APOA1_SAIBB
ID APOA1_SAIBB Reviewed; 266 AA.
AC A0A2K6TRM6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 24.
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 Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Saimiri boliviensis.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (OCT-2020).
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. {ECO:0000250|UniProtKB:P02647}.
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 {ECO:0000250|UniProtKB:P02647}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.
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 RefSeq; XP_003923713.1; XM_003923664.2.
DR RefSeq; XP_010332821.1; XM_010334519.1.
DR AlphaFoldDB; A0A2K6TRM6; -.
DR SMR; A0A2K6TRM6; -.
DR STRING; 39432.ENSSBOP00000022311; -.
DR Ensembl; ENSSBOT00000039158; ENSSBOP00000022311; ENSSBOG00000027691.
DR GeneID; 101038607; -.
DR KEGG; sbq:101038607; -.
DR CTD; 335; -.
DR GeneTree; ENSGT00950000182929; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0018206; P:peptidyl-methionine modification; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; IEA:Ensembl.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR GO; GO:0051180; P:vitamin transport; IEA:Ensembl.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 3: Inferred from homology;
KW Cholesterol metabolism; HDL; Lipid metabolism; Lipid transport;
KW Lipoprotein; Oxidation; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..266
FT /note="Apolipoprotein A-I"
FT /id="PRO_5014467984"
FT CHAIN 25..266
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000451969"
FT CHAIN 25..265
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT /id="PRO_0000451970"
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..209
FT /note="7"
FT REPEAT 210..231
FT /note="8"
FT REPEAT 232..242
FT /note="9; half-length"
FT REPEAT 243..266
FT /note="10"
FT REGION 68..266
FT /note="10 X approximate tandem repeats"
FT MOD_RES 110
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT MOD_RES 136
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
SQ SEQUENCE 266 AA; 30705 MW; A5D1473438246D68 CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDEPPQS PWDRVKDLAT VYVDSVKESG KDYVSQFETS
ALGKQLNLKL LDNWDSLTST VNKLREQLGP VTQEFWDNLE KETEQLRQEM NKDLEEVKAK
VQPYLDDFQK KWQEEMNLYS QKLEPLRTEF QEGAFQKLQD LREKLRPVAE QVRDRARAHV
DTLRTQLAPY SDELRQRLAT RLEALKESGA TLAEYQAKAS EHLSALGEKA KPAFEDLRQG
LLPVLESFKV SFLSALDEYA KKLSSQ
