ID A0A6P5QC81_MUSCR Unreviewed; 517 AA. AC A0A6P5QC81; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 19-JAN-2022, entry version 6. DE RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028}; DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028}; GN Name=Cdc25a {ECO:0000313|RefSeq:XP_021027721.2}; OS Mus caroli (Ryukyu mouse) (Ricefield mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10089 {ECO:0000313|Proteomes:UP000515126, ECO:0000313|RefSeq:XP_021027721.2}; RN [1] {ECO:0000313|RefSeq:XP_021027721.2} RP IDENTIFICATION. RG RefSeq; RL Submitted (FEB-2021) to UniProtKB. CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control. CC Tyrosine protein phosphatase required for progression of the cell CC cycle. {ECO:0000256|RuleBase:RU368028}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; CC Evidence={ECO:0000256|ARBA:ARBA00001490, CC ECO:0000256|RuleBase:RU368028}; CC -!- SIMILARITY: Belongs to the MPI phosphatase family. CC {ECO:0000256|ARBA:ARBA00011065, ECO:0000256|RuleBase:RU368028}. 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 RefSeq; XP_021027721.2; XM_021172062.2. DR Proteomes; UP000515126; Genome assembly. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule. DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro. DR CDD; cd01530; Cdc25; 1. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like_dom. DR InterPro; IPR036873; Rhodanese-like_dom_sf. DR Pfam; PF06617; M-inducer_phosp; 1. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU368028}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, KW ECO:0000256|RuleBase:RU368028}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368028}; KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|RuleBase:RU368028}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912, KW ECO:0000256|RuleBase:RU368028}. FT DOMAIN 369..475 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT REGION 178..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 253..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..269 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 270..293 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 517 AA; 58240 MW; CD35870B065B3C67 CRC64; MELGPEPPHR RRLFFTCSPT PAPQPTGNML FGASAAGGLS PVTNLTVTMD QLEGLGSDCE KRMEARNNSS LQRMGSSEST DSGFCLDSPG PLDSKENLEI SLMRINSLPK LLGCSPALKR SHSDSLDHDT FHLIDQDENK ENEAFEFKKP IRPASRHIHE EGKDPFTHRQ NSAPARMLSS NESESGNFSP LFTPQSPVKA TFSDEDDGFI DLLDGENMKN DEETPSCMAS LWTAPLVMRR PTNLADRCGL FDSPSPCCSS SSSSSTRAVL KRTDRSHEES PRGTKRRKSV PSPVKADVLE PSQLPSQSLS LMSSPKGTIE NILDSDPRDL IGDFSKGYLF NTVSGKHQDL KYISPEIMAS VLNGKFANLI KEFVIIDCRY PYEYEGGHIK GAVNLHMEEE VEDFLLKNPI VPTDGKRVIV VFHCEFSSER GPRMCRYVRE RDRLGNEYPK LHYPELYVLK GGYKEFFLKC QSHCEPPSYR PMHHEDFKED LKKFRTKSRT WAGEKSKREM YSRLKKL //