ID   APOA1_FUKDA             Reviewed;         264 AA.
AC   P0DTU7;
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   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver;
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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RL   Unpublished observations (MAR-2020).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; AYUG01101138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_010627698.1; XM_010629396.2.
DR   AlphaFoldDB; P0DTU7; -.
DR   SMR; P0DTU7; -.
DR   GeneID; 104865719; -.
DR   CTD; 335; -.
DR   OMA; KEVREMW; -.
DR   Proteomes; UP000028990; 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_0000450137"
FT   CHAIN           25..264
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000450138"
FT   CHAIN           25..263
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
FT                   /id="PRO_0000450139"
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"
SQ   SEQUENCE   264 AA;  30685 MW;  A22A11BCC7FEEFC7 CRC64;
     MKAVVLAVAV LFLTGSQARH FWQRDEPQTS WDRVKDFATM YVDVIQESGK DYVAQLDAST
     LGKQLNLNLL ENWDTLSSAF SKLREQLGHV SQEFWDTFEK DTAWLREEMN KDLEKVKKKV
     QPFLDSFQEK MQEEVKRYRH KVEPLSLELR DGAHQQLKEL QEKLGPLGKD LKDHALVHMD
     ELRSHLRTYT EEMGQILAER LGAIKESTSL AEYQTKASEH LRTFSKKAKP ILEDLRQGLL
     PVAENFKTNI KNTFDQITKH VTTQ