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P57791 (FACE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CAAX prenyl protease 2

EC=3.4.22.-
Alternative name(s):
Farnesylated proteins-converting enzyme 2
Short name=FACE-2
Prenyl protein-specific endoprotease 2
RCE1 homolog
Gene names
Name:Rce1
Synonyms:Face2, Rce1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 By similarity.

Enzyme regulation

Deubiquitination by USP17L2/USP17 negatively regulates the proteolytic activity toward Ras GTPases By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Ubiquitinated. Undergoes 'Lys-48'-and 'Lys-63'-linked ubiquitination. 'Lys-48' ubiquitination induces its degradation. Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains By similarity.

Disruption phenotype

Mice show defective Ras processing and mislocalization of Ras within cells. Ref.3

Sequence similarities

Belongs to the peptidase U48 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 329328CAAX prenyl protease 2
PRO_0000194831

Regions

Transmembrane36 – 5621Helical; Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane193 – 21321Helical; Potential
Transmembrane226 – 24621Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane282 – 30221Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict17 – 2711PERQPESAALS → QSGTRVSRAE Ref.2
Sequence conflict621R → K in BAB28566. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P57791 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: C2A49617EDC77EC8

FASTA32935,867
        10         20         30         40         50         60 
MAALGGDGLR LLSVSRPERQ PESAALSGPG SGLCCWVSVF SCFSLACSYV GSLYVWKSEL 

        70         80         90        100        110        120 
PRDHPAVIKR RSTSVLVVSS LSPLCVLLWR ELTGIQPGTS LLTLMGFRLE GIFPAALLPL 

       130        140        150        160        170        180 
LLTMILFLGP LMQLSMDCPC DLTDGLKVVL APRSWARCLT DMRWLRNQVI APLTEELVFR 

       190        200        210        220        230        240 
ACMLPMLAPC TGLGPAVFTC PLFFGVAHFH HIIEQLRFRQ SSVGSIFVSA AFQFSYTAVF 

       250        260        270        280        290        300 
GAYTAFLFIR TGHLIGPVLC HSFCNYMGFP AVCAALEHPQ KWPLLAGYAL GVGLFLLLLQ 

       310        320 
PLTDPKLYGS LPLCMLLERT GASETLLCS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and expression analysis of the gene encoding the murine Caax protease Face-2."
Cadinanos J., Freije J.M.P.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-329.
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells."
Kim E., Ambroziak P., Otto J.C., Taylor B., Ashby M., Shannon K., Casey P.J., Young S.G.
J. Biol. Chem. 274:8383-8390(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251644 Genomic DNA. Translation: CAC17013.1.
AJ251645 mRNA. Translation: CAC17014.1.
AK012946 mRNA. Translation: BAB28566.1.
CCDSCCDS29432.1.
RefSeqNP_075620.1. NM_023131.1.
UniGeneMm.391143.

3D structure databases

ProteinModelPortalP57791.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075287.

Protein family/group databases

MEROPSM79.002.

PTM databases

PhosphoSiteP57791.

Proteomic databases

PaxDbP57791.
PRIDEP57791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025823; ENSMUSP00000025823; ENSMUSG00000024889.
GeneID19671.
KEGGmmu:19671.
UCSCuc008gaj.1. mouse.

Organism-specific databases

CTD9986.
MGIMGI:1336895. Rce1.

Phylogenomic databases

eggNOGNOG264307.
GeneTreeENSGT00390000004124.
HOGENOMHOG000006037.
HOVERGENHBG002541.
InParanoidP57791.
KOK08658.
OMAYSAFLFA.
OrthoDBEOG7F24TC.
PhylomeDBP57791.
TreeFamTF313800.

Gene expression databases

ArrayExpressP57791.
BgeeP57791.
GenevestigatorP57791.

Family and domain databases

InterProIPR003675. CAAX_protease.
[Graphical view]
PfamPF02517. Abi. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296986.
PROP57791.
SOURCESearch...

Entry information

Entry nameFACE2_MOUSE
AccessionPrimary (citable) accession number: P57791
Secondary accession number(s): Q9CSF8, Q9EP68
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot