APOA1_PANTR
ID APOA1_PANTR Reviewed; 267 AA.
AC P0DJG0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21298813; DOI=10.1016/j.cbd.2009.09.001;
RA Puppione D.L., Della Donna L., Laganowsky A.D., Bassilian S., Souda P.,
RA Ryder O.A., Whitelegge J.P.;
RT "Mass spectral analyses of the two major apolipoproteins of great ape high
RT density lipoproteins.";
RL Comp. Biochem. Physiol. 4:305-309(2009).
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 -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=28079.33;
CC Mass_error=1.258; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21298813};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-I]: Mass=27953.3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:21298813};
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR RefSeq; XP_001153383.1; XM_001153383.4.
DR RefSeq; XP_001153517.1; XM_001153517.4.
DR RefSeq; XP_016777528.1; XM_016922039.1.
DR RefSeq; XP_016777529.1; XM_016922040.1.
DR RefSeq; XP_016777530.1; XM_016922041.1.
DR RefSeq; XP_508770.1; XM_508770.5.
DR AlphaFoldDB; P0DJG0; -.
DR BMRB; P0DJG0; -.
DR SMR; P0DJG0; -.
DR STRING; 9598.ENSPTRP00000007404; -.
DR PaxDb; P0DJG0; -.
DR PRIDE; P0DJG0; -.
DR Ensembl; ENSPTRT00000008023; ENSPTRP00000007404; ENSPTRG00000004316.
DR Ensembl; ENSPTRT00000095290; ENSPTRP00000080550; ENSPTRG00000046016.
DR GeneID; 107967226; -.
DR KEGG; ptr:107967226; -.
DR CTD; 335; -.
DR VGNC; VGNC:10228; APOA1.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P0DJG0; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR TreeFam; TF334458; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004316; Expressed in liver and 11 other tissues.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0034364; C:high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
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:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein 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 CHAIN 19..267
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425330"
FT CHAIN 25..267
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000416563"
FT CHAIN 25..266
FT /note="Truncated apolipoprotein A-I"
FT /id="PRO_0000416564"
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; 30778 MW; 1A28B8366E620310 CRC64;
MKAAVLTLAV LFLTGSQARH FWQQDEPPQS PWDRVKDLAT VYVDVLKDSG RDYVSQFEGS
ALGKQLNLKL LDNWDSVTST FSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL QEGARQKLHE LQEKLSPLGE EMRDRARAHV
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA TEHLSTLSEK AKPALEDLRQ
GLLPVLESFK VSFLSALEEY TKKLNTQ
