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

 APOC3_RAT               Reviewed;         101 AA.
P06759;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
23-MAY-2018, entry version 114.
RecName: Full=Apolipoprotein C-III;
Short=Apo-CIII;
Short=ApoC-III;
AltName: Full=Apolipoprotein C3;
Flags: Precursor;
Name=Apoc3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=3020028;
Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
"Linkage, evolution, and expression of the rat apolipoprotein A-I, C-
III, and A-IV genes.";
J. Biol. Chem. 261:13268-13277(1986).
[2]
SEQUENCE REVISION TO 60.
Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
-!- TISSUE SPECIFICITY: Synthesized predominantly in liver and to a
lesser degree in intestine. {ECO:0000269|PubMed:3020028}.
-!- 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-96 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; J02596; AAA40746.1; -; Genomic_DNA.
PIR; B24700; B24700.
UniGene; Rn.129547; -.
ProteinModelPortal; P06759; -.
SMR; P06759; -.
STRING; 10116.ENSRNOP00000067045; -.
iPTMnet; P06759; -.
PhosphoSitePlus; P06759; -.
PaxDb; P06759; -.
PRIDE; P06759; -.
RGD; 2136; Apoc3.
eggNOG; ENOG410JE3N; Eukaryota.
eggNOG; ENOG4111APE; LUCA.
HOVERGEN; HBG050549; -.
InParanoid; P06759; -.
PhylomeDB; P06759; -.
PRO; PR:P06759; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P06759; RN.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0042627; C:chylomicron; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IBA:GO_Central.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
GO; GO:0005319; F:lipid transporter activity; TAS:RGD.
GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:RGD.
GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IEP:RGD.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006869; P:lipid transport; TAS:RGD.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
GO; GO:0042953; P:lipoprotein transport; IDA:RGD.
GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; IBA:GO_Central.
GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IBA:GO_Central.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IBA:GO_Central.
GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IDA:RGD.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IBA:GO_Central.
GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IBA:GO_Central.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
GO; GO:0034014; P:response to triglyceride; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IBA:GO_Central.
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.
2: Evidence at transcript level;
Chylomicron; Complete proteome; Glycoprotein; Lipid degradation;
Lipid metabolism; Lipid transport; Oxidation; Reference proteome;
Secreted; Sialic acid; Signal; Transport; VLDL.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 101 Apolipoprotein C-III.
/FTId=PRO_0000002035.
REGION 69 101 Lipid-binding. {ECO:0000250}.
SITE 41 41 May interact with the LDL receptor.
{ECO:0000250|UniProtKB:P02656}.
MOD_RES 64 64 Methionine sulfoxide.
{ECO:0000250|UniProtKB:P33622}.
CARBOHYD 96 96 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P02656}.
SEQUENCE 101 AA; 11117 MW; 1A7260DB909692D2 CRC64;
MQPRMLLIVA LVALLASARA DEGEGSLLLG SMQGYMEQAS KTVQDALSSM QESDIAVVAS
RGWMDNRFKS LKGYWSKFTD KFTGLWESGP EDQLTTPTLE P


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