ID MPIP_SCHPO STANDARD; PRT; 596 AA. AC P06652; DT 01-JAN-1988 (Rel. 06, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE M-phase inducer phosphatase (EC 3.1.3.48) (Mitosis initiation protein) DE (P80). GN Name=cdc25; ORFNames=SPAC24H6.05; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86161690; PubMed=3955656; DOI=10.1016/0092-8674(86)90546-5; RA Russell P., Nurse P.; RT "cdc25+ functions as an inducer in the mitotic control of fission RT yeast."; RL Cell 45:145-153(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M., Lyne R., Stewart A., RA Sgouros J., Peat N., Hayles J., Baker S., 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., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K., Murphy L., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J., 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., Fritzc C., Holzer E., Moestl D., Hilbert H., RA Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., RA 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). CC -!- FUNCTION: This protein functions as a dosage-dependent inducer in CC mitotic control. It is a tyrosine protein phosphatase required for CC progression of the cell cycle. It may directly dephosphorylate CC p34(cdc2) and activate the p34(cdc2) kinase activity. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- SIMILARITY: Belongs to the MPI phosphatase family. CC -!- SIMILARITY: Contains 1 rhodanese domain. CC -!- CAUTION: Ref.2 sequence differs from that shown due to a CC frameshift in position 571. 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; M13158; AAA35294.1; -. DR EMBL; Z54142; CAA90849.1; -. DR PIR; S62407; S62407. DR HSSP; P30305; 1QB0. DR GeneDB_SPombe; SPAC24H6.05; -. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR PROSITE; PS50206; RHODANESE_3; 1. KW Cell division; Hydrolase; Mitosis; Protein phosphatase. FT DOMAIN 429 533 Rhodanese. FT ACT_SITE 480 480 By similarity. FT CONFLICT 571 596 GQSVLASPDVNDSPTAMHSLSTLRRF -> WPKCVSFPRR FT (in Ref. 1). SQ SEQUENCE 596 AA; 66565 MW; CF8D430FC7BD38C1 CRC64; MDSPLSSLSF TNTLSGKRNV LRPAARELKL MSDRNANQEL DFFFPKSKHI ASTLVDPFGK TCSTASPASS LAADMSMNMH IDESPALPTP RRTLFRSLSC TVETPLANKT IVSPLPESPS NDALTESYFF RQPASKYSIT QDSPRVSSTI AYSFKPKASI ALNTTKSEAT RSSLSSSSFD SYLRPNVSRS RSSGNAPPFL RSRSSSSYSI NKKKGTSGGQ ATRHLTYALS RTCSQSSNTT SLLESCLTDD TDDFELMSDH EDTFTMGKVA DLPESSVELV EDAASIQRPN SDFGACNDNS LDDLFQASPI KPIDMLPKIN KDIAFPSLKV RSPSPMAFAM QEDAEYDEQD TPVLRRTQSM FLNSTRLGLF KSQDLVCVTP KQSTKESERF ISSHVEDLSL PCFAVKEDSL KRITQETLLG LLDGKFKDIF DKCIIIDCRF EYEYLGGHIS TAVNLNTKQA IVDAFLSKPL THRVALVFHC EHSAHRAPHL ALHFRNTDRR MNSHRYPFLY YPEVYILHGG YKSFYENHKN RCDPINYVPM NDASHVMTCT KAMNNFKRNA TFMRTKSYTF GQSVLASPDV NDSPTAMHSL STLRRF //