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MDE10_SCHPO
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   03-AUG-2022, entry version 150.
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; 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   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 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 envelopes
RT   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., 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   [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 fission
RT   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 rim at
CC       the end of meiosis.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:14871934}.
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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   AlphaFoldDB; O13766; -.
DR   SMR; O13766; -.
DR   BioGRID; 278653; 1.
DR   STRING; 4896.SPAC17A5.04c.1; -.
DR   MEROPS; M12.180; -.
DR   PaxDb; O13766; -.
DR   EnsemblFungi; SPAC17A5.04c.1; SPAC17A5.04c.1:pep; SPAC17A5.04c.
DR   GeneID; 2542178; -.
DR   KEGG; spo:SPAC17A5.04c; -.
DR   PomBase; SPAC17A5.04c; mde10.
DR   VEuPathDB; FungiDB:SPAC17A5.04c; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   HOGENOM; CLU_522915_0_0_1; -.
DR   InParanoid; O13766; -.
DR   OMA; CDIEEYC; -.
DR   PhylomeDB; O13766; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-8941237; Invadopodia formation.
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; HDA: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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
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   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Meiosis;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW   Sporulation; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..512
FT                   /note="Zinc metalloprotease mde10"
FT                   /id="PRO_0000029210"
FT   DOMAIN          65..306
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          315..402
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        246..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..394
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         230
FT                   /note="E->A: No effect on sporulation."
FT                   /evidence="ECO:0000269|PubMed:14871934"
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
 
 
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