RCE1_SCHPO
ID RCE1_SCHPO Reviewed; 271 AA.
AC O94448;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Probable CAAX prenyl protease 2;
DE EC=3.4.-.-;
DE AltName: Full=Prenyl protein-specific endoprotease 2;
DE Short=PPSEP 2;
GN ORFNames=SPAC1687.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000250|UniProtKB:Q03530}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q03530}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22596.1; -; Genomic_DNA.
DR PIR; T37745; T37745.
DR RefSeq; NP_593120.1; NM_001018516.2.
DR AlphaFoldDB; O94448; -.
DR BioGRID; 279204; 3.
DR STRING; 4896.SPAC1687.02.1; -.
DR MEROPS; G05.002; -.
DR PaxDb; O94448; -.
DR EnsemblFungi; SPAC1687.02.1; SPAC1687.02.1:pep; SPAC1687.02.
DR GeneID; 2542754; -.
DR KEGG; spo:SPAC1687.02; -.
DR PomBase; SPAC1687.02; -.
DR VEuPathDB; FungiDB:SPAC1687.02; -.
DR eggNOG; KOG4130; Eukaryota.
DR HOGENOM; CLU_049909_1_0_1; -.
DR InParanoid; O94448; -.
DR OMA; HSFCNWC; -.
DR PhylomeDB; O94448; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-9648002; RAS processing.
DR PRO; PR:O94448; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:PomBase.
DR GO; GO:0071586; P:CAAX-box protein processing; ISO:PomBase.
DR GO; GO:0007323; P:peptide pheromone maturation; ISO:PomBase.
DR InterPro; IPR039731; Rce1.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR13046; PTHR13046; 1.
DR Pfam; PF02517; Rce1-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="Probable CAAX prenyl protease 2"
FT /id="PRO_0000194833"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT ACT_SITE 160
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 213
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 217
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
SQ SEQUENCE 271 AA; 31025 MW; 7274E9EE225348BB CRC64;
MRVYLISFFF TAIYVVSLYT FPVARPRPSL NRNDPKVITA RCISVLLASS VCCILTRLII
GPSLNVFTFP TDQVLKSLLH AATIFIGPLY EVWIVDKEYR LFFIHLKDCL SNAIAWRNII
IGPLSEELTF RCCIVPICEA AGWSRLKIIF VAPLLFGMAH IHHTYEFLLA YPNAYIAAAL
QTVVQFSYTT VFGWYTTHLF LSTHSLFPSF LVHAFCNSMG LPTLYGKIGN RNQTRIYYTL
LLLGVLIFYM TWGITDFNNH QDFEPRLVPL N
