FACE2_MOUSE
ID FACE2_MOUSE Reviewed; 329 AA.
AC P57791; Q9CSF8; Q9EP68;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=CAAX prenyl protease 2;
DE EC=3.4.-.-;
DE AltName: Full=Farnesylated proteins-converting enzyme 2;
DE Short=FACE-2;
DE AltName: Full=Prenyl protein-specific endoprotease 2;
DE AltName: Full=RCE1 homolog;
GN Name=Rce1; Synonyms=Face2, Rce1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Cadinanos J., Freije J.M.P.;
RT "Characterization and expression analysis of the gene encoding the murine
RT Caax protease Face-2.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-329.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10085069; DOI=10.1074/jbc.274.13.8383;
RA Kim E., Ambroziak P., Otto J.C., Taylor B., Ashby M., Shannon K.,
RA Casey P.J., Young S.G.;
RT "Disruption of the mouse Rce1 gene results in defective Ras processing and
RT mislocalization of Ras within cells.";
RL J. Biol. Chem. 274:8383-8390(1999).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated and geranylated proteins. Seems to be able to process K-
CC Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y256, ECO:0000305|PubMed:10085069}.
CC -!- ACTIVITY REGULATION: Deubiquitination by USP17L2/USP17 negatively
CC regulates the proteolytic activity toward Ras GTPases.
CC {ECO:0000250|UniProtKB:Q9Y256}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y256}.
CC -!- PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked
CC ubiquitination. 'Lys-48' ubiquitination induces its degradation.
CC Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin
CC chains (By similarity). {ECO:0000250|UniProtKB:Q9Y256}.
CC -!- DISRUPTION PHENOTYPE: Mice show defective Ras processing and
CC mislocalization of Ras within cells. {ECO:0000269|PubMed:10085069}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; AJ251644; CAC17013.1; -; Genomic_DNA.
DR EMBL; AJ251645; CAC17014.1; -; mRNA.
DR EMBL; AK012946; BAB28566.1; -; mRNA.
DR CCDS; CCDS29432.1; -.
DR RefSeq; NP_075620.1; NM_023131.1.
DR AlphaFoldDB; P57791; -.
DR BioGRID; 202838; 2.
DR STRING; 10090.ENSMUSP00000025823; -.
DR ChEMBL; CHEMBL1075287; -.
DR MEROPS; G05.002; -.
DR iPTMnet; P57791; -.
DR PhosphoSitePlus; P57791; -.
DR SwissPalm; P57791; -.
DR EPD; P57791; -.
DR MaxQB; P57791; -.
DR PaxDb; P57791; -.
DR PeptideAtlas; P57791; -.
DR PRIDE; P57791; -.
DR ProteomicsDB; 277034; -.
DR Antibodypedia; 16385; 130 antibodies from 26 providers.
DR DNASU; 19671; -.
DR Ensembl; ENSMUST00000025823; ENSMUSP00000025823; ENSMUSG00000024889.
DR GeneID; 19671; -.
DR KEGG; mmu:19671; -.
DR UCSC; uc008gaj.1; mouse.
DR CTD; 9986; -.
DR MGI; MGI:1336895; Rce1.
DR VEuPathDB; HostDB:ENSMUSG00000024889; -.
DR eggNOG; KOG4130; Eukaryota.
DR GeneTree; ENSGT00390000004124; -.
DR HOGENOM; CLU_049909_3_0_1; -.
DR InParanoid; P57791; -.
DR OMA; HSFCNWC; -.
DR OrthoDB; 1607650at2759; -.
DR PhylomeDB; P57791; -.
DR TreeFam; TF313800; -.
DR BRENDA; 3.4.99.B1; 3474.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 19671; 15 hits in 76 CRISPR screens.
DR PRO; PR:P57791; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P57791; protein.
DR Bgee; ENSMUSG00000024889; Expressed in white adipose tissue and 62 other tissues.
DR ExpressionAtlas; P57791; baseline and differential.
DR Genevisible; P57791; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008238; F:exopeptidase activity; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0071586; P:CAAX-box protein processing; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; ISO:MGI.
DR InterPro; IPR039731; Rce1.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR13046; PTHR13046; 1.
DR Pfam; PF02517; Rce1-like; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y256"
FT CHAIN 2..329
FT /note="CAAX prenyl protease 2"
FT /id="PRO_0000194831"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 175
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT ACT_SITE 208
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 261
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 265
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y256"
FT CONFLICT 17..27
FT /note="PERQPESAALS -> QSGTRVSRAE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="R -> K (in Ref. 2; BAB28566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 35867 MW; C2A49617EDC77EC8 CRC64;
MAALGGDGLR LLSVSRPERQ PESAALSGPG SGLCCWVSVF SCFSLACSYV GSLYVWKSEL
PRDHPAVIKR RSTSVLVVSS LSPLCVLLWR ELTGIQPGTS LLTLMGFRLE GIFPAALLPL
LLTMILFLGP LMQLSMDCPC DLTDGLKVVL APRSWARCLT DMRWLRNQVI APLTEELVFR
ACMLPMLAPC TGLGPAVFTC PLFFGVAHFH HIIEQLRFRQ SSVGSIFVSA AFQFSYTAVF
GAYTAFLFIR TGHLIGPVLC HSFCNYMGFP AVCAALEHPQ KWPLLAGYAL GVGLFLLLLQ
PLTDPKLYGS LPLCMLLERT GASETLLCS
