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P02655 (APOC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein C-II

Short name=Apo-CII
Short name=ApoC-II
Alternative name(s):
Apolipoprotein C2
Gene names
Name:APOC2
Synonyms:APC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly.

Subcellular location

Secreted.

Tissue specificity

Secreted in plasma.

Involvement in disease

Hyperlipoproteinemia 1B (HLPP1B) [MIM:207750]: Autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the apolipoprotein C2 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
Lipid transport
Transport
   Cellular componentChylomicron
Secreted
VLDL
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hyperlipidemia
   DomainSignal
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol efflux

Inferred from direct assay PubMed 11162594. Source: BHF-UCL

cholesterol homeostasis

Inferred by curator PubMed 15778093. Source: BHF-UCL

chylomicron remnant clearance

Inferred from direct assay PubMed 4020294. Source: BHF-UCL

chylomicron remodeling

Inferred by curator PubMed 10727238. Source: BHF-UCL

high-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 15778093. Source: BHF-UCL

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein metabolic process

Traceable author statement. Source: Reactome

lipoprotein transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of catalytic activity

Inferred from direct assay PubMed 182536. Source: GOC

negative regulation of cholesterol transport

Inferred from mutant phenotype PubMed 15778093. Source: BHF-UCL

negative regulation of lipid metabolic process

Inferred from direct assay PubMed 182536. Source: BHF-UCL

negative regulation of receptor-mediated endocytosis

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

negative regulation of very-low-density lipoprotein particle clearance

Inferred from direct assay PubMed 1917954. Source: BHF-UCL

phospholipid efflux

Inferred from direct assay PubMed 11162594. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of fatty acid biosynthetic process

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

positive regulation of lipoprotein lipase activity

Inferred from direct assay PubMed 10727238PubMed 15878877. Source: BHF-UCL

positive regulation of phospholipase activity

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

positive regulation of phospholipid catabolic process

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

positive regulation of triglyceride catabolic process

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

positive regulation of very-low-density lipoprotein particle remodeling

Inferred by curator PubMed 10727238. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

reverse cholesterol transport

Inferred by curator PubMed 15778093. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride homeostasis

Inferred from mutant phenotype PubMed 17018885. Source: BHF-UCL

triglyceride-rich lipoprotein particle remodeling

Traceable author statement PubMed 17018885. Source: BHF-UCL

very-low-density lipoprotein particle remodeling

Traceable author statement PubMed 15778093. Source: BHF-UCL

   Cellular_componentchylomicron

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

early endosome

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

intermediate-density lipoprotein particle

Inferred from direct assay PubMed 17336988. Source: BHF-UCL

low-density lipoprotein particle

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

spherical high-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

   Molecular_functionlipase inhibitor activity

Inferred from direct assay PubMed 182536. Source: BHF-UCL

lipid binding

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

lipoprotein lipase activator activity

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

phospholipase activator activity

Inferred from direct assay PubMed 10727238. Source: BHF-UCL

phospholipase binding

Inferred from physical interaction PubMed 10727238. Source: BHF-UCL

protein homodimerization activity

Inferred from mutant phenotype PubMed 8245722. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.13 Ref.14
Chain23 – 10179Apolipoprotein C-II
PRO_0000002024

Regions

Region23 – 3816O-glycosylated at one site
Region43 – 519Lipid binding
Region55 – 7824Lipoprotein lipase cofactor

Natural variations

Natural variant411K → T. Ref.21 Ref.22
VAR_000639
Natural variant481W → R in HLPP1B; variant Wakayama. Ref.23
VAR_000640
Natural variant601E → K in San Francisco; found in hyperlipidemic patients. Ref.20
Corresponds to variant rs5122 [ dbSNP | Ensembl ].
VAR_000641
Natural variant771K → Q in Africa. Ref.19 Ref.24
Corresponds to variant rs5126 [ dbSNP | Ensembl ].
VAR_000642

