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   24-JAN-2024, entry version 153.
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; 10090-ENSMUSP00000025823; -.
DR   PeptideAtlas; P57791; -.
DR   ProteomicsDB; 277034; -.
DR   Pumba; P57791; -.
DR   Antibodypedia; 16385; 145 antibodies from 26 providers.
DR   DNASU; 19671; -.
DR   Ensembl; ENSMUST00000025823.6; ENSMUSP00000025823.4; ENSMUSG00000024889.6.
DR   GeneID; 19671; -.
DR   KEGG; mmu:19671; -.
DR   UCSC; uc008gaj.1; mouse.
DR   AGR; MGI:1336895; -.
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; 25538at2759; -.
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 81 CRISPR screens.
DR   PRO; PR:P57791; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P57791; Protein.
DR   Bgee; ENSMUSG00000024889; Expressed in white adipose tissue and 65 other cell types or tissues.
DR   ExpressionAtlas; P57791; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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   InterPro; IPR039731; Rce1.
DR   InterPro; IPR003675; Rce1-like.
DR   PANTHER; PTHR13046:SF0; CAAX PRENYL PROTEASE 2; 1.
DR   PANTHER; PTHR13046; PROTEASE U48 CAAX PRENYL PROTEASE RCE1; 1.
DR   Pfam; PF02517; Rce1-like; 1.
DR   Genevisible; P57791; MM.
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
//