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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!
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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

DescriptionRecName: 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 synonymsMDE10_SCHPO , O13766 , Q9USG1 , 804BDA2333621DAB
match map segment
iprf:DISINTEGRIN_2 ipfam:Disintegrin iprf:ADAM_MEPRO ismart:DISIN  
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].
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
//