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P57791

- FACE2_MOUSE

UniProt

P57791 - FACE2_MOUSE

Protein

CAAX prenyl protease 2

Gene

Rce1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    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.By similarity

    Enzyme regulationi

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

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. CAAX-box protein processing Source: UniProtKB
    2. proteolysis Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    MEROPSiM79.002.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Rce1
    Synonyms:Face2, Rce1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1336895. Rce1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show defective Ras processing and mislocalization of Ras within cells.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 329328CAAX prenyl protease 2PRO_0000194831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    PaxDbiP57791.
    PRIDEiP57791.

    PTM databases

    PhosphoSiteiP57791.

    Expressioni

    Gene expression databases

    ArrayExpressiP57791.
    BgeeiP57791.
    GenevestigatoriP57791.

    Structurei

    3D structure databases

    ProteinModelPortaliP57791.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei36 – 5621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei75 – 9521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei112 – 13221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei193 – 21321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei226 – 24621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei254 – 27421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei282 – 30221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase U48 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG264307.
    GeneTreeiENSGT00390000004124.
    HOGENOMiHOG000006037.
    HOVERGENiHBG002541.
    InParanoidiP57791.
    KOiK08658.
    OMAiYSAFLFA.
    OrthoDBiEOG7F24TC.
    PhylomeDBiP57791.
    TreeFamiTF313800.

    Family and domain databases

    InterProiIPR003675. CAAX_protease.
    [Graphical view]
    PfamiPF02517. Abi. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P57791-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALGGDGLR LLSVSRPERQ PESAALSGPG SGLCCWVSVF SCFSLACSYV    50
    GSLYVWKSEL PRDHPAVIKR RSTSVLVVSS LSPLCVLLWR ELTGIQPGTS 100
    LLTLMGFRLE GIFPAALLPL LLTMILFLGP LMQLSMDCPC DLTDGLKVVL 150
    APRSWARCLT DMRWLRNQVI APLTEELVFR ACMLPMLAPC TGLGPAVFTC 200
    PLFFGVAHFH HIIEQLRFRQ SSVGSIFVSA AFQFSYTAVF GAYTAFLFIR 250
    TGHLIGPVLC HSFCNYMGFP AVCAALEHPQ KWPLLAGYAL GVGLFLLLLQ 300
    PLTDPKLYGS LPLCMLLERT GASETLLCS 329
    Length:329
    Mass (Da):35,867
    Last modified:April 27, 2001 - v1
    Checksum:iC2A49617EDC77EC8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 2711PERQPESAALS → QSGTRVSRAE(PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti62 – 621R → K in BAB28566. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251644 Genomic DNA. Translation: CAC17013.1.
    AJ251645 mRNA. Translation: CAC17014.1.
    AK012946 mRNA. Translation: BAB28566.1.
    CCDSiCCDS29432.1.
    RefSeqiNP_075620.1. NM_023131.1.
    UniGeneiMm.391143.

    Genome annotation databases

    EnsembliENSMUST00000025823; ENSMUSP00000025823; ENSMUSG00000024889.
    GeneIDi19671.
    KEGGimmu:19671.
    UCSCiuc008gaj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251644 Genomic DNA. Translation: CAC17013.1 .
    AJ251645 mRNA. Translation: CAC17014.1 .
    AK012946 mRNA. Translation: BAB28566.1 .
    CCDSi CCDS29432.1.
    RefSeqi NP_075620.1. NM_023131.1.
    UniGenei Mm.391143.

    3D structure databases

    ProteinModelPortali P57791.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1075287.

    Protein family/group databases

    MEROPSi M79.002.

    PTM databases

    PhosphoSitei P57791.

    Proteomic databases

    PaxDbi P57791.
    PRIDEi P57791.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025823 ; ENSMUSP00000025823 ; ENSMUSG00000024889 .
    GeneIDi 19671.
    KEGGi mmu:19671.
    UCSCi uc008gaj.1. mouse.

    Organism-specific databases

    CTDi 9986.
    MGIi MGI:1336895. Rce1.

    Phylogenomic databases

    eggNOGi NOG264307.
    GeneTreei ENSGT00390000004124.
    HOGENOMi HOG000006037.
    HOVERGENi HBG002541.
    InParanoidi P57791.
    KOi K08658.
    OMAi YSAFLFA.
    OrthoDBi EOG7F24TC.
    PhylomeDBi P57791.
    TreeFami TF313800.

    Miscellaneous databases

    NextBioi 296986.
    PROi P57791.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P57791.
    Bgeei P57791.
    Genevestigatori P57791.

    Family and domain databases

    InterProi IPR003675. CAAX_protease.
    [Graphical view ]
    Pfami PF02517. Abi. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiFACE2_MOUSE
    AccessioniPrimary (citable) accession number: P57791
    Secondary accession number(s): Q9CSF8, Q9EP68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3