ID   APOA1_TUPBE             Reviewed;         265 AA.
AC   O18759;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
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   Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=37347;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Lu X., Chen B., Zhao Y., Wang K., Xue H., Zeng W.;
RT   "Cloning and sequencing of tree shrew apolipoprotein AI cDNA.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; AF005638; AAB82326.1; -; mRNA.
DR   AlphaFoldDB; O18759; -.
DR   SMR; O18759; -.
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: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: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                   /evidence="ECO:0000250"
FT   CHAIN           19..265
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000425338"
FT   CHAIN           25..265
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000001956"
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..265
FT                   /note="10"
FT   REGION          67..265
FT                   /note="10 X approximate tandem repeats"
FT   MOD_RES         193
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         242
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         244
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  30332 MW;  60076BC39FAEA165 CRC64;
     MKAVVLTLAV LFLTGSQARH FWQQDEPQSS WDRVRDLANV YVDAVKESGR EYVSQLEASA
     LGKQLNLKLV DNWDTLGSTF QKVHEHLGPV AQEFWEKLEK ETEELRREIN KDLEDVRQKT
     QPFLDEIQKK WQEDLERYRQ KVEPLSAQLR EGARQKLMEL QEQVTPLGED LRDSVRAYAD
     TLRTQLAPYS EQMRKTLGAR LEAIKEGGSA SLAEYHAKAS EQLSALGEKA KPVLEDIHQG
     LMPMWESFKT GVLNVIDEAA KKLTA