STE24_SCHPO
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 03-AUG-2022, entry version 144.
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 (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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X in
CC which C is an S-isoprenylated cysteine residue, A is usually
CC aliphatic and X is the C-terminal residue of the substrate protein,
CC and may be any of several amino acids.; EC=3.4.24.84;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; CU329670; CAA92258.1; -; Genomic_DNA.
DR PIR; T38737; T38737.
DR RefSeq; NP_593547.1; NM_001018980.2.
DR AlphaFoldDB; Q10071; -.
DR SMR; Q10071; -.
DR BioGRID; 279876; 7.
DR STRING; 4896.SPAC3H1.05.1; -.
DR MaxQB; Q10071; -.
DR PaxDb; Q10071; -.
DR EnsemblFungi; SPAC3H1.05.1; SPAC3H1.05.1:pep; SPAC3H1.05.
DR GeneID; 2543456; -.
DR KEGG; spo:SPAC3H1.05; -.
DR PomBase; SPAC3H1.05; -.
DR VEuPathDB; FungiDB:SPAC3H1.05; -.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; Q10071; -.
DR OMA; LPFKIYK; -.
DR PhylomeDB; Q10071; -.
DR PRO; PR:Q10071; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:PomBase.
DR GO; GO:0071586; P:CAAX-box protein processing; ISO:PomBase.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISO:PomBase.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..474
FT /note="Probable CAAX prenyl protease 1"
FT /id="PRO_0000138847"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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
