RCE1

Protein-coding gene in the species Homo sapiens
RCE1
Identifiers
AliasesRCE1, FACE2, RCE1A, RCE1B, Ras converting CAAX endopeptidase 1
External IDsOMIM: 605385; MGI: 1336895; HomoloGene: 3769; GeneCards: RCE1; OMA:RCE1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for RCE1
Genomic location for RCE1
Band11q13.2Start66,842,835 bp[1]
End66,846,552 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for RCE1
Genomic location for RCE1
Band19|19 AStart4,622,591 bp[2]
End4,625,641 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS
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
SpeciesHumanMouse
Entrez

9986

19671

Ensembl

ENSG00000173653

ENSMUSG00000024889

UniProt

Q9Y256

P57791

RefSeq (mRNA)

NM_005133
NM_001032279

NM_023131

RefSeq (protein)

NP_001027450
NP_005124

NP_075620
NP_001355641
NP_001355642
NP_001355643
NP_001355644

Location (UCSC)Chr 11: 66.84 – 66.85 MbChr 19: 4.62 – 4.63 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000173653 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  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.
  7. ^ a b "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. 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.


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