ID   APOA1_MARMO             Reviewed;         264 AA.
AC   D7PGV9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 32.
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   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=W810;
RX   PubMed=21520143; DOI=10.1002/jmv.22104;
RA   Fioravanti J., Gomar C., Medina-Echeverz J., Otano I., Benito A.,
RA   Prieto J., Gonzalez-Aseguinolaza G., Berraondo P.;
RT   "Characterization of woodchuck apolipoprotein A-I: A new tool for drug
RT   delivery and identification of altered isoforms in the woodchuck chronic
RT   hepatitis model.";
RL   J. Med. Virol. 83:1221-1229(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (APR-2019) 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=D7PGV9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=D7PGV9-2; Sequence=Not described;
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; GU562343; ADG96165.1; -; mRNA.
DR   EMBL; CABDUW010000004; VTJ51515.1; -; Genomic_DNA.
DR   EMBL; CABDUW010000004; VTJ51516.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PGV9; -.
DR   SMR; D7PGV9; -.
DR   PRIDE; D7PGV9; -.
DR   Proteomes; UP000335636; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cholesterol metabolism; Glycoprotein; HDL;
KW   Lipid metabolism; Lipid transport; Lipoprotein; Oxidation; Palmitate;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW   Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..264
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_5003105138"
FT   CHAIN           25..264
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000450145"
FT   CHAIN           25..263
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
FT                   /id="PRO_0000450146"
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"
SQ   SEQUENCE   264 AA;  30502 MW;  16BC39BAE2213F1D CRC64;
     MKAVVLTVAV FFLTGSQARH FWQQDEPQSS WDRMKDFATV YLDAVKDSGR DYVTQFETSA
     LGKQLNLKLL DNWDSLSSTV SKLREQIGPV TQEFWDKLEK DTVSLRQEMN KDLEEVKLKV
     QPYLDEFQKR WQEDVERYRQ QVEPLGTELR EGARQKLQEL HEKLSPLGQE LRDRARAHVD
     ALRTHLAPYS DELRQRLAAR LEALKESSSL ADYQAKATEH LSALGEKAKP ALEDLRQGLL
     PVLENLKMSF WSAVDEATKK LTTQ