ID   FACE2_RAT               Reviewed;         308 AA.
AC   B0BMW8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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}.
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   -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR   EMBL; BC158593; AAI58594.1; -; mRNA.
DR   RefSeq; NP_001094055.1; NM_001100585.1.
DR   RefSeq; XP_006230852.1; XM_006230790.3.
DR   AlphaFoldDB; B0BMW8; -.
DR   STRING; 10116.ENSRNOP00000026454; -.
DR   MEROPS; G05.002; -.
DR   GeneID; 309153; -.
DR   KEGG; rno:309153; -.
DR   UCSC; RGD:1309261; rat.
DR   CTD; 9986; -.
DR   RGD; 1309261; Rce1.
DR   VEuPathDB; HostDB:ENSRNOG00000019468; -.
DR   eggNOG; KOG4130; Eukaryota.
DR   InParanoid; B0BMW8; -.
DR   OrthoDB; 1607650at2759; -.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   Reactome; R-RNO-9648002; RAS processing.
DR   PRO; PR:B0BMW8; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019468; Expressed in pancreas and 20 other tissues.
DR   ExpressionAtlas; B0BMW8; baseline and differential.
DR   Genevisible; B0BMW8; RN.
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:RGD.
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:RGD.
DR   InterPro; IPR039731; Rce1.
DR   InterPro; IPR003675; Rce1-like.
DR   PANTHER; PTHR13046; PTHR13046; 2.
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..308
FT                   /note="CAAX prenyl protease 2"
FT                   /id="PRO_0000356244"
FT   TRANSMEM        25..45
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        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
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            240
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   SITE            244
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"
SQ   SEQUENCE   308 AA;  33646 MW;  681F6CDAFB143A5B CRC64;
     MAALGGDGLR LLSVSRPERQ PESAALSSPG PGLCCWVSVF SCFSLACSYV GSLYVWKSEL
     PRDHPAVIKR RFTSVLVVSS LSPLCVLLWR ELTGIQPGTS LLTLMGFRLE GIFPAALLPL
     LLTMILFLGP LMQLCMDCPC DLTDGLKVVL APRSWARRLT DMRWLRNQVI APLTEELVFR
     ACMLPMLAPC TGLGPAVFTC PLFFGVAHFH HIIEQLRFRQ SSVGSIFLSA GHLIGPVLCH
     SFCNYMGFPA VCAALEHPQK WPLLAGYALG VGLFLLLLQP LTDPKLYGSL PLCMLLERTG
     ASETLLCS