Apolipoprotein C-III precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P02656 (APOC3_HUMAN)

Last modified November 24, 2009. Version 102. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Apolipoprotein C-III
      Short name=Apo-CIII
      Short name=ApoC-III

Gene names

Name:

APOC3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	99 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles.
Subcellular location	Secreted.
Tissue specificity	Constitutes 50% of the protein fraction of VLDL and 2% of that of HDL. Synthesized predominantly in liver and to a lesser degree in intestine.
Post-translational modification	O-linked glycan consists of Gal-GalNAc disaccharide, further modified with up to 3 sialic acid residues.
Involvement in disease	Defects in APOC3 may be a cause of hyperalphalipoproteinemia [MIM:143470]. Affected individuals show high levels of alpha-lipoprotein (high density lipoprotein/HDL).
Sequence similarities	Belongs to the apolipoprotein C3 family.

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Ontologies

Keywords
Biological process	Lipid degradation Lipid transport Transport
Cellular component	Chylomicron Secreted VLDL
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	Cdc42 protein signal transduction Inferred from direct assay. Source: UniProtKB G-protein coupled receptor protein signaling pathway Inferred from direct assay. Source: UniProtKB cholesterol efflux Inferred from direct assay. Source: UniProtKB cholesterol homeostasis Inferred from mutant phenotype. Source: UniProtKB chylomicron remnant clearance Inferred from direct assay. Source: UniProtKB high-density lipoprotein particle remodeling Inferred from mutant phenotype. Source: UniProtKB lipoprotein metabolic process Inferred from electronic annotation. Source: InterPro negative regulation of cholesterol import Inferred from mutant phenotype. Source: UniProtKB negative regulation of fatty acid biosynthetic process Inferred from direct assay. Source: UniProtKB negative regulation of high-density lipoprotein particle clearance Inferred from mutant phenotype. Source: UniProtKB negative regulation of lipoprotein lipase activity Inferred from direct assay. Source: UniProtKB negative regulation of low-density lipoprotein particle clearance Inferred from mutant phenotype. Source: UniProtKB negative regulation of receptor-mediated endocytosis Inferred from direct assay. Source: UniProtKB negative regulation of triglyceride catabolic process Inferred from direct assay. Source: UniProtKB negative regulation of very-low-density lipoprotein particle clearance Inferred from direct assay. Source: UniProtKB negative regulation of very-low-density lipoprotein particle remodeling Inferred from direct assay. Source: UniProtKB phospholipid efflux Inferred from direct assay. Source: UniProtKB reverse cholesterol transport Inferred by curator. Source: UniProtKB triglyceride catabolic process Inferred from direct assay. Source: UniProtKB triglyceride homeostasis Inferred from mutant phenotype. Source: UniProtKB very-low-density lipoprotein particle assembly Traceable author statement. Source: UniProtKB
Cellular component	chylomicron Inferred from direct assay. Source: UniProtKB intermediate-density lipoprotein particle Inferred from direct assay. Source: UniProtKB spherical high-density lipoprotein particle Inferred from direct assay. Source: UniProtKB very-low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	cholesterol binding Inferred by curator. Source: UniProtKB high-density lipoprotein receptor binding Inferred from physical interaction. Source: UniProtKB lipase inhibitor activity Inferred from direct assay. Source: UniProtKB phospholipid binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.7 Ref.8

Chain

21 – 99

Apolipoprotein C-III Ref.7

PRO_0000002031

Regions

Region

68 – 99

Lipid-binding

Amino acid modifications

Glycosylation

O-linked (GalNAc...) Ref.9

CAR_000168

Natural variations

Natural variant

K → E in hyperalphalipoproteinemia. Ref.10

VAR_000643

Natural variant

T → A in C-III-0; unglycosylated. Ref.9

VAR_000644

Experimental info

Sequence conflict

52 – 53

ES → SQ AA sequence Ref.8

Sequence conflict

57 – 59

QQA → AQQ AA sequence Ref.8

Secondary structure

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P02656-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D4E806339FAE4DA7
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FASTA

10,852

        10         20         30         40         50         60 
MQPRVLLVVA LLALLASARA SEAEDASLLS FMQGYMKHAT KTAKDALSSV QESQVAQQAR 

