ID   APOA1_PAPHA             Reviewed;         267 AA.
AC   P68293; P15568; P17929;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
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   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2907746; DOI=10.1016/0378-1119(88)90181-3;
RA   Hixson J.E., Borenstein S., Cox L.A., Rainwater D.L., Vandeberg J.L.;
RT   "The baboon gene for apolipoprotein A-I: characterization of a cDNA clone
RT   and identification of DNA polymorphisms for genetic studies of cholesterol
RT   metabolism.";
RL   Gene 74:483-490(1988).
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; M35634; AAA35380.1; -; mRNA.
DR   AlphaFoldDB; P68293; -.
DR   SMR; P68293; -.
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   2: Evidence at transcript level;
KW   Cholesterol metabolism; Glycoprotein; HDL; Lipid metabolism;
KW   Lipid transport; Lipoprotein; Oxidation; Palmitate; Phosphoprotein; Repeat;
KW   Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT   CHAIN           19..267
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000425332"
FT   CHAIN           25..267
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000001948"
FT   CHAIN           25..266
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416577"
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"
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