APOA1_MACFA
ID APOA1_MACFA Reviewed; 267 AA.
AC P68292; P15568; P17929;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3106152; DOI=10.1016/0378-1119(86)90389-6;
RA Polites H.G., Melchior G.W., Castle C.K., Marotti K.R.;
RT "The primary structure of cynomolgus monkey apolipoprotein A-1 deduced from
RT the cDNA sequence: comparison to the human sequence.";
RL Gene 49:103-110(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1610902; DOI=10.1016/0167-4781(92)90079-f;
RA Murray R.W., Marotti K.R.;
RT "Nucleotide sequence of the cynomolgus monkey apolipoprotein A-I gene and
RT corresponding flanking regions.";
RL Biochim. Biophys. Acta 1131:207-210(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=1917942; DOI=10.1016/s0021-9258(18)55234-0;
RA Sorci-Thomas M., Kearns M.W.;
RT "Transcriptional regulation of the apolipoprotein A-I gene. Species-
RT specific expression correlates with rates of gene transcription.";
RL J. Biol. Chem. 266:18045-18050(1991).
RN [4]
RP PROTEIN SEQUENCE OF 25-48.
RX PubMed=3105581; DOI=10.1021/bi00379a037;
RA Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L., Kantor M.A.,
RA Nicolosi R.J., Shulman R.S.;
RT "Homologues of the human C and A apolipoproteins in the Macaca fascicularis
RT (cynomolgus) monkey.";
RL Biochemistry 26:1457-1463(1987).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15411; AAA36834.1; -; mRNA.
DR EMBL; M83242; AAA36832.1; -; Genomic_DNA.
DR EMBL; M69223; AAA36831.1; -; Genomic_DNA.
DR PIR; A26529; A26529.
DR RefSeq; NP_001270674.1; NM_001283745.1.
DR RefSeq; XP_015290827.1; XM_015435341.1.
DR AlphaFoldDB; P68292; -.
DR SMR; P68292; -.
DR STRING; 9541.XP_005579788.1; -.
DR GeneID; 101925978; -.
DR CTD; 335; -.
DR VEuPathDB; HostDB:ENSMFAG00000037868; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR Proteomes; UP000233100; Chromosome 14.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
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:0018158; P:protein oxidation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
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 CHAIN 19..267
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425324"
FT CHAIN 25..267
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001942"
FT CHAIN 25..266
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416574"
FT REPEAT 68..89
FT /note="1"
FT REPEAT 90..111
FT /note="2"
FT REPEAT 112..122
FT /note="3; half-length"
FT REPEAT 123..144
FT /note="4"
FT REPEAT 145..166
FT /note="5"
FT REPEAT 167..188
FT /note="6"
FT REPEAT 189..210
FT /note="7"
FT REPEAT 211..232
FT /note="8"
FT REPEAT 233..243
FT /note="9; half-length"
FT REPEAT 244..267
FT /note="10"
FT REGION 68..267
FT /note="10 X approximate tandem repeats"
FT MOD_RES 110
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 136
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="L -> P (in Ref. 1; AAA36834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30735 MW; 869955C024088E21 CRC64;
MKATVLTLAV LFLTGSQARH FWQQDEPPQT PWDRVKDLVT VYVEALKDSG KDYVSQFEGS
ALGKQLNLKL LDNWDSVTST VSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL HEGTRQKLHE LHEKLSPLGE EVRDRARAHV
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA SEHLSTLSEK AKPALEDLRQ
GLLPVLESFK VSFLSALEEY TKKLSTQ
