ID   APOA1_MICOH             Reviewed;         265 AA.
AC   P0DTU9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
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   Microtus ochrogaster (Prairie vole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Microtus.
OX   NCBI_TaxID=79684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Microtus ochrogaster.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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RL   Unpublished observations (MAR-2020).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; CM001675.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005347313.1; XM_005347256.2.
DR   AlphaFoldDB; P0DTU9; -.
DR   SMR; P0DTU9; -.
DR   GeneID; 102002535; -.
DR   CTD; 335; -.
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; Repeat;
KW   Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..265
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000450147"
FT   CHAIN           25..265
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000450148"
FT   CHAIN           25..264
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
FT                   /id="PRO_0000450149"
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:Q00623"
FT   MOD_RES         241
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:Q00623"
FT   MOD_RES         243
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:Q00623"
SQ   SEQUENCE   265 AA;  30715 MW;  FA089E8072915D44 CRC64;
     MKAVVLAVAV LFLTGSQARH FWQQDEPPQS SWDRVKDFAT VYVDAVKDTG RDYVSQFETS
     ALGKQLNLNL LENWDTLGSS VGRLQEQLGP VTQEFWDNLE KDTDWLRQEM NKDLEDVKTK
     VQPYLDQFQS KWQEEVARYR QKVEPLGAEL REGARQKLQE LQEKLAPVGE DLRDRMRQHV
     DTLRTKLAPY SDKMRDRLAE RLAQLKDSAT LAEYHTKATE HLKTFSEKAK PALEDLRQGV
     MPMLESFRVR LMSMIDEASK KLSAQ