APOA1_NANGA
ID APOA1_NANGA Reviewed; 264 AA.
AC P0DTV1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
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 Nannospalax galili (Northern Israeli blind subterranean mole rat) (Spalax
OS galili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=1026970;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24892994; DOI=10.1038/ncomms4966;
RA Fang X., Nevo E., Han L., Levanon E.Y., Zhao J., Avivi A., Larkin D.,
RA Jiang X., Feranchuk S., Zhu Y., Fishman A., Feng Y., Sher N., Xiong Z.,
RA Hankeln T., Huang Z., Gorbunova V., Zhang L., Zhao W., Wildman D.E.,
RA Xiong Y., Gudkov A., Zheng Q., Rechavi G., Liu S., Bazak L., Chen J.,
RA Knisbacher B.A., Lu Y., Shams I., Gajda K., Farre M., Kim J., Lewin H.A.,
RA Ma J., Band M., Bicker A., Kranz A., Mattheus T., Schmidt H., Seluanov A.,
RA Azpurua J., McGowen M.R., Ben Jacob E., Li K., Peng S., Zhu X., Liao X.,
RA Li S., Krogh A., Zhou X., Brodsky L., Wang J.;
RT "Genome-wide adaptive complexes to underground stresses in blind mole rats
RT Spalax.";
RL Nat. Commun. 5:3966-3966(2014).
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (MAR-2020).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 EMBL; AXCS01177051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008849164.1; XM_008850942.2.
DR AlphaFoldDB; P0DTV1; -.
DR SMR; P0DTV1; -.
DR Ensembl; ENSNGAT00000025518; ENSNGAP00000019853; ENSNGAG00000019547.
DR GeneID; 103748325; -.
DR KEGG; ngi:103748325; -.
DR CTD; 335; -.
DR GeneTree; ENSGT00950000182929; -.
DR OMA; KEVREMW; -.
DR Proteomes; UP000694381; 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 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..264
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000450153"
FT CHAIN 25..264
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000450154"
FT CHAIN 25..263
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT /id="PRO_0000450155"
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..207
FT /note="7; truncated"
FT REPEAT 208..229
FT /note="8"
FT REPEAT 230..240
FT /note="9; half-length"
FT REPEAT 241..264
FT /note="10"
FT REGION 67..264
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT MOD_RES 193
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
FT MOD_RES 240
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02647"
SQ SEQUENCE 264 AA; 30804 MW; 8BFA162E90C10228 CRC64;
MKAVVLAVAV LFLTGSQARH FWQQDEPQSP WDRVKDFATV YVDAVKDSGR EYVSQFETSA
LGKQLNLNLL ENWDTFGSTF GRLQEQLGPV TREFWDSLEK DTDWLRQEMN KDLEEVKQKV
QPYLDEFQKK WEEEVERYRP KVEPLGAQLR EGARQKLEEL QKQLVPLGED LRDRARLHVD
ALRTKLAPYS DQMRDRLAER LTALRDNPKL AEYHARATEH LKKLGEKTKP TLEDLRQGLM
PWLESLKAKA LSVLDEATQK LNTQ
