ID G1PFU4_MYOLU Unreviewed; 493 AA.
AC G1PFU4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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|Ensembl:ENSMLUP00000009472.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009472.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009472.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000009472.2}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AAPE02012944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PFU4; -.
DR STRING; 59463.ENSMLUP00000009472; -.
DR Ensembl; ENSMLUT00000010393.2; ENSMLUP00000009472.2; ENSMLUG00000010385.2.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000161460; -.
DR HOGENOM; CLU_014464_4_0_1; -.
DR InParanoid; G1PFU4; -.
DR OMA; CEPRSYC; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
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:UP000001074}.
FT DOMAIN 341..448
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55599 MW; 7481CFA0973C3DB2 CRC64;
KSGDRRYRRE LGESSETMSA ELTSCTREEG SPGTGPSFRS HQRKILNLLL ERDASFTICR
DLPGTPVDKL FGDSANQSSL SGGTPNRCLD LSNLSSGEMS ATQLTAPGDL DGTGRGPLDS
SGPQEIQLAW RNQHKHLIKC SPGRPLCSTP KALDHGNKKK DTICSSSTNK ENDNGNLVES
EMKYLGSPIT VVPKLGKNLK LGKDQAEEIS DELMEFSLED QEEAKSSVSD NGNGWNIPIN
SWREREKEKH RFVVPLMPDQ LRFYYYSWPS KIVKGLGLKK TVSLCDINAT QMLEEASNQG
YLTGDFSKVC ALPTVSGRHQ DLKYISPETV AALLLGKFQG LIEKFYIIDC RYPYEYLGGH
IQGALNLFSQ EELCNFFLKM PIVPLDTQKR IIIVFHCEFS SERGPRMCRS LREEDRALNQ
YPALYYPELY ILKGGYRDFF PDYTVLCEPQ SYCPMHHQDH KAELLRCRSQ SKAWEGKRQL
QEQIALLVKD VNL
//
