APOA1_PANHO
ID APOA1_PANHO Reviewed; 262 AA.
AC P0DMA8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 21.
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 Pantholops hodgsonii (Chiru) (Tibetan antelope).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Antilopinae; Pantholops.
OX NCBI_TaxID=59538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23673643; DOI=10.1038/ncomms2860;
RA Ge R.L., Cai Q., Shen Y.Y., San A., Ma L., Zhang Y., Yi X., Chen Y.,
RA Yang L., Huang Y., He R., Hui Y., Hao M., Li Y., Wang B., Ou X., Xu J.,
RA Zhang Y., Wu K., Geng C., Zhou W., Zhou T., Irwin D.M., Yang Y., Ying L.,
RA Bao H., Kim J., Larkin D.M., Ma J., Lewin H.A., Xing J., Platt R.N. II,
RA Ray D.A., Auvil L., Capitanu B., Zhang X., Zhang G., Murphy R.W., Wang J.,
RA Zhang Y.P., Wang J.;
RT "Draft genome sequence of the Tibetan antelope.";
RL Nat. Commun. 4:1858-1858(2013).
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RL Unpublished observations (NOV-2013).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; AGTT01159304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005980012.1; XM_005979950.1.
DR AlphaFoldDB; P0DMA8; -.
DR SMR; P0DMA8; -.
DR PRIDE; P0DMA8; -.
DR OrthoDB; 1553412at2759; -.
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; Repeat;
KW Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..262
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425331"
FT CHAIN 25..262
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000425095"
FT CHAIN 25..261
FT /note="Truncated apolipoprotein A-I"
FT /id="PRO_0000425096"
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..184
FT /note="6"
FT REPEAT 185..206
FT /note="7"
FT REPEAT 207..227
FT /note="8"
FT REPEAT 228..238
FT /note="9; half-length"
FT REPEAT 239..262
FT /note="10"
FT REGION 67..262
FT /note="10 X approximate tandem repeats"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 238
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 29941 MW; 2BDF5E99FBFBAF13 CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDEPQSS WDRVKDFATV YVEAIKDSGR DYVAQFEASA
LGKQLNLKLL DNWDTLASTL SKVREQLGPV TQEFWDNLEK ETAALRQEMN KDLEEVKQKV
QPYLDEFQRK WHEEVEIYRQ KVAPLGEEFR EGARQKVQEL QDRLSPLAQE LRDRARAHVE
KQLAPYSDDL RQRLTARLEA LKEGGGSLAE YHAKATEQLK ALGEKAKPAL EDLRQGLMPV
LESLKVSILA AIDEASKKLN AQ
