RCE1

RCE1 homolog, prenyl protein peptidase (S. cerevisiae)

Identifiers

RCE1; FACE2; RCE1A; RCE1B

External IDs

OMIM: 605385 MGI: 1336895 HomoloGene: 3769 GeneCards: RCE1 Gene

3.4.22.-

Gene Ontology
Molecular function	• metalloendopeptidase activity • hydrolase activity
Cellular component	• endoplasmic reticulum • endoplasmic reticulum membrane • integral to plasma membrane • membrane
Biological process	• proteolysis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
66.61 – 66.61 Mb

Chr 19:
4.62 – 4.63 Mb

PubMed search

[1]

[2]

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.
^ ^a ^b "Entrez Gene: RCE1 RCE1 homolog, prenyl protein peptidase (S. cerevisiae)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9986.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2937830.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173957.
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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.

RCE1

References

Further reading