ID   FACE2_CAEEL             Reviewed;         266 AA.
AC   G5EEP3;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=CAAX prenyl protease 2 homolog {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000269|PubMed:12487630};
DE   AltName: Full=Farnesylated proteins-converting enzyme 2 {ECO:0000303|PubMed:12487630};
DE            Short=FACE-2 {ECO:0000303|PubMed:12487630};
GN   Name=fce-2 {ECO:0000312|WormBase:F48F5.5};
GN   ORFNames=F48F5.5 {ECO:0000312|WormBase:F48F5.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:CAD31791.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=12487630; DOI=10.1042/bj20021514;
RA   Cadinanos J., Schmidt W.K., Fueyo A., Varela I., Lopez-Otin C.,
RA   Freije J.M.P.;
RT   "Identification, functional expression and enzymic analysis of two distinct
RT   CaaX proteases from Caenorhabditis elegans.";
RL   Biochem. J. 370:1047-1054(2003).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC       farnesylated and geranylated proteins. {ECO:0000269|PubMed:12487630}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein
CC       {ECO:0000255}. Membrane {ECO:0000269|PubMed:12487630}.
CC   -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR   EMBL; AJ487543; CAD31791.1; -; mRNA.
DR   EMBL; Z81541; CAD91634.1; -; Genomic_DNA.
DR   RefSeq; NP_001023947.1; NM_001028776.2.
DR   AlphaFoldDB; G5EEP3; -.
DR   STRING; 6239.F48F5.5; -.
DR   MEROPS; G05.003; -.
DR   PaxDb; G5EEP3; -.
DR   EnsemblMetazoa; F48F5.5.1; F48F5.5.1; WBGene00001406.
DR   GeneID; 3565253; -.
DR   KEGG; cel:CELE_F48F5.5; -.
DR   CTD; 3565253; -.
DR   WormBase; F48F5.5; CE34031; WBGene00001406; fce-2.
DR   eggNOG; KOG4130; Eukaryota.
DR   GeneTree; ENSGT00390000004124; -.
DR   HOGENOM; CLU_049909_3_0_1; -.
DR   InParanoid; G5EEP3; -.
DR   OMA; ASHFHHI; -.
DR   OrthoDB; 1607650at2759; -.
DR   PhylomeDB; G5EEP3; -.
DR   Reactome; R-CEL-9648002; RAS processing.
DR   PRO; PR:G5EEP3; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00001406; Expressed in embryo and 3 other tissues.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:WormBase.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:WormBase.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0071586; P:CAAX-box protein processing; IDA:WormBase.
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   Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..266
FT                   /note="CAAX prenyl protease 2 homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000431786"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        131
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   ACT_SITE        164
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   SITE            216
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   SITE            220
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
SQ   SEQUENCE   266 AA;  30917 MW;  974FCBBBE6A7043B CRC64;
     MGAGLVSACL PISYVLLVHL FDRNGTDRND PESVKRRFKG ALLSNFVSIV VTAFYLRDYT
     DSPMLEMGVR WDNIGQSITY PFILMNAFYL GQFVMMQIDR TLWHYFDWYE WKLCFNSWVW
     RRDIIVGPIT EEIVFRACSS TLMAHVYGPT MTILLNPIPF AASHFHHIWD DQRRGYSLAH
     SILQRGFQFC YTYLFGAFAT WLQLTTRHAI VPIIAHAFCN AQGLPLWLEI PNYPKRRDRL
     TLYAAYSVGF AAFVHLLYTR NGMPTP