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

 APOC3_HUMAN             Reviewed;          99 AA.
P02656; Q08E83; Q6Q786;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 182.
RecName: Full=Apolipoprotein C-III;
Short=Apo-CIII;
Short=ApoC-III;
AltName: Full=Apolipoprotein C3;
Flags: Precursor;
Name=APOC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6439535; DOI=10.1089/dna.1.1984.3.449;
Protter A.A., Levy-Wilson B., Miller J., Bencen G., White T.,
Seilhamer J.J.;
"Isolation and sequence analysis of the human apolipoprotein CIII gene
and the intergenic region between the apo AI and apo CIII genes.";
DNA 3:449-456(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6548954; DOI=10.1089/dna.1984.3.359;
Levy-Wilson B., Appleby V., Protter A.A., Auperin D., Seilhamer J.J.;
"Isolation and DNA sequence of full-length cDNA for human
preapolipoprotein CIII.";
DNA 3:359-364(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2989400;
Karathanasis S.K., Zannis V.I., Breslow J.L.;
"Isolation and characterization of cDNA clones corresponding to two
different human apoC-III alleles.";
J. Lipid Res. 26:451-456(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=6328445; DOI=10.1093/nar/12.9.3917;
Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
Baralle F.E.;
"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
abundance.";
Nucleic Acids Res. 12:3917-3932(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15108119; DOI=10.1007/s00439-004-1106-x;
Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D.,
Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G.,
Nickerson D.A., Weiss K.M.;
"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.";
Hum. Genet. 115:36-56(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 21-99.
PubMed=3949020; DOI=10.1016/0014-5793(86)80300-3;
Hospattankar A.V., Brewer H.B. Jr., Ronan R., Fairwell T.;
"Amino acid sequence of human plasma apolipoprotein C-III from
normolipidemic subjects.";
FEBS Lett. 197:67-73(1986).
[8]
PROTEIN SEQUENCE OF 21-99.
PubMed=4846755;
Brewer H.B. Jr., Shulman R., Herbert P., Ronan R., Wehrly K.;
"The complete amino acid sequence of alanine apolipoprotein (apoC-3),
and apolipoprotein from human plasma very low density lipoproteins.";
J. Biol. Chem. 249:4975-4984(1974).
[9]
REVIEW.
PubMed=18201179; DOI=10.1111/j.1742-1241.2007.01678.x;
Chan D.C., Chen M.M., Ooi E.M., Watts G.F.;
"An ABC of apolipoprotein C-III: a clinically useful new
cardiovascular risk factor?";
Int. J. Clin. Pract. 62:799-809(2008).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-94, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
REVIEW.
PubMed=22510806; DOI=10.1097/MOL.0b013e328352dc70;
Yao Z., Wang Y.;
"Apolipoprotein C-III and hepatic triglyceride-rich lipoprotein
production.";
Curr. Opin. Lipidol. 23:206-212(2012).
[13]
GLYCOSYLATION AT THR-94, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23527852; DOI=10.1021/pr400136p;
Nicolardi S., van der Burgt Y.E., Dragan I., Hensbergen P.J.,
Deelder A.M.;
"Identification of new apolipoprotein-CIII glycoforms with ultrahigh
resolution MALDI-FTICR mass spectrometry of human sera.";
J. Proteome Res. 12:2260-2268(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
STRUCTURE BY NMR IN COMPLEX WITH SDS MICELLES, AND FUNCTION.
PubMed=18408013; DOI=10.1074/jbc.M800756200;
Gangabadage C.S., Zdunek J., Tessari M., Nilsson S., Olivecrona G.,
Wijmenga S.S.;
"Structure and dynamics of human apolipoprotein CIII.";
J. Biol. Chem. 283:17416-17427(2008).
[16]
VARIANT C-III-0 ALA-94, AND GLYCOSYLATION AT THR-94.
PubMed=3123586;
Maeda H., Hashimoto R.K., Oguro T., Hiraga S., Uzawa H.;
"Molecular cloning of a human apoC-III variant: Thr 74-->Ala 74
mutation prevents O-glycosylation.";
J. Lipid Res. 28:1405-1409(1987).
[17]
VARIANT HALP2 GLU-78.
PubMed=2022742; DOI=10.1172/JCI115190;
von Eckardstein A., Holz H., Sandkamp M., Weng W., Funke H.,
Assmann G.;
"Apolipoprotein C-III(Lys-58-->Glu). Identification of an
apolipoprotein C-III variant in a family with
hyperalphalipoproteinemia.";
J. Clin. Invest. 87:1724-1731(1991).
-!- FUNCTION: Component of triglyceride-rich very low density
lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma
(PubMed:18201179, PubMed:22510806). Plays a multifaceted role in
triglyceride homeostasis (PubMed:18201179, PubMed:22510806).
Intracellularly, promotes hepatic very low density lipoprotein 1
(VLDL1) assembly and secretion; extracellularly, attenuates
hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs)
(PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs
by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by
remnant receptors (PubMed:18201179, PubMed:22510806). 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
(PubMed:18408013). {ECO:0000269|PubMed:18408013,
ECO:0000303|PubMed:18201179, ECO:0000303|PubMed:22510806}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:18201179,
ECO:0000303|PubMed:22510806}.
-!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:6328445}.
-!- 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:0000269|PubMed:19838169,
ECO:0000269|PubMed:23527852, ECO:0000269|PubMed:3123586}.
-!- DISEASE: Hyperalphalipoproteinemia 2 (HALP2) [MIM:614028]: A
condition characterized by high levels of high density lipoprotein
(HDL) and increased HDL cholesterol levels.
{ECO:0000269|PubMed:2022742}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the apolipoprotein C3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J00098; AAB59515.1; -; Genomic_DNA.
EMBL; M33043; AAB59372.1; -; Genomic_DNA.
EMBL; M33041; AAB59372.1; JOINED; Genomic_DNA.
EMBL; M33042; AAB59372.1; JOINED; Genomic_DNA.
EMBL; X01392; CAA25648.1; -; Genomic_DNA.
EMBL; X01388; CAA25644.1; -; mRNA.
EMBL; X03120; CAA26895.1; -; Genomic_DNA.
EMBL; V01513; CAA24757.1; -; mRNA.
EMBL; M28613; AAA51760.1; -; mRNA.
EMBL; M28614; AAA51761.1; -; mRNA.
EMBL; X00567; CAA25233.1; -; mRNA.
EMBL; AY422951; AAQ91810.1; -; Genomic_DNA.
EMBL; AY555191; AAS68230.1; -; Genomic_DNA.
EMBL; BC027977; AAH27977.1; -; mRNA.
EMBL; BC121081; AAI21082.1; -; mRNA.
CCDS; CCDS8377.1; -.
PIR; A90950; LPHUC3.
RefSeq; NP_000031.1; NM_000040.1.
UniGene; Hs.73849; -.
PDB; 2JQ3; NMR; -; A=21-99.
PDBsum; 2JQ3; -.
ProteinModelPortal; P02656; -.
SMR; P02656; -.
BioGrid; 106842; 23.
IntAct; P02656; 3.
STRING; 9606.ENSP00000227667; -.
CarbonylDB; P02656; -.
GlyConnect; 58; -.
iPTMnet; P02656; -.
PhosphoSitePlus; P02656; -.
UniCarbKB; P02656; -.
BioMuta; APOC3; -.
DMDM; 114026; -.
DOSAC-COBS-2DPAGE; P02656; -.
SWISS-2DPAGE; P02656; -.
MaxQB; P02656; -.
PaxDb; P02656; -.
PeptideAtlas; P02656; -.
PRIDE; P02656; -.
DNASU; 345; -.
Ensembl; ENST00000227667; ENSP00000227667; ENSG00000110245.
GeneID; 345; -.
KEGG; hsa:345; -.
UCSC; uc001ppt.2; human.
CTD; 345; -.
DisGeNET; 345; -.
EuPathDB; HostDB:ENSG00000110245.11; -.
GeneCards; APOC3; -.
HGNC; HGNC:610; APOC3.
MalaCards; APOC3; -.
MIM; 107720; gene.
MIM; 614028; phenotype.
neXtProt; NX_P02656; -.
