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APOA1_PANTA
ID   APOA1_PANTA             Reviewed;         151 AA.
AC   P0DM92;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Apolipoprotein A-I;
DE            Short=Apo-AI;
DE            Short=ApoA-I;
DE   AltName: Full=Apolipoprotein A1;
DE   Contains:
DE     RecName: Full=Truncated apolipoprotein A-I;
DE   Flags: Precursor; Fragment;
GN   Name=APOA1;
OS   Panthera tigris altaica (Siberian tiger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC   Panthera.
OX   NCBI_TaxID=74533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24045858; DOI=10.1038/ncomms3433;
RA   Cho Y.S., Hu L., Hou H., Lee H., Xu J., Kwon S., Oh S., Kim H.M., Jho S.,
RA   Kim S., Shin Y.A., Kim B.C., Kim H., Kim C.U., Luo S.J., Johnson W.E.,
RA   Koepfli K.P., Schmidt-Kuntzel A., Turner J.A., Marker L., Harper C.,
RA   Miller S.M., Jacobs W., Bertola L.D., Kim T.H., Lee S., Zhou Q., Jung H.J.,
RA   Xu X., Gadhvi P., Xu P., Xiong Y., Luo Y., Pan S., Gou C., Chu X.,
RA   Zhang J., Liu S., He J., Chen Y., Yang L., Yang Y., He J., Liu S., Wang J.,
RA   Kim C.H., Kwak H., Kim J.S., Hwang S., Ko J., Kim C.B., Kim S.,
RA   Bayarlkhagva D., Paek W.K., Kim S.J., O'Brien S.J., Wang J., Bhak J.;
RT   "The tiger genome and comparative analysis with lion and snow leopard
RT   genomes.";
RL   Nat. Commun. 4:2433-2433(2013).
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (OCT-2013).
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; ATCQ01045854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DM92; -.
DR   SMR; P0DM92; -.
DR   Proteomes; UP000675900; Unplaced.
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;
KW   Reference proteome; Repeat; Secreted; Signal; Steroid metabolism;
KW   Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000424674"
FT   CHAIN           25..>151
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000424675"
FT   CHAIN           25..>151
FT                   /note="Truncated apolipoprotein A-I"
FT                   /id="PRO_0000424676"
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   REGION          67..143
FT                   /note="4 X approximate tandem repeats"
FT   MOD_RES         109
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   NON_TER         151
SQ   SEQUENCE   151 AA;  17613 MW;  00110789A7148399 CRC64;
     MKAVVLTLAV LFLTGSQARH FWQQDDPQSP WDRVKDLVTV YVDAVKDGGR EYVAQFEASA
     LGKQLNLKLL DNWDTLGSTI TKLREQIGPV TQEFWDNLEK ETEVLRQEMS KDLEEVKQKV
     QPYLDDFQKK WQEEVELYRQ KVAPLGTELR E
 
 
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