APOA1_ODORO
ID APOA1_ODORO Reviewed; 266 AA.
AC P0DMS6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 20.
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 Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Odobenidae; Odobenus.
OX NCBI_TaxID=9708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foote A.D., Gilbert M.T.P., Liu Y., Lee S.L., Dugan-Rocha S., Jhangiani S.,
RA Bandaranaike D., Batterton M., Bellair M., Bess C., Blankenburg K.,
RA Chao H., Denson S., Dinh H., Elkadiri S., Fu Q., Hernandez B., Javaid M.,
RA Jayaseelan J.C., Lee S., Li M., Liu X., Matskevitch T., Munidasa M.,
RA Najjar R., Nguyen L., Ongeri F., Osuji N., Perales L., Pu L.-L., Puazo M.,
RA Qi S., Qu C., Quiroz J., Raj R., Shafer J., Shen H., Tabassum N.,
RA Tang L.-Y., Taylor A., Weissenberger G., Wu Y.-Q., Xin Y., Zhang Y.,
RA Zhu Y., Zou X., Muzny D., Worley K., Gibbs R.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (DEC-2014).
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 EMBL; ANOP01055729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004415532.1; XM_004415475.1.
DR RefSeq; XP_012423227.1; XM_012567773.1.
DR AlphaFoldDB; P0DMS6; -.
DR SMR; P0DMS6; -.
DR STRING; 9708.P0DMS6; -.
DR GeneID; 101382508; -.
DR KEGG; oro:101382508; -.
DR CTD; 335; -.
DR OrthoDB; 1553412at2759; -.
DR Proteomes; UP000245340; 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 3: Inferred from homology;
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..266
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000432016"
FT CHAIN 25..266
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000432017"
FT CHAIN 25..265
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT /id="PRO_0000432018"
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..266
FT /note="10"
FT REGION 67..266
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
SQ SEQUENCE 266 AA; 30215 MW; 61113129AB15B0B4 CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDEPQSP WDRVKDLATV YVDVVKDGGR DYVAQFEASA
LGKQLNLKLL DNWDTLSSTV AKLREQIGPV TQEFWDNLEK ETEVLRQEMN KDLEEVKKKV
QPYLDEFQSK WHEEVELYRQ KVAPLGAELS EGARQKLQEL QEKLSPLGEE LRDRARTHVD
ALRAQLAPYS DQLRERLATR LQALKEGGGA ALAEYHAKAS EQLSVLREKA KPALEDLRQG
LLPVLESFRT SLLAAVDEAT KKLNAQ
