APOA1_CHICK
ID APOA1_CHICK Reviewed; 264 AA.
AC P08250;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 157.
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 Flags: Precursor;
GN Name=APOA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3118875; DOI=10.1016/0006-291x(87)91137-5;
RA Byrnes L., Luo C.-C., Li W.-H., Yang C.-Y., Chan L.;
RT "Chicken apolipoprotein A-I: cDNA sequence, tissue expression and
RT evolution.";
RL Biochem. Biophys. Res. Commun. 148:485-492(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3126099; DOI=10.1016/0378-1119(87)90211-3;
RA Ferrari S., Tarugi P., Drusiani E., Calandra S., Fregni M.;
RT "The complete sequence of chick apolipoprotein AI mRNA and its expression
RT in the developing chick.";
RL Gene 60:39-46(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3108248; DOI=10.1016/s0021-9258(18)48202-6;
RA Rajavashisth T.B., Dawson P.A., Williams D.L., Shackelford J.E.,
RA Lebherz H., Lusis A.J.;
RT "Structure, evolution, and regulation of chicken apolipoprotein A-I.";
RL J. Biol. Chem. 262:7058-7065(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1512510;
RA Lamon-Fava S., Sastry R., Ferrari S., Rajavashisth T.B., Lusis A.J.,
RA Karathanasis S.K.;
RT "Evolutionary distinct mechanisms regulate apolipoprotein A-I gene
RT expression: differences between avian and mammalian apoA-I gene
RT transcription control regions.";
RL J. Lipid Res. 33:831-842(1992).
RN [5]
RP PROTEIN SEQUENCE OF 25-44.
RX PubMed=6406496; DOI=10.1016/s0021-9258(18)32348-2;
RA Shackelford J.E., Lebherz H.G.;
RT "Synthesis and secretion of apolipoprotein A1 by chick breast muscle.";
RL J. Biol. Chem. 258:7175-7180(1983).
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).
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:G5BQH5}.
CC -!- INTERACTION:
CC P08250; Q9KH15: pMGA1.2; Xeno; NbExp=2; IntAct=EBI-1635960, EBI-13636839;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC chylomicrons.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; M17961; AAA48593.1; -; mRNA.
DR EMBL; M18746; AAA48594.1; -; mRNA.
DR EMBL; M25559; AAA48592.1; -; mRNA.
DR EMBL; M96012; AAA48597.1; -; Genomic_DNA.
DR PIR; JH0471; LPCHA1.
DR RefSeq; NP_990856.1; NM_205525.4.
DR AlphaFoldDB; P08250; -.
DR SMR; P08250; -.
DR BioGRID; 676780; 1.
DR IntAct; P08250; 2.
DR STRING; 9031.ENSGALP00000011510; -.
DR PaxDb; P08250; -.
DR Ensembl; ENSGALT00000011524; ENSGALP00000011510; ENSGALG00000007114.
DR GeneID; 396536; -.
DR KEGG; gga:396536; -.
DR CTD; 335; -.
DR VEuPathDB; HostDB:geneid_396536; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P08250; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR PhylomeDB; P08250; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Reactome; R-GGA-2168880; Scavenging of heme from plasma.
DR Reactome; R-GGA-3000471; Scavenging by Class B Receptors.
DR Reactome; R-GGA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-GGA-8963896; HDL assembly.
DR Reactome; R-GGA-8964011; HDL clearance.
DR Reactome; R-GGA-8964058; HDL remodeling.
DR PRO; PR:P08250; -.
DR Proteomes; UP000000539; Chromosome 24.
DR Bgee; ENSGALG00000007114; Expressed in ovary and 13 other tissues.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0045445; P:myoblast differentiation; TAS:AgBase.
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:1901247; P:negative regulation of lung ciliated cell differentiation; IMP:AgBase.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:AgBase.
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; HDL; Lipid metabolism;
KW Lipid transport; Reference proteome; Repeat; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..18
FT CHAIN 19..264
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425341"
FT CHAIN 25..264
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001960"
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..231
FT /note="8"
FT REPEAT 232..242
FT /note="9; half-length"
FT REPEAT 243..264
FT /note="10"
FT REGION 67..264
FT /note="10 X approximate tandem repeats"
FT CONFLICT 16
FT /note="T -> I (in Ref. 3; AAA48592 and 4; AAA48597)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> K (in Ref. 3; AAA48592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 30680 MW; 968320E81E2AC5C2 CRC64;
MRGVLVTLAV LFLTGTQARS FWQHDEPQTP LDRIRDMVDV YLETVKASGK DAIAQFESSA
VGKQLDLKLA DNLDTLSAAA AKLREDMAPY YKEVREMWLK DTEALRAELT KDLEEVKEKI
RPFLDQFSAK WTEELEQYRQ RLTPVAQELK ELTKQKVELM QAKLTPVAEE ARDRLRGHVE
ELRKNLAPYS DELRQKLSQK LEEIREKGIP QASEYQAKVM EQLSNLREKM TPLVQEFRER
LTPYAENLKN RLISFLDELQ KSVA