        70         80         90 
GWVTDGFSSL KDYWSTVKDK FSEFWDLDPE VRPTSAVAA

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence analysis of the human apolipoprotein CIII gene and the intergenic region between the apo AI and apo CIII genes." Protter A.A., Levy-Wilson B., Miller J., Bencen G., White T., Seilhamer J.J. DNA 3:449-456(1984) [PubMed: 6439535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Isolation and DNA sequence of full-length cDNA for human preapolipoprotein CIII." Levy-Wilson B., Appleby V., Protter A.A., Auperin D., Seilhamer J.J. DNA 3:359-364(1984) [PubMed: 6548954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation and characterization of cDNA clones corresponding to two different human apoC-III alleles." Karathanasis S.K., Zannis V.I., Breslow J.L. J. Lipid Res. 26:451-456(1985) [PubMed: 2989400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance." Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C., Baralle F.E. Nucleic Acids Res. 12:3917-3932(1984) [PubMed: 6328445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster." 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. Hum. Genet. 115:36-56(2004) [PubMed: 15108119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Spleen.
[7]	"Amino acid sequence of human plasma apolipoprotein C-III from normolipidemic subjects." Hospattankar A.V., Brewer H.B. Jr., Ronan R., Fairwell T. FEBS Lett. 197:67-73(1986) [PubMed: 3949020] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-99.
[8]	"The complete amino acid sequence of alanine apolipoprotein (apoC-3), and apolipoprotein from human plasma very low density lipoproteins." Brewer H.B. Jr., Shulman R., Herbert P., Ronan R., Wehrly K. J. Biol. Chem. 249:4975-4984(1974) [PubMed: 4846755] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-99.
[9]	"Molecular cloning of a human apoC-III variant: Thr 74-->Ala 74 mutation prevents O-glycosylation." Maeda H., Hashimoto R.K., Oguro T., Hiraga S., Uzawa H. J. Lipid Res. 28:1405-1409(1987) [PubMed: 3123586] [Abstract] Cited for: VARIANT C-III-0 ALA-94, GLYCOSYLATION AT THR-94.
[10]	"Apolipoprotein C-III(Lys-58-->Glu). Identification of an apolipoprotein C-III variant in a family with hyperalphalipoproteinemia." von Eckardstein A., Holz H., Sandkamp M., Weng W., Funke H., Assmann G. J. Clin. Invest. 87:1724-1731(1991) [PubMed: 2022742] [Abstract] Cited for: VARIANT HYPERALPHALIPOPROTEINEMIA GLU-78.
+	Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

J00098 Genomic DNA. Translation: AAB59515.1.
M33043, M33041, M33042 Genomic DNA. Translation: AAB59372.1.
X01392 Genomic DNA. Translation: CAA25648.1.
X01388 mRNA. Translation: CAA25644.1.
X03120 Genomic DNA. Translation: CAA26895.1.
V01513 mRNA. Translation: CAA24757.1.
M28613 mRNA. Translation: AAA51760.1.
M28614 mRNA. Translation: AAA51761.1.
X00567 mRNA. Translation: CAA25233.1.
AY422951 Genomic DNA. Translation: AAQ91810.1.
AY555191 Genomic DNA. Translation: AAS68230.1.
BC027977 mRNA. Translation: AAH27977.1.
BC121081 mRNA. Translation: AAI21082.1.

IPI

IPI00021857.

PIR

LPHUC3. A90950.

RefSeq

NP_000031.1.

UniGene

Hs.73849

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JQ3	NMR	-	A	21-99	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P02656.

PTM databases

GlycoSuiteDB

P02656.

2-D gel databases

SWISS-2DPAGE

P02656.

DOSAC-COBS-2DPAGE

P02656.

Proteomic databases

PRIDE

P02656.

Genome annotation databases

Ensembl

ENST00000227667; ENSP00000227667; ENSG00000110245; Homo sapiens. [Genome view]
ENST00000360377; ENSP00000353540; ENSG00000110245; Homo sapiens. [Genome view]
ENST00000375345; ENSP00000364494; ENSG00000110245; Homo sapiens. [Genome view]

GeneID

345.

KEGG

hsa:345.

UCSC

uc001ppt.1. human.

Organism-specific databases

CTD

345.

GeneCards

GC11P116205.

H-InvDB

HIX0010157.
HIX0041426.

HGNC

HGNC:610. APOC3.

MIM

107720. gene.
143470. phenotype.

Orphanet

79506. Cholesterol-ester transfer protein deficiency.

PharmGKB

PA53.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02656.

HOVERGEN

P02656.

Enzyme and pathway databases

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P02656.

Bgee

P02656.

CleanEx

HS_APOC3.

Genevestigator

P02656.

GermOnline

ENSG00000110245. Homo sapiens.

Family and domain databases

InterPro

IPR008403. Apo-CIII.
[Graphical view]

PANTHER

PTHR14225. Apo-CIII. 1 hit.

Pfam

PF05778. Apo-CIII. 1 hit.
[Graphical view]

ProDom

PD010414. Apo-CIII. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other Resources

NextBio

1423.

SOURCE

Search...

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Entry information

Entry name

APOC3_HUMAN

Accession

Primary (citable) accession number: P02656
Secondary accession number(s): Q08E83, Q6Q786

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 24, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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