Summary: Apolipoprotein C-II
This is the Wikipedia entry entitled "Apolipoprotein C2". More...
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Apolipoprotein C2 Edit Wikipedia article
PDB rendering based on 1by6.
|nmr structure of human apolipoprotein c-ii in the presence of sds|
The protein encoded by this gene is secreted in plasma where it is a component of very low density lipoproteins and chylomicrons. This protein activates the enzyme lipoprotein lipase in capillaries, which hydrolyzes triglycerides and thus provides free fatty acids for cells. Mutations in this gene cause hyperlipoproteinemia type IB, characterized by xanthomas, pancreatitis, and hepatosplenomegaly, but no increased risk for atherosclerosis. Lab tests will show elevated blood levels of triglycerides, cholesterol, and chylomicrons
 Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
- The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430". http://www.wikipathways.org/index.php/Pathway:WP430.
 See also
- Kim SY, Park SM, Lee ST (2006). "Apolipoprotein C-II is a novel substrate for matrix metalloproteinases". Biochem. Biophys. Res. Commun. 339 (1): 47–54. doi:10.1016/j.bbrc.2005.10.182. PMID 16314153.
- "Entrez Gene: APOC2 apolipoprotein C-II". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=344.
- Jackson RL, Baker HN, Gilliam EB, Gotto AM (1977). "Primary structure of very low density apolipoprotein C-II of human plasma.". Proc. Natl. Acad. Sci. U.S.A. 74 (5): 1942–5. doi:10.1073/pnas.74.5.1942. PMC 431048. PMID 194244. //www.ncbi.nlm.nih.gov/pmc/articles/PMC431048/.
- Lycksell PO, Ohman A, Bengtsson-Olivecrona G, et al. (1992). "Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII.". Eur. J. Biochem. 205 (1): 223–31. doi:10.1111/j.1432-1033.1992.tb16772.x. PMID 1555583.
- Hegele RA, Connelly PW, Maguire GF, et al. (1992). "An apolipoprotein CII mutation, CIILys19----Thr' identified in patients with hyperlipidemia.". Dis. Markers 9 (2): 73–80. PMID 1782747.
- Crecchio C, Capurso A, Pepe G (1990). "Identification of the mutation responsible for a case of plasmatic apolipoprotein CII deficiency (Apo CII-Bari).". Biochem. Biophys. Res. Commun. 168 (3): 1118–27. doi:10.1016/0006-291X(90)91145-I. PMID 1971748.
- Bengtsson-Olivecrona G, Sletten K (1990). "Primary structure of the bovine analogues to human apolipoproteins CII and CIII. Studies on isoforms and evidence for proteolytic processing.". Eur. J. Biochem. 192 (2): 515–21. doi:10.1111/j.1432-1033.1990.tb19255.x. PMID 2209608.
- Wei CF, Tsao YK, Robberson DL, et al. (1986). "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.". J. Biol. Chem. 260 (28): 15211–21. PMID 2415514.
- Fojo SS, Lohse P, Parrott C, et al. (1989). "A nonsense mutation in the apolipoprotein C-IIPadova gene in a patient with apolipoprotein C-II deficiency.". J. Clin. Invest. 84 (4): 1215–9. doi:10.1172/JCI114287. PMC 329780. PMID 2477392. //www.ncbi.nlm.nih.gov/pmc/articles/PMC329780/.
- Jackson CL, Bruns GA, Breslow JL (1986). "Isolation of cDNA and genomic clones for apolipoprotein C-II". Meth. Enzymol.. Methods in Enzymology 128: 788–800. doi:10.1016/0076-6879(86)28106-9. ISBN 9780121820282. PMID 3014272.
- Fojo SS, Law SW, Brewer HB (1987). "The human preproapolipoprotein C-II gene. Complete nucleic acid sequence and genomic organization". FEBS Lett. 213 (1): 221–6. doi:10.1016/0014-5793(87)81495-3. PMID 3030808.
- Fojo SS, Stalenhoef AF, Marr K, et al. (1989). "A deletion mutation in the ApoC-II gene (ApoC-II Nijmegen) of a patient with a deficiency of apolipoprotein C-II". J. Biol. Chem. 263 (34): 17913–6. PMID 3192518.
- Fojo SS, Beisiegel U, Beil U, et al. (1988). "Donor splice site mutation in the apolipoprotein (Apo) C-II gene (Apo C-IIHamburg) of a patient with Apo C-II deficiency". J. Clin. Invest. 82 (5): 1489–94. doi:10.1172/JCI113756. PMC 442713. PMID 3263393. //www.ncbi.nlm.nih.gov/pmc/articles/PMC442713/.
- Connelly PW, Maguire GF, Hofmann T, Little JA (1987). "Structure of apolipoprotein C-IIToronto, a nonfunctional human apolipoprotein". Proc. Natl. Acad. Sci. U.S.A. 84 (1): 270–3. doi:10.1073/pnas.84.1.270. PMC 304185. PMID 3467353. //www.ncbi.nlm.nih.gov/pmc/articles/PMC304185/.
- Fairwell T, Hospattankar AV, Brewer HB, Khan SA (1987). "Human plasma apolipoprotein C-II: total solid-phase synthesis and chemical and biological characterization". Proc. Natl. Acad. Sci. U.S.A. 84 (14): 4796–800. doi:10.1073/pnas.84.14.4796. PMC 305192. PMID 3474626. //www.ncbi.nlm.nih.gov/pmc/articles/PMC305192/.
- Fojo SS, Taam L, Fairwell T, et al. (1986). "Human preproapolipoprotein C-II. Analysis of major plasma isoforms". J. Biol. Chem. 261 (21): 9591–4. PMID 3525527.
- Das HK, Jackson CL, Miller DA, et al. (1987). "The human apolipoprotein C-II gene sequence contains a novel chromosome 19-specific minisatellite in its third intron". J. Biol. Chem. 262 (10): 4787–93. PMID 3558370.
- Connelly PW, Maguire GF, Little JA (1988). "Apolipoprotein CIISt. Michael. Familial apolipoprotein CII deficiency associated with premature vascular disease". J. Clin. Invest. 80 (6): 1597–606. doi:10.1172/JCI113246. PMC 442428. PMID 3680515. //www.ncbi.nlm.nih.gov/pmc/articles/PMC442428/.
- Baggio G, Manzato E, Gabelli C, et al. (1986). "Apolipoprotein C-II deficiency syndrome. Clinical features, lipoprotein characterization, lipase activity, and correction of hypertriglyceridemia after apolipoprotein C-II administration in two affected patients". J. Clin. Invest. 77 (2): 520–7. doi:10.1172/JCI112332. PMC 423374. PMID 3944267. //www.ncbi.nlm.nih.gov/pmc/articles/PMC423374/.
- Menzel HJ, Kane JP, Malloy MJ, Havel RJ (1986). "A variant primary structure of apolipoprotein C-II in individuals of African descent". J. Clin. Invest. 77 (2): 595–601. doi:10.1172/JCI112342. PMC 423392. PMID 3944271. //www.ncbi.nlm.nih.gov/pmc/articles/PMC423392/.
- Sharpe CR, Sidoli A, Shelley CS, et al. (1984). "Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance". Nucleic Acids Res. 12 (9): 3917–32. doi:10.1093/nar/12.9.3917. PMC 318799. PMID 6328445. //www.ncbi.nlm.nih.gov/pmc/articles/PMC318799/.
- Jackson CL, Bruns GA, Breslow JL (1984). "Isolation and sequence of a human apolipoprotein CII cDNA clone and its use to isolate and map to human chromosome 19 the gene for apolipoprotein CII". Proc. Natl. Acad. Sci. U.S.A. 81 (10): 2945–9. doi:10.1073/pnas.81.10.2945. PMC 345197. PMID 6328478. //www.ncbi.nlm.nih.gov/pmc/articles/PMC345197/.
Apolipoprotein C-II Provide feedback
Apolipoprotein C-II (ApoC-II) is the major activator of lipoprotein lipase, a key enzyme in the regulation of triglyceride levels in human serum .
Storjohann R, Rozek A, Sparrow JT, Cushley RJ; , Biochim Biophys Acta 2000;1486:253-264.: Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine. PUBMED:10903476 EPMC:10903476
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008019
Apolipoprotein CII (apoC-II) is a surface constituent of plasma lipoproteins and the activator for lipoprotein lipase (LPL). It is therefore central for lipid transport in blood. Lipoprotein lipase is a key enzyme in the regulation of triglyceride levels in human serum [PUBMED:10903476]. It is the C-terminal helix of apoC-II that is responsible for the activation of LPL [PUBMED:12590574]. The active peptide of apoC-II occurs at residues 44-79 and has been shown to reverse the symptoms of genetic apoC-II deficiency in a human subject [PUBMED:10903476].
Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix. The first 12 residues of apoC-II are structurally heterogeneous but the rest of the protein forms a predominantly helical structure [PUBMED:11331005].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||chylomicron (GO:0042627)|
|Molecular function||enzyme activator activity (GO:0008047)|
|Biological process||lipid transport (GO:0006869)|
|lipid metabolic process (GO:0006629)|
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|Seed source:||Pfam-B_6456 (release 7.8)|
|Number in seed:||6|
|Number in full:||40|
|Average length of the domain:||73.00 aa|
|Average identity of full alignment:||46 %|
|Average coverage of the sequence by the domain:||75.96 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Apo-CII domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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