MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=Zinc metalloprotease mde10; EC=3.4.24.-; AltName: Full=Meiotically up-regulated gene 139 protein; AltName: Full=Sporulation protein mde10; Flags: Precursor; |
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MyHits synonyms | MDE10_SCHPO , O13766 , Q9USG1 , 804BDA2333621DAB |
![]() Legends: 1, ACT_SITE {ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095}; 2, Zinc; catalytic. {ECO:0000250}; 3, Zinc; catalytic. {ECO:0000305}; 4, N-linked (GlcNAc...). {ECO:0000255}; 5, MUTAGEN E->A: No affect on sporulation. {ECO:0000269|PubMed:14871934}; 6, SIGNAL {ECO:0000255}; 7, Disintegrin. {ECO:0000255|PROSITE- ProRule:PRU00068}; 8, iprf:DISINTEGRIN_2 [T]; 9, ipfam:Disintegrin [T].
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ID MDE10_SCHPO Reviewed; 512 AA. AC O13766; Q9USG1; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 18-JAN-2017, entry version 124. DE RecName: Full=Zinc metalloprotease mde10; DE EC=3.4.24.-; DE AltName: Full=Meiotically up-regulated gene 139 protein; DE AltName: Full=Sporulation protein mde10; DE Flags: Precursor; GN Name=mde10; Synonyms=mug139; ORFNames=SPAC17A5.04c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; 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., 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-49, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 38364 / 968; RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x; RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., RA Hiraoka Y.; RT "Large-scale screening of intracellular protein localization in living RT fission yeast cells by the use of a GFP-fusion genomic DNA library."; RL Genes Cells 5:169-190(2000). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF RP GLU-230. RX PubMed=14871934; DOI=10.1128/EC.3.1.27-39.2004; RA Nakamura T., Abe H., Hirata A., Shimoda C.; RT "ADAM family protein Mde10 is essential for development of spore RT envelopes in the fission yeast Schizosaccharomyces pombe."; RL Eukaryot. Cell 3:27-39(2004). RN [4] 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., RA San-Segundo P., Smith G.R., Moreno S.; RT "A large-scale screen in S. pombe identifies seven novel genes RT required for critical meiotic events."; RL Curr. Biol. 15:2056-2062(2005). RN [5] 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 RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). CC -!- FUNCTION: Has a role in the development of the spore envelope. CC {ECO:0000269|PubMed:14871934, ECO:0000269|PubMed:16303567}. 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. Spore wall. CC Note=Endoplasmic reticulum during meiosis. Located at the spore CC rim at the end of meiosis. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:14871934}. CC -!- SIMILARITY: Contains 1 disintegrin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00068}. CC -!- SIMILARITY: Contains 1 peptidase M12B domain. CC {ECO:0000255|PROSITE-ProRule:PRU00276}. DR EMBL; CU329670; CAB11504.1; -; Genomic_DNA. DR EMBL; AB027771; BAA87075.1; -; Genomic_DNA. DR PIR; T37819; T37819. DR RefSeq; NP_593472.1; NM_001018905.2. DR ProteinModelPortal; O13766; -. DR BioGrid; 278653; 1. DR MINT; MINT-4667763; -. DR MEROPS; M12.180; -. DR PRIDE; O13766; -. DR EnsemblFungi; SPAC17A5.04c.1; SPAC17A5.04c.1:pep; SPAC17A5.04c. DR GeneID; 2542178; -. DR KEGG; spo:SPAC17A5.04c; -. DR EuPathDB; FungiDB:SPAC17A5.04c; -. DR PomBase; SPAC17A5.04c; mde10. DR InParanoid; O13766; -. DR OMA; TAGRVEW; -. DR OrthoDB; EOG092C21C3; -. DR PhylomeDB; O13766; -. DR Reactome; R-SPO-6798695; Neutrophil degranulation. DR PRO; PR:O13766; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005619; C:ascospore wall; IDA:PomBase. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase. DR GO; GO:0030476; P:ascospore wall assembly; IMP:PomBase. DR CDD; cd04271; ZnMc_ADAM_fungal; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR034028; ZnMc_ADAM_fungal. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Hydrolase; Meiosis; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Signal; Sporulation; Zinc. FT SIGNAL 1 15 {ECO:0000255}. FT CHAIN 16 512 Zinc metalloprotease mde10. FT /FTId=PRO_0000029210. FT DOMAIN 65 306 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 315 402 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT ACT_SITE 230 230 {ECO:0000255|PROSITE-ProRule:PRU00276, FT ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 229 229 Zinc; catalytic. {ECO:0000250}. FT METAL 233 233 Zinc; catalytic. {ECO:0000250}. FT METAL 239 239 Zinc; catalytic. {ECO:0000305}. FT CARBOHYD 35 35 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 432 432 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 246 254 {ECO:0000250}. FT DISULFID 374 394 {ECO:0000250}. FT MUTAGEN 230 230 E->A: No affect on sporulation. FT {ECO:0000269|PubMed:14871934}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 315 402 iprf:DISINTEGRIN_2 [T] FT MYHIT 324 397 ipfam:Disintegrin [T] FT MYHIT 65 296 iprf:ADAM_MEPRO [T] FT MYHIT 324 400 ismart:DISIN [T] SQ SEQUENCE 512 AA; 56440 MW; 804BDA2333621DAB CRC64; MRLVLLFSCV LAVSSYAEII LAHSDENLLS RTKNNLSKWN ENRLYDYGSK STMSLPVSSL FPALQTLWIG VVADCSYVTH FTSRMEAKKH IFQEFEGVST LYEDSFNINV QIHSLILPSA HDCSANVVDR PEISMSPRIS IEEKLEIFSK WKYESPGNNV FEAISPHERE SFPSEPQVSV LFTSSVKRSP HGVSWFATIC SETHIENEWH VGPLSVVSAY PNDRLVVAHE IGHILGLIHD CNKKSCGDHS EACCPLSSSL CDAQELYIMN PSNSYTYANL RFSDCSILQL HSLVEKKYVS LSCLSKPSEK SVLRLGTCGN GIVEDGEECD CGEDCENNPC CDGKTCKLTK GSLCDDQQDA CCYQCHFKNA GTLCRQSTNP CDKPEFCTGI SSKCPVDENW DDGRICQDSL GMGSCASGVC TSASRQCKKL TNFSSLSCHS DSCKVSCQNE DGTCFISAKD YIDGTRCRGG LCYNGVCVPI EGSSASWSKQ PSLFCASGTM LISLAVIAWF FW // |