ID   APOC3_HORSE             Reviewed;          97 AA.
AC   P0DN28;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Apolipoprotein C-III;
DE            Short=Apo-CIII;
DE            Short=ApoC-III;
DE   AltName: Full=Apolipoprotein C3;
DE   Flags: Precursor;
GN   Name=APOC3;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mongolian;
RX   PubMed=24828444; DOI=10.1038/srep04958;
RA   Huang J., Zhao Y., Shiraigol W., Li B., Bai D., Ye W., Daidiikhuu D.,
RA   Yang L., Jin B., Zhao Q., Gao Y., Wu J., Bao W., Li A., Zhang Y., Han H.,
RA   Bai H., Bao Y., Zhao L., Zhai Z., Zhao W., Sun Z., Zhang Y., Meng H.,
RA   Dugarjaviin M.;
RT   "Analysis of horse genomes provides insight into the diversification and
RT   adaptive evolution of karyotype.";
RL   Sci. Rep. 4:4958-4958(2014).
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUL-2015).
CC   -!- FUNCTION: Component of triglyceride-rich very low density lipoproteins
CC       (VLDL) and high density lipoproteins (HDL) in plasma. Plays a
CC       multifaceted role in triglyceride homeostasis. Intracellularly,
CC       promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and
CC       secretion; extracellularly, attenuates hydrolysis and clearance of
CC       triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by
CC       inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant
CC       receptors. Formed of several curved helices connected via semiflexible
CC       hinges, so that it can wrap tightly around the curved micelle surface
CC       and easily adapt to the different diameters of its natural binding
CC       partners. {ECO:0000250|UniProtKB:P02656}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR   EMBL; ATDM01002572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DN28; -.
DR   SMR; P0DN28; -.
DR   STRING; 9796.ENSECAP00000039343; -.
DR   PaxDb; P0DN28; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR   GO; GO:0034363; C:intermediate-density lipoprotein particle; 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: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:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic 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:0010987; P:negative regulation of high-density lipoprotein particle clearance; IBA:GO_Central.
DR   GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IBA:GO_Central.
DR   GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IBA:GO_Central.
DR   GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IBA:GO_Central.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IBA:GO_Central.
DR   GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR   Gene3D; 6.10.90.10; -; 1.
DR   InterPro; IPR008403; Apo-CIII.
DR   InterPro; IPR038195; Apo_CIII_sf.
DR   PANTHER; PTHR14225; PTHR14225; 1.
DR   Pfam; PF05778; Apo-CIII; 1.
PE   3: Inferred from homology;
KW   Chylomicron; Glycoprotein; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Reference proteome; Secreted; Sialic acid; Signal;
KW   Transport; VLDL.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..97
FT                   /note="Apolipoprotein C-III"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
FT                   /id="PRO_0000433959"
FT   REGION          66..97
FT                   /note="Lipid-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
FT   SITE            39
FT                   /note="May interact with the LDL receptor"
FT                   /evidence="ECO:0000250|UniProtKB:P02656"
SQ   SEQUENCE   97 AA;  10598 MW;  23EF2A4FEBF0F591 CRC64;
     MQPRVLLIAA LLALLATAAE DKDASLLDVV QGYMQQASKT AKDTLTSMQE SQVAQQARDW
     VNDGLSSLKD YWGKLKGKFS SFWDSTFEDT TPSPAVA