ID   APOA1_BALAS             Reviewed;         265 AA.
AC   P0DMA6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
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   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zheng Y., Li E., Zhan S., Cho Y.S.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (NOV-2013).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; ATDI01007014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007196619.1; XM_007196557.1.
DR   AlphaFoldDB; P0DMA6; -.
DR   SMR; P0DMA6; -.
DR   STRING; 9767.XP_007196619.1; -.
DR   GeneID; 103019302; -.
DR   KEGG; bacu:103019302; -.
DR   CTD; 335; -.
DR   Proteomes; UP000261681; Unplaced.
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;
KW   Reference proteome; Repeat; Secreted; Signal; Steroid metabolism;
KW   Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..265
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000425318"
FT   CHAIN           25..265
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000425090"
FT   CHAIN           25..264
FT                   /note="Truncated apolipoprotein A-I"
FT                   /id="PRO_0000425091"
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..142
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..230
FT                   /note="8"
FT   REPEAT          231..241
FT                   /note="9; half-length"
FT   REPEAT          242..265
FT                   /note="10"
FT   REGION          67..265
FT                   /note="10 X approximate tandem repeats"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  30514 MW;  3AC098E87A3A9151 CRC64;
     MKAVVLTLAV LFLTGSQARH FWQQDDPQSS WDRVKDFATV YVDAIKDSGR DYVTQFEASA
     LGKQLNLKLL DNWDSLTSTF AKVREQLGPV TREFWDNLEK ETESLRQEMN KDLQEVKQKV
     QPYLDEFQKK WQEELQIYRQ KVAPLGEELR EGARQKVQEL QDKLTPLAEE MRDRARAHVE
     TLRQQLAPYS DELRQRMAAR FEMLKEGGGS LVQYHAKASE QLKALGEKAK PALEDLRQGL
     LPVLENLKVS ILAAIDEASK KLNAQ