ID   APOA1_ORYAF             Reviewed;         265 AA.
AC   P0DMC0;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 14.
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   Orycteropus afer (Aardvark).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tubulidentata; Orycteropodidae; Orycteropus.
OX   NCBI_TaxID=9818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
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 Orycteropus afer.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (DEC-2013).
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 (By similarity). {ECO:0000250}.
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.
CC   -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC       chylomicrons.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- PTM: Palmitoylated. {ECO:0000250}.
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; ALYB01062454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DMC0; -.
DR   SMR; P0DMC0; -.
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   2: Evidence at transcript level;
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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..265
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000425327"
FT   CHAIN           27..265
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000425259"
FT   CHAIN           27..264
FT                   /note="Truncated apolipoprotein A-I"
FT                   /id="PRO_0000425260"
FT   REPEAT          69..90
FT                   /note="1"
FT   REPEAT          91..112
FT                   /note="2"
FT   REPEAT          113..123
FT                   /note="3; half-length"
FT   REPEAT          124..145
FT                   /note="4"
FT   REPEAT          146..167
FT                   /note="5"
FT   REPEAT          168..189
FT                   /note="6"
FT   REPEAT          190..209
FT                   /note="7"
FT   REPEAT          210..230
FT                   /note="8"
FT   REPEAT          231..241
FT                   /note="9; half-length"
FT   REPEAT          242..265
FT                   /note="10"
FT   REGION          69..265
FT                   /note="10 X approximate tandem repeats"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         195
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         241
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  30718 MW;  96B5F0F824B6D0EA CRC64;
     METKAVVLTL AVLFLTGSQA RHFWQQDEPQ TSWSRVKDLV TVYLDALKDS SRDYVSQFEA
     SALGKQLNLK ILDNWDTLSS TFTKLQEQMR PIFQKLWEDL DKETSPLREV LNKDLEELKQ
     KVQPYLDQFQ KKWQEEVELF RQKMAPLGTE LREGSRQKLQ ELQEKLGPLG EELRDSLRSH
     VDALRTQLAP YTEEMRQRLA SRLEALKESN LAEYHTKASE HLSALRENAK PALEDFRQGL
     MPVLEGFQKS VLAALDEATK KLNSQ