RCE1
Ras converting CAAX endopeptidase 1 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | RCE1 ; FACE2; RCE1A; RCE1B | ||||||||||||
External IDs | OMIM: 605385 MGI: 1336895 HomoloGene: 3769 ChEMBL: 3411 GeneCards: RCE1 Gene | ||||||||||||
EC number | 3.4.22.- | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 9986 | 19671 | |||||||||||
Ensembl | ENSG00000173653 | ENSMUSG00000024889 | |||||||||||
UniProt | Q9Y256 | P57791 | |||||||||||
RefSeq (mRNA) | NM_001032279 | NM_023131 | |||||||||||
RefSeq (protein) | NP_001027450 | NP_075620 | |||||||||||
Location (UCSC) |
Chr 11: 66.84 – 66.85 Mb |
Chr 19: 4.62 – 4.63 Mb | |||||||||||
PubMed search | |||||||||||||
CAAX prenyl protease 2 is an enzyme that in humans is encoded by the RCE1 gene.[1][2][3]
This gene encodes an integral membrane protein which is classified as a member of the metalloproteinase family. This enzyme is thought to function in the maintenance and processing of CAAX-type prenylated proteins.[3]
References
- ↑ Otto JC, Kim E, Young SG, Casey PJ (Apr 1999). "Cloning and characterization of a mammalian prenyl protein-specific protease". J Biol Chem 274 (13): 8379–82. doi:10.1074/jbc.274.13.8379. PMID 10085068.
- ↑ Freije JM, Blay P, Pendas AM, Cadinanos J, Crespo P, Lopez-Otin C (Jul 1999). "Identification and chromosomal location of two human genes encoding enzymes potentially involved in proteolytic maturation of farnesylated proteins". Genomics 58 (3): 270–80. doi:10.1006/geno.1999.5834. PMID 10373325.
- 1 2 "Entrez Gene: RCE1 RCE1 homolog, prenyl protein peptidase (S. cerevisiae)".
Further reading
- Plummer LJ, Hildebrandt ER, Porter SB, et al. (2006). "Mutational Analysis of the Ras Converting Enzyme Reveals a Requirement for Glutamate and Histidine Residues". J. Biol. Chem. 281 (8): 4596–605. doi:10.1074/jbc.M506284200. PMC 2937830. PMID 16361710.
- 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:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Bergo MO, Lieu HD, Gavino BJ, et al. (2004). "On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy". J. Biol. Chem. 279 (6): 4729–36. doi:10.1074/jbc.M310081200. PMID 14625273.
- Maske CP, Hollinshead MS, Higbee NC, et al. (2003). "A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation". J. Cell Biol. 162 (7): 1223–32. doi:10.1083/jcb.200303113. PMC 2173957. PMID 14504265.
- Hollander IJ, Frommer E, Aulabaugh A, Mallon R (2003). "Human Ras converting enzyme endoproteolytic specificity at the P2' and P3' positions of K-Ras-derived peptides". Biochim. Biophys. Acta 1649 (1): 24–9. doi:10.1016/s1570-9639(03)00150-x. PMID 12818187.
- 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:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Hollander I, Frommer E, Mallon R (2000). "Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides". Anal. Biochem. 286 (1): 129–37. doi:10.1006/abio.2000.4795. PMID 11038283.
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