RCE1

RCE1
Identifiers
Aliases	RCE1, FACE2, RCE1A, RCE1B, Ras converting CAAX endopeptidase 1
External IDs	OMIM: 605385; MGI: 1336895; GeneCards: RCE1
Enzyme activity
Gene location (Human)
Chr.	Chromosome 11 (human)
End	66,846,552 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	4,625,641 bp
RNA expression pattern
	Top expressed in
	mucosa of transverse colon; ; right hemisphere of cerebellum; ; granulocyte; ; right testis; ; left testis; ; skin of abdomen; ; parotid gland; ; gonad; ; anterior pituitary; ; skin of leg;
	Top expressed in
	white adipose tissue; ; proximal tubule; ; right kidney; ; bone marrow; ; yolk sac; ; adrenal gland; ; placenta; ; lip; ; islet of Langerhans; ; mesencephalon;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	peptidase activity; cysteine-type endopeptidase activity; endopeptidase activity; metalloendopeptidase activity; hydrolase activity;
Cellular component	integral component of membrane; integral component of endoplasmic reticulum membrane; integral component of plasma membrane; endoplasmic reticulum membrane; membrane; endoplasmic reticulum; cytosol;
Biological process	proteolysis; CAAX-box protein processing; protein deubiquitination;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	9986
	19671
	ENSG00000173653
	ENSMUSG00000024889
	Q9Y256
	P57791
	NM_005133; NM_001032279
	NM_023131
	NP_001027450; NP_005124
	NP_075620; NP_001355641; NP_001355642; NP_001355643; NP_001355644
	Wikidata
View/Edit Human	View/Edit Mouse

CAAX prenyl protease 2 is an enzyme that in humans is encoded by the RCE1 gene.^[5]^[6]^[7]

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.^[7]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000173653 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024889 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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)".

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. Bibcode:2002PNAS...9916899M. 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.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000173653 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024889 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10085068-5] 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.

[pmid10373325-6] 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.

[entrez-7] 1 2 "Entrez Gene: RCE1 RCE1 homolog, prenyl protein peptidase (S. cerevisiae)".

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This page was redesigned at the edge.

RCE1

References

Further reading