APOC3_BOVIN
ID APOC3_BOVIN Reviewed; 96 AA.
AC P19035; Q2M2T0; Q75T83;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Nitanai A., Endoh D., Oikawa S., Katoh N.;
RT "Bovine apolipoprotein C-III (ApoC3) gene, complete CDS.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-89.
RX PubMed=2209608; DOI=10.1111/j.1432-1033.1990.tb19255.x;
RA Bengtsson-Olivecrona G., Sletten K.;
RT "Primary structure of the bovine analogues to human apolipoproteins CII and
RT CIII. Studies on isoforms and evidence for proteolytic processing.";
RL Eur. J. Biochem. 192:515-521(1990).
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 -!- PTM: The most abundant glycoforms are characterized by an O-linked
CC disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc),
CC further modified with up to 3 sialic acid residues. Less abundant
CC glycoforms are characterized by more complex and fucosylated glycan
CC moieties. O-glycosylated on Thr-92 with a core 1 or possibly core 8
CC glycan. {ECO:0000250|UniProtKB:P02656}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR EMBL; AB126687; BAD15291.1; -; mRNA.
DR EMBL; BC111661; AAI11662.1; -; mRNA.
DR PIR; S13188; S13188.
DR RefSeq; NP_001001175.1; NM_001001175.2.
DR AlphaFoldDB; P19035; -.
DR SMR; P19035; -.
DR STRING; 9913.ENSBTAP00000016453; -.
DR PaxDb; P19035; -.
DR PeptideAtlas; P19035; -.
DR PRIDE; P19035; -.
DR Ensembl; ENSBTAT00000016453; ENSBTAP00000016453; ENSBTAG00000012398.
DR GeneID; 408009; -.
DR KEGG; bta:408009; -.
DR CTD; 345; -.
DR VEuPathDB; HostDB:ENSBTAG00000012398; -.
DR VGNC; VGNC:56243; APOC3.
DR eggNOG; ENOG502SZ00; Eukaryota.
DR GeneTree; ENSGT00390000015395; -.
DR HOGENOM; CLU_154694_0_0_1; -.
DR InParanoid; P19035; -.
DR OMA; YWSTFKG; -.
DR OrthoDB; 1613530at2759; -.
DR TreeFam; TF338209; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000012398; Expressed in liver and 73 other tissues.
DR ExpressionAtlas; P19035; baseline and differential.
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:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
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:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
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:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW Chylomicron; Direct protein sequencing; Glycoprotein; Lipid degradation;
KW Lipid metabolism; Lipid transport; Oxidation; Reference proteome; Secreted;
KW Sialic acid; Signal; Transport; VLDL.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2209608"
FT CHAIN 24..96
FT /note="Apolipoprotein C-III"
FT /id="PRO_0000002028"
FT REGION 68..96
FT /note="Lipid-binding"
FT /evidence="ECO:0000250"
FT SITE 41
FT /note="May interact with the LDL receptor"
FT /evidence="ECO:0000250|UniProtKB:P02656"
FT MOD_RES 63
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P33622"
FT CARBOHYD 92
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02656"
FT CONFLICT 87
FT /note="S -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 96 AA; 10692 MW; C39C5A5B57294497 CRC64;
MQPRLLLLAA FLALLVLPEA TKAEEGSLLD KMQGYVKEAT KTAKDALSSV QESQVAQQAR
DWMTESFSSL KDYWSSFKGK FTDFWESATS PTQSPP
