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Database: UniProt
Entry: G3H423_CRIGR
LinkDB: G3H423_CRIGR
Original site: G3H423_CRIGR 
ID   G3H423_CRIGR            Unreviewed;       480 AA.
AC   G3H423;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE            EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
GN   ORFNames=I79_005018 {ECO:0000313|EMBL:EGV92415.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV92415.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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   EMBL; JH000136; EGV92415.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3H423; -.
DR   STRING; 10029.G3H423; -.
DR   PaxDb; 10029-XP_007621845-1; -.
DR   eggNOG; KOG3772; Eukaryota.
DR   InParanoid; G3H423; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
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:SF48; M-PHASE INDUCER PHOSPHATASE 2; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   Pfam; PF06617; M-inducer_phosp; 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:UP000001075}.
FT   DOMAIN          331..438
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  55374 MW;  2938FD4C43CE9AF7 CRC64;
     MSSESSESSD AGLCMDSPSP MDPQKAEHSF EQAIQAASRV IQNEQFTIKR FRSLPVRLLD
     HSPVLQNITN SQALDSRKKH EAGYRAANSL GEDKENDGYV FKMPWESTRP NPAQALVEWA
     SRREAFAQRP SSAPDLMCLT PERKMEVEEL SPMAQSSSSL TPVERASEDD DGFVDILESD
     LKDDDVVPPG MENLFSAPLV KNLDKEESQD LIMFSKCQRL YRSPSMPCSV IRPILKRLER
     PQDKDTPVQS KRRKSVTPLE EQQPEEPKAR VFRSKSLCHE IESILDSDHR GLIGDYSKAF
     LLQTVDGKHQ DLKYISPETM VALLTGKFSN MVEKFVIVDC RYPYEYEGGH IKNAVNLPLE
     RDVETFLLQR PIKPCSLDKR IILIFHCEFS SERGPRMCRF VRERDRAAND YPSLYYPEMY
     ILKGGYKEFF PQHPNFCEPQ NYRPMNHKAF RDELRTFRLK TRSWAGERSR RELCSRLQDQ
//
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