ID   STE24_SCHPO             Reviewed;         474 AA.
AC   Q10071;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Probable CAAX prenyl protease 1;
DE            EC=3.4.24.84;
DE   AltName: Full=Prenyl protein-specific endoprotease 1;
DE            Short=PPSEP 1;
GN   ORFNames=SPAC3H1.05;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: The peptide bond hydrolyzed can be designated
CC       -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is
CC       usually aliphatic and X is the C-terminal residue of the substrate
CC       protein, and may be any of several amino acids.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M48A family.
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DR   EMBL; CU329670; CAA92258.1; -; Genomic_DNA.
DR   PIR; T38737; T38737.
DR   RefSeq; NP_593547.1; -.
DR   MEROPS; M48.001; -.
DR   GeneID; 2543456; -.
DR   KEGG; spo:SPAC3H1.05; -.
DR   NMPDR; fig|4896.1.peg.3517; -.
DR   GeneDB_Spombe; SPAC3H1.05; -.
DR   OMA; Q10071; KAADYTI.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-001224-MON; -.
DR   BRENDA; 3.4.24.84; 653.
DR   ArrayExpress; Q10071; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Transmembrane; Zinc.
FT   CHAIN         1    474       Probable CAAX prenyl protease 1.
FT                                /FTId=PRO_0000138847.
FT   TRANSMEM    103    123       Potential.
FT   TRANSMEM    196    216       Potential.
FT   TRANSMEM    230    250       Potential.
FT   TRANSMEM    344    364       Potential.
FT   TRANSMEM    381    401       Potential.
FT   ACT_SITE    333    333       By similarity.
FT   ACT_SITE    415    415       Proton donor (By similarity).
FT   METAL       332    332       Zinc; catalytic (By similarity).
FT   METAL       336    336       Zinc; catalytic (By similarity).
FT   METAL       411    411       Zinc; catalytic (By similarity).
SQ   SEQUENCE   474 AA;  54001 MW;  50AC2F96E25C76C5 CRC64;
     MSPGLCFLKE ISVIQATPKP TTRSFANCCK MGILQHLMHI LDIPGFPWKI VIAGFSIGKY
     AWDLYLRRRQ VPYLLREKPP AILAEHVDEK KYQKALSYAR DKSWFSTIVS TFTLAVDLLI
     IKYDGLSYLW NITKFPWMDK LAASSSRFSL STSITHSCVF MFGLTLFSRL IQIPFNLYST
     FVIEEKYGFN KSTLKIFVID LLKELSLGGL LMSVVVGVFV KILTKFGDNF IMYAWGAYIV
     FGLILQTIAP SLIMPLFYKF TPLENGSLRT QIEELAASIN FPLKKLYVID ASRRSTHSNA
     FFYGLPWNKG IVLFDTLVKN HTEPELIAIL GHELGHWYMS HNLINTIIDY GMSLFHLFLF
     AAFIRNNSLY TSFNFITEKP VIVGLLLFSD ALGPLSSILT FASNKVSRLC EYQADAFAKQ
     LGYAKDLGDG LIRIHDDNLS PLEFDSLYTS YYHSHPILVD RLNAIDYTTL KKNN
//