APOA1_RAT
ID APOA1_RAT Reviewed; 259 AA.
AC P04639; O08877; O09054; Q5EBB2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6426956; DOI=10.1111/j.1432-1033.1984.tb08129.x;
RA Poncin J.E., Martial J.A., Gielen J.E.;
RT "Cloning and structure analysis of the rat apolipoprotein A-I cDNA.";
RL Eur. J. Biochem. 140:493-498(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3020028; DOI=10.1016/s0021-9258(18)69300-7;
RA Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
RT "Linkage, evolution, and expression of the rat apolipoprotein A-I, C-III,
RT and A-IV genes.";
RL J. Biol. Chem. 261:13268-13277(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SHRSP, and Wistar Kyoto; TISSUE=Spleen;
RX PubMed=9415807; DOI=10.1080/15216549700204801;
RA Chiang A.-N., Fan K.-C., Shaw G.-C., Yang U.-C.;
RT "Repetitive elements in the third intron of murine apolipoprotein A-I
RT gene.";
RL Biochem. Mol. Biol. Int. 43:989-996(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-45 (PRECURSOR PROTEIN).
RC STRAIN=Sprague-Dawley;
RX PubMed=6798036; DOI=10.1016/s0021-9258(19)68295-5;
RA Gordon J.I., Smith D.P., Andy R., Alpers D.H., Schonfeld G., Strauss A.W.;
RT "The primary translation product of rat intestinal apolipoprotein A-I mRNA
RT is an unusual preproprotein.";
RL J. Biol. Chem. 257:971-978(1982).
RN [6]
RP PROTEIN SEQUENCE OF 36-46; 162-168 AND 202-212, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
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 -!- INTERACTION:
CC P04639; Q7TMA5: Apob; NbExp=2; IntAct=EBI-2925493, EBI-15185298;
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; M00001; AAA40749.1; -; mRNA.
DR EMBL; X00558; CAA25224.1; -; mRNA.
DR EMBL; J02597; AAA40745.1; -; Genomic_DNA.
DR EMBL; U79576; AAB58428.1; -; Genomic_DNA.
DR EMBL; U79577; AAB58429.1; -; Genomic_DNA.
DR EMBL; U79578; AAB58430.1; -; Genomic_DNA.
DR EMBL; BC089820; AAH89820.1; -; mRNA.
DR PIR; A24700; A24700.
DR RefSeq; NP_036870.1; NM_012738.1.
DR AlphaFoldDB; P04639; -.
DR SMR; P04639; -.
DR BioGRID; 247155; 1.
DR DIP; DIP-29911N; -.
DR IntAct; P04639; 4.
DR STRING; 10116.ENSRNOP00000065206; -.
DR CarbonylDB; P04639; -.
DR iPTMnet; P04639; -.
DR PhosphoSitePlus; P04639; -.
DR PaxDb; P04639; -.
DR PRIDE; P04639; -.
DR Ensembl; ENSRNOT00000074357; ENSRNOP00000065206; ENSRNOG00000045679.
DR GeneID; 25081; -.
DR KEGG; rno:25081; -.
DR CTD; 335; -.
DR RGD; 2130; Apoa1.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P04639; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR PhylomeDB; P04639; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-8963896; HDL assembly.
DR Reactome; R-RNO-8963901; Chylomicron remodeling.
DR Reactome; R-RNO-8964011; HDL clearance.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR Reactome; R-RNO-9707616; Heme signaling.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P04639; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000045679; Expressed in jejunum and 18 other tissues.
DR Genevisible; P04639; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0034365; C:discoidal high-density lipoprotein particle; IDA:RGD.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; ISO:RGD.
DR GO; GO:0034190; F:apolipoprotein receptor binding; ISO:RGD.
DR GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0055102; F:lipase inhibitor activity; IDA:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0005319; F:lipid transporter activity; ISO:RGD.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IDA:RGD.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0070508; P:cholesterol import; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0030301; P:cholesterol transport; IDA:RGD.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0008211; P:glucocorticoid metabolic process; ISO:RGD.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:RGD.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; ISO:RGD.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0060192; P:negative regulation of lipase activity; IDA:RGD.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:RGD.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISO:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0018158; P:protein oxidation; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:RGD.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0051180; P:vitamin transport; ISO:RGD.
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:6798036"
FT CHAIN 19..259
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425335"
FT CHAIN 25..259
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001954"
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..161
FT /note="5; truncated"
FT REPEAT 162..183
FT /note="6"
FT REPEAT 184..203
FT /note="7; truncated"
FT REPEAT 204..225
FT /note="8"
FT REPEAT 226..236
FT /note="9; half-length"
FT REPEAT 237..259
FT /note="10"
FT REGION 67..259
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 236
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="Missing (in Ref. 3; AAB58428/AAB58429/AAB58430)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="E -> D (in Ref. 3; AAB58428/AAB58429/AAB58430)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="L -> P (in Ref. 3; AAB58428/AAB58429/AAB58430)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="G -> A (in Ref. 3; AAB58428/AAB58429/AAB58430)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="K -> R (in Ref. 1; CAA25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> G (in Ref. 1; CAA25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> R (in Ref. 1; CAA25224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 30062 MW; 28538891B2E3A6CD CRC64;
MKAAVLAVAL VFLTGCQAWE FWQQDEPQSQ WDRVKDFATV YVDAVKDSGR DYVSQFESST
LGKQLNLNLL DNWDTLGSTV GRLQEQLGPV TQEFWANLEK ETDWLRNEMN KDLENVKQKM
QPHLDEFQEK WNEEVEAYRQ KLEPLGTELH KNAKEMQRHL KVVAEEFRDR MRVNADALRA
KFGLYSDQMR ENLAQRLTEI KNHPTLIEYH TKASDHLKTL GEKAKPALDD LGQGLMPVLE
AWKAKIMSMI DEAKKKLNA
