ID A0A2Y9F2A1_PHYMC Unreviewed; 418 AA.
AC A0A2Y9F2A1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
GN Name=CDC25C {ECO:0000313|RefSeq:XP_007113039.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007113039.1};
RN [1] {ECO:0000313|RefSeq:XP_007113039.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007113039.1};
RG RefSeq;
RL Submitted (NOV-2023) 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}.
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DR RefSeq; XP_007113039.1; XM_007112977.3.
DR AlphaFoldDB; A0A2Y9F2A1; -.
DR GeneID; 102978115; -.
DR CTD; 995; -.
DR OrthoDB; 12481at2759; -.
DR Proteomes; UP000248484; Chromosome 8.
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; Rhodanese-like domain; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR10828:SF64; M-PHASE INDUCER PHOSPHATASE 3; 1.
DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT DOMAIN 266..373
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 47805 MW; DF396C86CC87DF77 CRC64;
MSAAQFTTSS DLDETGHLDS TGPEEIQLAG MNYHQHLVKC SPAQLLCSTP NALDHGHRKK
DAICSSSANK ENENSTSKPL EWWVPRNLRS PLFLLDNGNL VESEMKHLGS PITTVSKLDK
NPELGENQTE EISDELMEFS LEDQDEAKAP VNRSCLYRSS SLPDSLNSPR LKQMVKFKDN
TIPDKVKKKY CSSHKELRKG LGIKKMVSLC DINMTQMLEE ESNQGPLIGD FSKVCALPTV
SGRHQDLKYV NPETVAALLL GKFQGLIEKF YIIDCRYPYE YLGGHIQGAL NLYGQEELYN
FFLKKPIVPL DTQKRIIIVF HCEFSSERGP RMYRSLRQED RAVNQYPALY YPELYILKGG
YRDFFPEYME LCEPQSYCPM HHQDHKAELL RCRNQSKAWE GERQLQEQIA LLVKDVSP
//
