ID   FACE2_BOVIN             Reviewed;         308 AA.
AC   A6H7A0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC146167; AAI46168.1; -; mRNA.
DR   RefSeq; NP_001092567.1; NM_001099097.1.
DR   AlphaFoldDB; A6H7A0; -.
DR   STRING; 9913.ENSBTAP00000042314; -.
DR   MEROPS; G05.002; -.
DR   PaxDb; A6H7A0; -.
DR   PRIDE; A6H7A0; -.
DR   Ensembl; ENSBTAT00000044861; ENSBTAP00000042314; ENSBTAG00000019696.
DR   GeneID; 539539; -.
DR   KEGG; bta:539539; -.
DR   CTD; 9986; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019696; -.
DR   VGNC; VGNC:33828; RCE1.
DR   eggNOG; KOG4130; Eukaryota.
DR   GeneTree; ENSGT00390000004124; -.
DR   HOGENOM; CLU_049909_3_0_1; -.
DR   InParanoid; A6H7A0; -.
DR   OMA; HSFCNWC; -.
DR   OrthoDB; 1458907at2759; -.
DR   TreeFam; TF313800; -.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000019696; Expressed in retina and 104 other tissues.
DR   ExpressionAtlas; A6H7A0; baseline and differential.
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; IEA:Ensembl.
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; IEA:Ensembl.
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_0000356243"
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;  33455 MW;  E6706AF89C342D93 CRC64;
     MAALGGDGFR LLSVSRPERQ PESAALGGPG PGLCCWVSVF SCLSLACSYV GSLYVWKSEL
     PRDHPAVIKR RFTSVLVVSS LSPLCVLLWR ELTGIQPGTS LLTLMGFRLE GIFPAALLPL
     LLTMILFLGP LMQLSMDCPC DLADGLKVVL APRSWARCLT DMRWLRNQVI APLTEELVFR
     ACMLPMLAPC TGLGPAVFTC PLFFGVAHFH HIFEQLRFRQ SSVGSIFLSA GHLIGPVLCH
     SFCNYMGFPA VCAALEHPQR RPLLAGYALG VGLFLLLLQP LTDPKLYGSL PLCVLLERAG
     DSEAPLCS