ID F7B6Y3_XENTR Unreviewed; 562 AA.
AC F7B6Y3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 63.
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:ENSXETP00000014678,
GN ECO:0000313|RefSeq:XP_031753390.1,
GN ECO:0000313|Xenbase:XB-GENE-944821};
GN Synonyms=cdc25 {ECO:0000313|RefSeq:XP_031753390.1}, cdc25c-a
GN {ECO:0000313|RefSeq:XP_031753390.1}, cdc25c-b
GN {ECO:0000313|RefSeq:XP_031753390.1}, xcdc25c
GN {ECO:0000313|RefSeq:XP_031753390.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000014678};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000014678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000014678};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000014678}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_031753390.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031753390.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031753390.1};
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_031753390.1; XM_031897530.1.
DR Ensembl; ENSXETT00000014678; ENSXETP00000014678; ENSXETG00000006710.
DR AGR; Xenbase:XB-GENE-944821; -.
DR Xenbase; XB-GENE-944821; cdc25c.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_014464_4_0_1; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Bgee; ENSXETG00000006710; Expressed in egg cell and 12 other cell types or tissues.
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; 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:UP000008143}.
FT DOMAIN 413..520
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 63258 MW; A6B820E4CD6EACF3 CRC64;
MFQTSSGGSA EVMAENHIMS SEAPPKSNQG LHFRTNCRMI LNLLREKDSS VTFSPEQPLT
PVTDLAVGFS NLSTFTGETP KRCLDLSNLG DETGPLPTES PDRMSLGKVE SPKTQFVQFD
GLFTPDLGCK AKKCQRGNMN SVLPRLLCST PSFKKTSGGQ RSMSNKENES ELFKNPNCKP
VALVLPQEAV DSQFSPAPED KVDISLDEDC EMNILGSPIS AAAPCLEGPH DDIKMQNLDG
FADFFSVDEE EIENPSGAVG NLSSSMAILL SGPLLNQEVE VSNVNNISLN RSRLYRSPSM
PEKLDRPMLK RTVRPQDSET PVRIKRRRST SSPLQPEEEN CQPRRRGTSL KKTLSLCDVD
ISTVLDEDCG HRQLIGDFSK VYALPTVTGR HQDLRYITAE TLAALIHGDF SSLVENVFII
DCRYPYEYDG GHIKGALNLH RQEEVTDYFL KQPLAPSVAQ KRLIIVFHCE FSSERGPKMC
RFLREEDRAR NEYPGLYYPE LYLLKGGYKD FFPEYKELCE PQGYCPMHHQ DFREELLKFR
TKCKTSVGDR KRREQIARLM KL
//
