ANGPTL3
From Wikipedia, the free encyclopedia
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Angiopoietin-like 3
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| Identifiers | ||||||||||||||
| Symbol(s) | ANGPTL3; ANGPT5 | |||||||||||||
| External IDs | OMIM: 604774 MGI: 1353627 HomoloGene: 8499 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 27329 | 30924 | ||||||||||||
| Ensembl | ENSG00000132855 | ENSMUSG00000028553 | ||||||||||||
| Uniprot | Q9Y5C1 | Q3UEF5 | ||||||||||||
| Refseq | NM_014495 (mRNA) NP_055310 (protein) |
NM_013913 (mRNA) NP_038941 (protein) |
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| Location | Chr 1: 62.84 - 62.84 Mb | Chr 4: 98.52 - 98.53 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Angiopoietin-like 3, also known as ANGPTL3, is a human gene.[1]
The protein encoded by this gene is a member of the angiopoietin-like family of secreted factors. It is predominantly expressed in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. This protein may also play a role in the regulation of angiogenesis.[1]
[edit] References
[edit] Further reading
- Li C (2007). "Genetics and regulation of angiopoietin-like proteins 3 and 4.". Curr. Opin. Lipidol. 17 (2): 152–6. doi:. PMID 16531751.
- Conklin D, Gilbertson D, Taft DW, et al. (2000). "Identification of a mammalian angiopoietin-related protein expressed specifically in liver.". Genomics 62 (3): 477–82. doi:. PMID 10644446.
- Camenisch G, Pisabarro MT, Sherman D, et al. (2002). "ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo.". J. Biol. Chem. 277 (19): 17281–90. doi:. PMID 11877390.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:. PMID 12477932.
- Kaplan R, Zhang T, Hernandez M, et al. (2003). "Regulation of the angiopoietin-like protein 3 gene by LXR.". J. Lipid Res. 44 (1): 136–43. PMID 12518032.
- Shimamura M, Matsuda M, Kobayashi S, et al. (2003). "Angiopoietin-like protein 3, a hepatic secretory factor, activates lipolysis in adipocytes.". Biochem. Biophys. Res. Commun. 301 (2): 604–9. PMID 12565906.
- Zeng L, Dai J, Ying K, et al. (2003). "Identification of a novel human angiopoietin-like gene expressed mainly in heart.". J. Hum. Genet. 48 (3): 159–62. doi:. PMID 12624729.
- Ono M, Shimizugawa T, Shimamura M, et al. (2004). "Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo.". J. Biol. Chem. 278 (43): 41804–9. doi:. PMID 12909640.
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:. PMID 12975309.
- Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites.". Protein Sci. 13 (10): 2819–24. doi:. PMID 15340161.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:. PMID 15489334.
- Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. doi:. PMID 16335952.
- Shimamura M, Matsuda M, Yasumo H, et al. (2007). "Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase.". Arterioscler. Thromb. Vasc. Biol. 27 (2): 366–72. doi:. PMID 17110602.

