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 27-MAR-2024, entry version 156.
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; 284812.O13766; -.
DR MEROPS; M12.180; -.
DR GlyCosmos; O13766; 2 sites, No reported glycans.
DR PaxDb; 4896-SPAC17A5-04c-1; -.
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; HERESFP; -.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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
//
