APOA1_DIPOR
ID APOA1_DIPOR Reviewed; 265 AA.
AC A0A1S3EL69;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Apolipoprotein A-I;
DE Short=Apo-AI;
DE Short=ApoA-I;
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 Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Kidney;
RA Liu Y., Qu J., Gnerre S., Cree A., Dinh H., Dugan S., Jhangiani S.,
RA Lee S.L., Nazareth L., Okwuonu G., Santibanez J., Anosike U.,
RA Bandaranaike D., Bickham C., Chao H., Chavez A., Dahdouli M., Dao M.,
RA Davila M., Davy-Carroll L., Denson S., Falls T., Fernandez S., Fernando P.,
RA Francis C., Ganer J., Garcia R. III, Gross S., Hale W., Heiman D.,
RA Hollins B., Javaid M., Johnson B., Jones J., Joshi V., Kalu J., Kisamo H.,
RA Largo L., Le T., Leal B., Legall F. III, Lemon S., Lewis L., Lopez J.,
RA Martinez E., Matakis S., Mercado I., Munidasa M., Narasimhan A., Ng B.,
RA Ngo D., Nguyen L., Obregon M., Ongeri F., Onwere C., Osuji N., Parra A.,
RA Perez A., Perez Y., Pham C., Primus E., Puazo R., Qi S., Qu C., Quiroz J.,
RA Raj R., Rajbhandari K., Ruiz S., Schneider B., Simmons D., Sisson I.,
RA Skinner E., Thornton R., Usmani K., Walker D., White C., Williams A.,
RA Woodworth J., Wright R., Young S., Yun X., Han Y., Kovar C., Reid J.G.,
RA Weinstock G., Doddapaneni H., Muzny D.M., Worley K.C., Gibbs R.A.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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; ABRO02010954.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012865101.1; XM_013009647.1.
DR AlphaFoldDB; A0A1S3EL69; -.
DR SMR; A0A1S3EL69; -.
DR STRING; 10020.ENSDORP00000011659; -.
DR GeneID; 105980742; -.
DR KEGG; dord:105980742; -.
DR CTD; 335; -.
DR OrthoDB; 1553412at2759; -.
DR Proteomes; UP000081671; 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 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..265
FT /note="Proapolipoprotein A-I"
FT /id="PRO_5010248087"
FT CHAIN 25..265
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000450135"
FT CHAIN 25..264
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT /id="PRO_0000450136"
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..208
FT /note="7; truncated"
FT REPEAT 209..230
FT /note="8"
FT REPEAT 231..241
FT /note="9; half-length"
FT REPEAT 242..265
FT /note="10"
FT REGION 68..265
FT /note="10 X approximate tandem repeats"
FT MOD_RES 110
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT MOD_RES 194
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
SQ SEQUENCE 265 AA; 30298 MW; 3D75113F4414083F CRC64;
MKAVVLAVAA LFLAGGEARH FWQRDEPQAS PWDKIKEFTT QYVDSVKDSG SEYLKQFETS
ALGTQMNLKL TENLDTLSST FSKLREQLGP VTQEFWQNLE KDTEWLRQEM NKDLADMKQK
VQPYMEQFQK TWQEEVERYR QKVEPLSTEL REGARQKLQE LQEKLAPLGA DLRDSARVHV
DALRTQLAPY SEQMRERLAE RLAALRDSPS LAEYQAKAHE HLKTLHEKAQ PALSDLGQGV
LPVLESLKAT LVGAIEEASK KLSSQ
