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 01-FEB-1996 (Rel. 33, Last annotation update) DE M-PHASE INDUCER PHOSPHATASE (EC 3.1.3.48) (MITOSIS INITIATION PROTEIN) DE (P80). GN CDC25 OR SPAC24H6.05. OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Archiascomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 86161690. 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; RA BARRELL B.G., RAJANDREAM M.A., WALSH S.V.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. 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 = CC PROTEIN TYROSINE + ORTHOPHOSPHATE. CC -!- SIMILARITY: STRONG, TO OTHER SPECIES M-PHASE INDUCER PHOSPHATASE CC AND IN GENERAL TO PROTEIN-TYROSINE PHOSPHATASES. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN FROM POSITION 571 CC ONWARD AND IS SHORTER (580 AA) DUE TO A FRAMESHIFT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; A25301; A25301. DR HSSP; P30304; 1C25. DR PFAM; PF00581; Rhodanese; 1. KW Cell division; Mitosis; Hydrolase. FT ACT_SITE 480 480 BY SIMILARITY. FT CONFLICT 571 596 GQSVLASPDVNDSPTAMHSLSTLRRF -> WPKCVSFPRR FT (IN REF. 1). SQ SEQUENCE 596 AA; 66565 MW; 5FCDB90D CRC32; 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 //