ID   APOA1_MUSPF             Reviewed;         266 AA.
AC   M3XYN3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 2.
DT   25-MAY-2022, entry version 32.
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   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Mustela.
OX   NCBI_TaxID=9669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ID#1420;
RA   Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S.,
RA   Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., Przyblyski D.,
RA   Ribeiro F., Russell P., Sharpe T., Turner-Maier J., Walker B.J., Young S.,
RA   Birren B., Lindblad-Toh K.;
RL   Submitted (APR-2011) 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; AEYP01026780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004749957.1; XM_004749900.2.
DR   AlphaFoldDB; M3XYN3; -.
DR   SMR; M3XYN3; -.
DR   STRING; 9669.ENSMPUP00000004184; -.
DR   GeneID; 101689587; -.
DR   KEGG; mpuf:101689587; -.
DR   CTD; 335; -.
DR   eggNOG; ENOG502S1XQ; Eukaryota.
DR   HOGENOM; CLU_058447_1_0_1; -.
DR   InParanoid; M3XYN3; -.
DR   Proteomes; UP000000715; 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   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   3: Inferred from homology;
KW   Cholesterol metabolism; HDL; Lipid metabolism; Lipid transport;
KW   Lipoprotein; Oxidation; Palmitate; Phosphoprotein; Reference proteome;
KW   Repeat; Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..266
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000432010"
FT   CHAIN           25..266
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000432011"
FT   CHAIN           25..265
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
FT                   /id="PRO_0000432012"
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..209
FT                   /note="7"
FT   REPEAT          210..231
FT                   /note="8"
FT   REPEAT          232..242
FT                   /note="9; half-length"
FT   REPEAT          243..266
FT                   /note="10"
FT   REGION          67..266
FT                   /note="10 X approximate tandem repeats"
FT   MOD_RES         109
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
SQ   SEQUENCE   266 AA;  30179 MW;  A9F720271BDD9138 CRC64;
     MKAVVLTLAV LFLTGSQARH FWQQDEPQSP WDRVKDLATV YVDAVKDGGR DYVAQFEASA
     LGKQLNLKLL DNWDSLSGTV AKLREQIGPV TQEFWDNLEK ETEALRQEMS KDLEEVKQKV
     QPYLDEFQKK WHEEVELYRQ KVAPLGTELR EGARQKLQEL QEKLTPLGEE LRDRARTHVD
     ALRAHLAPYS DQLRERLATR LQALKEGGSA SLAEYHAKAS EHLSALSEKA KPALEDLRQG
     LLPVLESFKV SLLAAVDEAA KKLNTQ