLKLL DNWDTLASTL SKVREQLGPV TQEFWDNLEK ETASLRQEMH KDLEEVKQKV
QPYLDEFQKK WHEEVEIYRQ KVAPLGEEFR EGARQKVQEL QDKLSPLAQE LRDRARAHVE
TLRQQLAPYS DDLRQRLTAR LEALKEGGGS LAEYHAKASE QLKALGEKAK PVLEDLRQGL
LPVLESLKVS ILAAIDEASK KLNAQ
