ID   APOA2_HORSE             Reviewed;          76 AA.
AC   P83704;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Apolipoprotein A-II;
DE            Short=Apo-AII;
DE            Short=ApoA-II;
DE   AltName: Full=Apolipoprotein A2;
GN   Name=APOA2 {ECO:0000250|UniProtKB:P02652};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, PYROGLUTAMATE FORMATION AT GLN-1, AND DISULFIDE BOND.
RC   TISSUE=Serum {ECO:0000269|PubMed:15253869};
RX   PubMed=15253869; DOI=10.1016/j.cbpc.2004.02.008;
RA   Puppione D.L., Fischer W.H., Park M., Whitelegge J.P., Schumaker V.N.,
RA   Golfeitz S., MacDonald M.H.;
RT   "Sequence of horse (Equus caballus) apoA-II. Another example of a dimer
RT   forming apolipoprotein.";
RL   Comp. Biochem. Physiol. 138B:213-220(2004).
CC   -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC       association with lipids, and affect the HDL metabolism. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:15253869). Interacts with
CC       NAXE and NDRG1 (By similarity). {ECO:0000250|UniProtKB:P02652,
CC       ECO:0000269|PubMed:15253869}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15253869}.
CC   -!- TISSUE SPECIFICITY: Plasma. {ECO:0000269|PubMed:15253869}.
CC   -!- MASS SPECTROMETRY: Mass=8616; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15253869};
CC   -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR   AlphaFoldDB; P83704; -.
DR   SMR; P83704; -.
DR   STRING; 9796.ENSECAP00000008027; -.
DR   PaxDb; P83704; -.
DR   PeptideAtlas; P83704; -.
DR   InParanoid; P83704; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR   GO; GO:0034190; F:apolipoprotein receptor binding; IBA:GO_Central.
DR   GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR   GO; GO:0008035; F:high-density lipoprotein particle binding; IBA:GO_Central.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR   GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR   GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR   GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR   GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR   GO; GO:0034374; P:low-density lipoprotein particle remodeling; IBA:GO_Central.
DR   GO; GO:0060192; P:negative regulation of lipase activity; IBA:GO_Central.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IBA:GO_Central.
DR   InterPro; IPR006801; ApoA-II.
DR   InterPro; IPR036172; ApoA-II_sf.
DR   PANTHER; PTHR11027; PTHR11027; 1.
DR   Pfam; PF04711; ApoA-II; 1.
DR   SUPFAM; SSF82936; SSF82936; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; HDL; Lipid transport;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Transport.
FT   CHAIN           1..76
FT                   /note="Apolipoprotein A-II"
FT                   /id="PRO_0000181374"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:15253869"
FT   DISULFID        6
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:15253869"
SQ   SEQUENCE   76 AA;  8617 MW;  D47CD17142C62E01 CRC64;
     QAEESCLQNL ASRYLQTVTD YGKDLVEKAL APELQAQAKA YFEKTQEQLT PLVKKIGNDL
     LNFFSHFIEL KTQPAT