OpenTargets; ENSG00000110245; -.
Orphanet; 79506; Cholesterol-ester transfer protein deficiency.
Orphanet; 33271; Non-alcoholic fatty liver disease.
PharmGKB; PA53; -.
eggNOG; ENOG410JE3N; Eukaryota.
eggNOG; ENOG4111APE; LUCA.
GeneTree; ENSGT00390000015395; -.
HOGENOM; HOG000247042; -.
HOVERGEN; HBG050549; -.
InParanoid; P02656; -.
KO; K08759; -.
PhylomeDB; P02656; -.
TreeFam; TF338209; -.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964058; HDL remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P02656; -.
ChiTaRS; APOC3; human.
EvolutionaryTrace; P02656; -.
GeneWiki; Apolipoprotein_C3; -.
GenomeRNAi; 345; -.
PRO; PR:P02656; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110245; -.
CleanEx; HS_APOC3; -.
ExpressionAtlas; P02656; baseline and differential.
Genevisible; P02656; HS.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL.
GO; GO:0030234; F:enzyme regulator activity; IDA:BHF-UCL.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0055102; F:lipase inhibitor activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034382; P:chylomicron remnant clearance; IDA:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
GO; GO:0060621; P:negative regulation of cholesterol import; IMP:BHF-UCL.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
GO; GO:0045833; P:negative regulation of lipid metabolic process; IDA:BHF-UCL.
GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IDA:BHF-UCL.
GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:BHF-UCL.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
GO; GO:0019433; P:triglyceride catabolic process; IDA:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IMP:HGNC.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; TAS:BHF-UCL.
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;
3D-structure; Chylomicron; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Lipid degradation; Lipid metabolism; Lipid transport; Polymorphism;
Reference proteome; Secreted; Sialic acid; Signal; Transport; VLDL.
SIGNAL 1 20 {ECO:0000269|PubMed:3949020,
ECO:0000269|PubMed:4846755}.
CHAIN 21 99 Apolipoprotein C-III.
{ECO:0000269|PubMed:3949020}.
/FTId=PRO_0000002031.
REGION 68 99 Lipid-binding.
SITE 37 37 May interact with the LDL receptor.
{ECO:0000305|PubMed:18408013}.
SITE 41 41 May interact with the LDL receptor.
{ECO:0000305|PubMed:18408013}.
SITE 44 44 May interact with the LDL receptor.
{ECO:0000305|PubMed:18408013}.
CARBOHYD 94 94 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:23527852,
ECO:0000269|PubMed:3123586}.
/FTId=CAR_000168.
VARIANT 78 78 K -> E (in HALP2; dbSNP:rs121918382).
{ECO:0000269|PubMed:2022742}.
/FTId=VAR_000643.
VARIANT 94 94 T -> A (in C-III-0; unglycosylated;
dbSNP:rs121918381).
{ECO:0000269|PubMed:3123586}.
/FTId=VAR_000644.
CONFLICT 52 53 ES -> SQ (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 57 59 QQA -> AQQ (in Ref. 8; AA sequence).
{ECO:0000305}.
HELIX 29 39 {ECO:0000244|PDB:2JQ3}.
HELIX 40 42 {ECO:0000244|PDB:2JQ3}.
HELIX 43 48 {ECO:0000244|PDB:2JQ3}.
HELIX 49 55 {ECO:0000244|PDB:2JQ3}.
HELIX 56 62 {ECO:0000244|PDB:2JQ3}.
TURN 63 68 {ECO:0000244|PDB:2JQ3}.
HELIX 69 80 {ECO:0000244|PDB:2JQ3}.
HELIX 83 85 {ECO:0000244|PDB:2JQ3}.
HELIX 93 98 {ECO:0000244|PDB:2JQ3}.
SEQUENCE 99 AA; 10852 MW; D4E806339FAE4DA7 CRC64;
MQPRVLLVVA LLALLASARA SEAEDASLLS FMQGYMKHAT KTAKDALSSV QESQVAQQAR
GWVTDGFSSL KDYWSTVKDK FSEFWDLDPE VRPTSAVAA


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