APOC3_PIG
ID APOC3_PIG Reviewed; 96 AA.
AC P27917; Q29208;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 131.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8468059; DOI=10.1006/geno.1993.1119;
RA Birchbauer A., Knipping G., Juritsch B., Aschauer H., Zechner R.;
RT "Characterization of the apolipoprotein AI and CIII genes in the domestic
RT pig.";
RL Genomics 15:643-652(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-96, PROTEIN SEQUENCE OF 34-58, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8428656; DOI=10.1016/0378-1119(93)90121-i;
RA Trieu V.N., Hasler-Rapacz J., Rapacz J., Black D.D.;
RT "Sequences and expression of the porcine apolipoprotein A-I and C-III
RT mRNAs.";
RL Gene 123:173-179(1993).
RN [4]
RP PROTEIN SEQUENCE OF 24-96.
RA Hasler-Rapacz J.O., Chaudhary R., Chowdhary B.P., Trieu V.N., Jackson K.,
RA Gustavsson I., Rapacz J.;
RL Submitted (OCT-1995) to UniProtKB.
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 -!- TISSUE SPECIFICITY: Synthesized predominantly in liver and to a lesser
CC degree in intestine. {ECO:0000269|PubMed:8428656,
CC ECO:0000269|PubMed:8468059}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR EMBL; L00627; AAA30993.1; -; Genomic_DNA.
DR EMBL; F14536; CAA23113.1; -; mRNA.
DR EMBL; M84133; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M84134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B46018; B46018.
DR RefSeq; NP_001002801.1; NM_001002801.1.
DR RefSeq; XP_005667429.1; XM_005667372.1.
DR RefSeq; XP_005667430.1; XM_005667373.1.
DR AlphaFoldDB; P27917; -.
DR SMR; P27917; -.
DR STRING; 9823.ENSSSCP00000015993; -.
DR PaxDb; P27917; -.
DR PeptideAtlas; P27917; -.
DR PRIDE; P27917; -.
DR Ensembl; ENSSSCT00000016435; ENSSSCP00000015993; ENSSSCG00000015069.
DR Ensembl; ENSSSCT00005035249; ENSSSCP00005021468; ENSSSCG00005022280.
DR Ensembl; ENSSSCT00005035285; ENSSSCP00005021487; ENSSSCG00005022280.
DR Ensembl; ENSSSCT00005035313; ENSSSCP00005021507; ENSSSCG00005022280.
DR Ensembl; ENSSSCT00005035342; ENSSSCP00005021529; ENSSSCG00005022280.
DR Ensembl; ENSSSCT00015106164; ENSSSCP00015044612; ENSSSCG00015078430.
DR Ensembl; ENSSSCT00025008549; ENSSSCP00025003367; ENSSSCG00025006471.
DR Ensembl; ENSSSCT00030090701; ENSSSCP00030041772; ENSSSCG00030064837.
DR Ensembl; ENSSSCT00035030741; ENSSSCP00035012006; ENSSSCG00035023450.
DR Ensembl; ENSSSCT00040033903; ENSSSCP00040013969; ENSSSCG00040025123.
DR Ensembl; ENSSSCT00040034204; ENSSSCP00040014101; ENSSSCG00040025123.
DR Ensembl; ENSSSCT00040034236; ENSSSCP00040014115; ENSSSCG00040025123.
DR Ensembl; ENSSSCT00040034260; ENSSSCP00040014128; ENSSSCG00040025123.
DR Ensembl; ENSSSCT00045024167; ENSSSCP00045016668; ENSSSCG00045014192.
DR Ensembl; ENSSSCT00050089653; ENSSSCP00050038492; ENSSSCG00050065822.
DR Ensembl; ENSSSCT00055026185; ENSSSCP00055020805; ENSSSCG00055013290.
DR Ensembl; ENSSSCT00060017063; ENSSSCP00060006774; ENSSSCG00060012997.
DR Ensembl; ENSSSCT00065007617; ENSSSCP00065003241; ENSSSCG00065005643.
DR Ensembl; ENSSSCT00070010689; ENSSSCP00070008797; ENSSSCG00070005639.
DR GeneID; 406187; -.
DR KEGG; ssc:406187; -.
DR CTD; 345; -.
DR VGNC; VGNC:85421; APOC3.
DR eggNOG; ENOG502SZ00; Eukaryota.
DR GeneTree; ENSGT00390000015395; -.
DR HOGENOM; CLU_154694_0_0_1; -.
DR InParanoid; P27917; -.
DR OMA; YWSTFKG; -.
DR OrthoDB; 1613530at2759; -.
DR TreeFam; TF338209; -.
DR Reactome; R-SSC-975634; Retinoid metabolism and transport.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000015069; Expressed in liver and 24 other tissues.
DR ExpressionAtlas; P27917; baseline.
DR Genevisible; P27917; SS.
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; Lipid degradation;
KW Lipid metabolism; Lipid transport; Reference proteome; Secreted; Signal;
KW Transport; VLDL.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..96
FT /note="Apolipoprotein C-III"
FT /id="PRO_0000002034"
FT REGION 68..96
FT /note="Lipid-binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 96 AA; 10704 MW; E4AC07F58C8A4DB2 CRC64;
MQPRVLLVAG LLVLLACAQA IEAEDTSLLD KMQDYVKQAT RTAQDALTSV KESEVAQQAR
GWVTDSISSL KDYWSTFKGK FTDFWDYTPK PEPSSS
