ID G1PHU0_MYOLU Unreviewed; 460 AA.
AC G1PHU0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 53.
DE RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
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:ENSMLUP00000010249.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000010249.2, 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:ENSMLUP00000010249.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; AAPE02049100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PHU0; -.
DR STRING; 59463.ENSMLUP00000010249; -.
DR Ensembl; ENSMLUT00000011248.2; ENSMLUP00000010249.2; ENSMLUG00000011239.2.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000160737; -.
DR HOGENOM; CLU_014464_0_1_1; -.
DR InParanoid; G1PHU0; -.
DR OMA; NSAPAQM; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000001074; 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:SF46; M-PHASE INDUCER PHOSPHATASE 1; 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:UP000001074}.
FT DOMAIN 312..418
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52172 MW; 1705E7329E9E98A7 CRC64;
EQPPEAKNSL QRMGSSESTD SGFCLDSPGP LDSKENRENP MRRINSLPLK LLGCSPALKR
SHSDSMDRDA FQLMDQEENK ENEAFEFKKP IRPASRGCLR RAEGGDLTQR QSSAPARMLS
SNERDSSDPG NLIPLFMPQS PVAATLSDED DGFMDLLDGE NLKNDEETSS CMASLWTAPL
VMRRTANVGN RCQLFDSTPT GSPALRSVLK RPDRSRELSP PGNPKRRKSA LRASPGAAAR
PEEPREILYP SPALVSPPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI
MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EDEVEDFLLK KPISPADGKR
VIVVFHCEFS SERGPRMCRY VRERDRLSNE YPRLHYPELY ILKGGYKEFF LKCQSHCEPP
SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL
//