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Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3)

 APOC3_MACFA             Reviewed;          99 AA.
P18659;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
23-MAY-2018, entry version 85.
RecName: Full=Apolipoprotein C-III;
Short=Apo-CIII;
Short=ApoC-III;
AltName: Full=Apolipoprotein C3;
Flags: Precursor;
Name=APOC3;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=8448212; DOI=10.1016/0167-4781(93)90226-4;
Osada J., Pocovi M., Nicolosi R.J., Schaefer E.J., Ordovas J.M.;
"Nucleotide sequences of the Macaca fascicularis apolipoprotein C-III
and A-IV genes.";
Biochim. Biophys. Acta 1172:335-339(1993).
[2]
PROTEIN SEQUENCE OF 21-36.
PubMed=3105581; DOI=10.1021/bi00379a037;
Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L.,
Kantor M.A., Nicolosi R.J., Shulman R.S.;
"Homologues of the human C and A apolipoproteins in the Macaca
fascicularis (cynomolgus) monkey.";
Biochemistry 26:1457-1463(1987).
-!- FUNCTION: Component of triglyceride-rich very low density
lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma.
Plays a multifaceted role in triglyceride homeostasis.
Intracellularly, promotes hepatic very low density lipoprotein 1
(VLDL1) assembly and secretion; extracellularly, attenuates
hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs).
Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and
the hepatic uptake of TRLs by remnant receptors. Formed of several
curved helices connected via semiflexible hinges, so that it can
wrap tightly around the curved micelle surface and easily adapt to
the different diameters of its natural binding partners.
{ECO:0000250|UniProtKB:P02656}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}.
-!- PTM: The most abundant glycoforms are characterized by an O-linked
disaccharide galactose linked to N-acetylgalactosamine (Gal-
GalNAc), further modified with up to 3 sialic acid residues. Less
abundant glycoforms are characterized by more complex and
fucosylated glycan moieties. O-glycosylated on Thr-94 with a core
1 or possibly core 8 glycan. {ECO:0000250|UniProtKB:P02656}.
-!- SIMILARITY: Belongs to the apolipoprotein C3 family.
{ECO:0000305}.
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EMBL; X68359; CAA48419.1; -; Genomic_DNA.
PIR; S30196; S29566.
RefSeq; XP_005579787.1; XM_005579730.1.
ProteinModelPortal; P18659; -.
SMR; P18659; -.
Ensembl; ENSMFAT00000022932; ENSMFAP00000004270; ENSMFAG00000001837.
GeneID; 102144085; -.
KEGG; mcf:102144085; -.
CTD; 345; -.
GeneTree; ENSGT00390000015395; -.
HOVERGEN; HBG050549; -.
KO; K08759; -.
GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
Gene3D; 1.10.225.30; -; 1.
InterPro; IPR008403; Apo-CIII.
InterPro; IPR038195; Apo_CIII_sf.
PANTHER; PTHR14225; PTHR14225; 1.
Pfam; PF05778; Apo-CIII; 1.
ProDom; PD010414; Apo-CIII; 1.
1: Evidence at protein level;
Chylomicron; Direct protein sequencing; Glycoprotein;
Lipid degradation; Lipid metabolism; Lipid transport; Secreted;
Sialic acid; Signal; Transport; VLDL.
SIGNAL 1 20 {ECO:0000269|PubMed:3105581}.
CHAIN 21 99 Apolipoprotein C-III.
/FTId=PRO_0000002032.
REGION 68 99 Lipid-binding. {ECO:0000250}.
SITE 41 41 May interact with the LDL receptor.
{ECO:0000250|UniProtKB:P02656}.
CARBOHYD 94 94 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P02656}.
SEQUENCE 99 AA; 10747 MW; 24B476162B43F733 CRC64;
MQPRVLLVAA LLSLLASARA SEAEDTSLLG FMQGYMQHAT KTAKDALTSV QESQVAQQAR
GWVTDGFSSL KDYWSTVKDK LSGFWDLNPE AKPTLAEAA


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