Experimental info

Sequence conflict361F → L Ref.7
Sequence conflict361F → L Ref.8

Secondary structure

................... 101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02655 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 51CB86FEDB174D84

FASTA10111,284
        10         20         30         40         50         60 
MGTRLLPALF LVLLVLGFEV QGTQQPQQDE MPSPTFLTQV KESLSSYWES AKTAAQNLYE 

        70         80         90        100 
KTYLPAVDEK LRDLYSKSTA AMSTYTGIFT DQVLSVLKGE E 

« Hide

References

« Hide 'large scale' references
[1]"The human preproapolipoprotein C-II gene. Complete nucleic acid sequence and genomic organization."
Fojo S.S., Law S.W., Brewer H.B. Jr.
FEBS Lett. 213:221-226(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human apolipoprotein C-II: complete nucleic acid sequence of preapolipoprotein C-II."
Fojo S.S., Law S.W., Brewer H.B. Jr.
Proc. Natl. Acad. Sci. U.S.A. 81:6354-6357(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The human apolipoprotein C-II gene sequence contains a novel chromosome 19-specific minisatellite in its third intron."
Das H.K., Jackson C.L., Miller D.A., Leff T., Breslow J.L.
J. Biol. Chem. 262:4787-4793(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The structure of the human apolipoprotein C-II gene. Electron microscopic analysis of RNA:DNA hybrids, complete nucleotide sequence, and identification of 5' homologous sequences among apolipoprotein genes."
Wei C.F., Tsao Y.K., Robberson D.L., Gotto A.M. Jr., Brown K., Chan L.
J. Biol. Chem. 260:15211-15221(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[6]Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H., Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[11]"The isolation and characterization of cDNA clones for human apolipoprotein CII."
Myklebost O., Williamson B., Markham A.F., Myklebost S.R., Rogers J., Woods D.E., Humphries S.E.
J. Biol. Chem. 259:4401-4404(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-101.
[12]"Isolation of cDNA and genomic clones for apolipoprotein C-II."
Jackson C.L., Bruns G.A.P., Breslow J.L.
Methods Enzymol. 128:788-800(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 11-101.
[13]"Amino acid sequence of human plasma apolipoprotein C-II from normal and hyperlipoproteinemic subjects."
Hospattankar A.V., Fairwell T., Ronan R., Brewer H.B. Jr.
J. Biol. Chem. 259:318-322(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-101.
[14]"Primary structure of very low density apolipoprotein C-II of human plasma."
Jackson R.L., Baker H.N., Gilliam E.B., Gotto A.M. Jr.
Proc. Natl. Acad. Sci. U.S.A. 74:1942-1945(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-101.
[15]"Expression of the apolipoprotein C-II gene during myelomonocytic differentiation of human leukemic cells."
Chun E.M., Park Y.J., Kang H.S., Cho H.M., Jun D.Y., Kim Y.H.
J. Leukoc. Biol. 69:645-650(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-101.
[16]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII."
Lycksell P.-O., Oehman A., Bengtsson-Olivecrona G., Johansson L.B.-A., Wijmenga S.S., Wernic D., Graeslund A.
Eur. J. Biochem. 205:223-231(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 72-101.
[18]"A refined three-dimensional solution structure of a carboxy terminal fragment of apolipoprotein CII."
Oehman A., Lycksell P.-O., Graeslund A.
Eur. Biophys. J. 22:351-357(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 72-101.
[19]"A variant primary structure of apolipoprotein C-II in individuals of African descent."
Menzel H.-J., Kane J.P., Malloy M.J., Havel R.J.
J. Clin. Invest. 77:595-601(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AFRICA GLN-77.
[20]"Molecular cloning and characteristics of a new apolipoprotein C-II mutant identified in three unrelated individuals with hypercholesterolemia and hypertriglyceridemia."
Pullinger C.R., Zysow B.R., Hennessy L.K., Frost P.H., Malloy M.J., Kanr J.P.
Hum. Mol. Genet. 2:69-74(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SAN FRANCISCO LYS-60.
[21]"An apolipoprotein CII mutation, CII Lys-19-->Thr identified in patients with hyperlipidemia."
Hegele R.A., Connelly P.W., Maguire G.F., Huff M.W., Leiter L., Wolfe B.M., Evans A.J., Little J.A.
Dis. Markers 9:73-80(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-41.
[22]"The apolipoprotein C-II variant apoC-II Lys-19-->Thr is not associated with dyslipidemia in an affected kindred."
Zysow B.R., Pullinger C.R., Hennessy L.K., Farese R.V. Jr., Ghassemzadeh M., Kane J.P.
Clin. Genet. 45:292-297(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-41.
[23]"A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama)."
Inadera H., Hibino A., Kobayashi J., Kanzaki T., Shirai K., Yukawa S., Saito Y., Yoshida S.
Biochem. Biophys. Res. Commun. 193:1174-1183(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1B WAKAYAMA ARG-48.
[24]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-77.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05151 Genomic DNA. Translation: CAA28798.1.
X00568 mRNA. Translation: CAA25234.1.
J02698 Genomic DNA. Translation: AAA98743.1.
AY422955 Genomic DNA. Translation: AAQ91814.1.
BT006708 mRNA. Translation: AAP35354.1.
FJ525875 Genomic DNA. Translation: ACN81313.1.
CH471126 Genomic DNA. Translation: EAW57311.1.
BC005348 mRNA. Translation: AAH05348.3.
M29844 mRNA. Translation: AAA51743.1.
M10612 Genomic DNA. Translation: AAB59380.1.
AF113884 mRNA. Translation: AAD28193.1.
PIRLPHUC2. A24238.
RefSeqNP_000474.2. NM_000483.4.
UniGeneHs.75615.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY6NMR-A66-101[»]
1I5JNMR-A23-101[»]
1O8TNMR-A23-101[»]
1SOHNMR-A23-101[»]
ProteinModelPortalP02655.
SMRP02655. Positions 23-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106841. 2 interactions.
IntActP02655. 4 interactions.
STRING9606.ENSP00000252490.

