APOA1_AILME
ID APOA1_AILME Reviewed; 266 AA.
AC D2HC77;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 66.
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 Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (NOV-2013).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; ACTA01112696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL192677; EFB21763.1; -; Genomic_DNA.
DR RefSeq; XP_002919539.1; XM_002919493.3.
DR AlphaFoldDB; D2HC77; -.
DR SMR; D2HC77; -.
DR STRING; 9646.ENSAMEP00000009115; -.
DR PRIDE; D2HC77; -.
DR Ensembl; ENSAMET00000025841; ENSAMEP00000035554; ENSAMEG00000008662.
DR Ensembl; ENSAMET00000035218; ENSAMEP00000040924; ENSAMEG00000008662.
DR GeneID; 100477643; -.
DR CTD; 335; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; D2HC77; -.
DR OMA; KEVREMW; -.
DR OrthoDB; 1553412at2759; -.
DR TreeFam; TF334458; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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:0000250"
FT CHAIN 19..266
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425317"
FT CHAIN 25..266
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000425087"
FT CHAIN 25..265
FT /note="Truncated apolipoprotein A-I"
FT /id="PRO_0000425088"
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..142
FT /note="4"
FT REPEAT 144..165
FT /note="5"
FT REPEAT 166..187
FT /note="6"
FT REPEAT 188..210
FT /note="7"
FT REPEAT 211..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 /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 30208 MW; CDA2A6E4431E0A4E CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDEPQSP WDRVKDLATV YVDAVKEGGR DYVAQFEASA
LGKQLNLKLL DNWDSLTSTV TKLREQIGPV TQEFWDNLEK ETEVLRQEMS KDLEEVKQKV
QPYLDEFQKN WHEEVELYRQ KVAPLGAELR EGARQKLQEL QEKLSPLGEE LRDRARIHVD
ALRAQLAPYS DQLRERLAAR LQALKEDGGA SLAEYHAKAS EHLSALSEKA KPALEDLRQG
LLPVLESFKV SLLAAVDEAA KKLNAQ
