MU138_SCHPO
ID MU138_SCHPO Reviewed; 969 AA.
AC O14077;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative zinc protease mug138;
DE EC=3.4.24.-;
DE AltName: Full=Meiotically up-regulated gene 138 protein;
GN Name=mug138; ORFNames=SPAC2E11.12c, SPACUNK4.12c;
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).
RN [2]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA20142.1; -; Genomic_DNA.
DR PIR; T41707; T41707.
DR RefSeq; NP_593966.1; NM_001019393.2.
DR AlphaFoldDB; O14077; -.
DR SMR; O14077; -.
DR BioGRID; 278898; 2.
DR STRING; 4896.SPACUNK4.12c.1; -.
DR MEROPS; M16.020; -.
DR MaxQB; O14077; -.
DR PaxDb; O14077; -.
DR EnsemblFungi; SPACUNK4.12c.1; SPACUNK4.12c.1:pep; SPACUNK4.12c.
DR GeneID; 2542436; -.
DR KEGG; spo:SPACUNK4.12c; -.
DR PomBase; SPACUNK4.12c; -.
DR VEuPathDB; FungiDB:SPACUNK4.12c; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_1_1; -.
DR InParanoid; O14077; -.
DR OMA; WIFDEMK; -.
DR PhylomeDB; O14077; -.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR PRO; PR:O14077; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Meiosis; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..969
FT /note="Putative zinc protease mug138"
FT /id="PRO_0000074429"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 969 AA; 112145 MW; 283A70BFBCFF3913 CRC64;
MDGKPQVEVI VNGQVVPNLD DREYRLIKLE NDLEVLLVRD PETDNASAAI DVHIGSQSNP
RELLGLAHFC EHLLFMGTKK YPDENEYRKY LESHNGISNA YTASNNTNYY FEVSHDALYG
ALDRFAQFFI DPLFLEECKD REIRAVDSEH CKNLQSDSWR FWRLYSVLSN PKSVFSKFNT
GNIETLGDVP KELGLDVRQE LLKFYDKYYS ANIMKLVIIG REPLDVLQDW AAELFSPIKN
KAVPIPKFPD PPYTDNEVRK ICYVKPVKNL RRLDIVFPIP GQYHKYKCRP AEYVCHLLGH
EGEGSYLAYL KSLGLATSLI AFNVSITEDA DIIVVSTFLT EEGLTDYQRV IKILFEYIRL
LDQTNAHKFL FEETRIMSEA QFKTRQKTPA YQYAHVVASK LQREYPRDKV LYYSSVLTEF
DPKGIQEVVE SLRPNNFFAI LAAHSIEKGL DNKEKFYGID YGLEDLDSQF IDSLLHIKTS
SELYLPLANE FIPWSLEVEK QPVTTKLKVP NLVRNDKFVR LWHKKDDTFW VPKANVFINF
ISPIARRSPK VSVSTTLYTR LIEDALGEYS YPASLAGLSF SLSPSTRGII LCISGFTDKL
HVLLEKVVAM MRDLKVHPQR FEILKNRLEQ ELKDYDALEA YHRSNHVLTW LSEPHSWSNA
ELREAIKDVQ VGDMSDFISD LLKQNFLESL VHGNYTEEDA KNLIESAQKL IDPKPVFASQ
LSRKRAIIVP EGGNYIYKTV VPNKEEKNSA IMYNLQISQL DDERSGALTR LARQIMKEPT
FSILRTKEQL GYIVFTLVRQ VTPFINLNIF VQSERSSTYL ESRIRALLDQ FKSEFLEMSD
EDFSKHKSSL INFMLEKHTN LKEESSMYWL RICDGFYDFT RLEKQAEIVS TITKDEFYSF
FINNIHYEGE NTKKISVHVV SQRCEDEVYE IPNVTIIENG NMFKESMTLS KAAFPLKPFD
EIDRSLLFN