PTM databases

PhosphoSiteP02655.

Polymorphism databases

DMDM114022.

2D gel databases

DOSAC-COBS-2DPAGEP02655.
SWISS-2DPAGEP02655.

Proteomic databases

PaxDbP02655.
PeptideAtlasP02655.
PRIDEP02655.

Protocols and materials databases

DNASU344.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252490; ENSP00000252490; ENSG00000234906.
ENST00000590360; ENSP00000466775; ENSG00000234906.
GeneID344.
KEGGhsa:344.

Organism-specific databases

CTD344.
GeneCardsGC19P045449.
HGNCHGNC:609. APOC2.
HPAHPA055877.
MIM207750. phenotype.
608083. gene.
neXtProtNX_P02655.
Orphanet309020. Familial apolipoprotein C-II deficiency.
PharmGKBPA52.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25045.
HOGENOMHOG000034002.
HOVERGENHBG050548.
InParanoidP02655.
PhylomeDBP02655.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP02655.
CleanExHS_APC2.
HS_APOC2.
GenevestigatorP02655.

Family and domain databases

Gene3D1.10.1440.10. 1 hit.
InterProIPR008019. Apo-CII.
IPR023121. ApoC-II_domain.
[Graphical view]
PANTHERPTHR16566. PTHR16566. 1 hit.
PfamPF05355. Apo-CII. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02655.
GeneWikiApolipoprotein_C2.
GenomeRNAi344.
NextBio1419.
PMAP-CutDBP02655.
PROP02655.
SOURCESearch...

Entry information

Entry nameAPOC2_HUMAN
AccessionPrimary (citable) accession number: P02655
Secondary accession number(s): C0JYY4 expand/collapse secondary AC list , Q9BS39, Q9UDE3, Q9UNK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM