ID   MPIP1_BOVIN             Reviewed;         525 AA.
AC   A7MBD1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=M-phase inducer phosphatase 1;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P30304};
DE   AltName: Full=Dual specificity phosphatase Cdc25A;
GN   Name=CDC25A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tyrosine protein phosphatase which functions as a dosage-
CC       dependent inducer of mitotic progression. Directly dephosphorylates
CC       CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in
CC       complex with cyclin-E, in vitro. {ECO:0000250|UniProtKB:P30304}.
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:0000250|UniProtKB:P30304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P30304};
CC   -!- ACTIVITY REGULATION: Stimulated by B-type cyclins. Stimulated by PIM1-
CC       mediated phosphorylation. {ECO:0000250|UniProtKB:P30304}.
CC   -!- SUBUNIT: Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3
CC       epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1
CC       is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2.
CC       Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage
CC       (By similarity). Interacts with HSP90AB1; prevents heat shock-mediated
CC       CDC25A degradation and contributes to cell cycle progression (By
CC       similarity). {ECO:0000250|UniProtKB:P30304}.
CC   -!- DOMAIN: The phosphodegron motif mediates interaction with specific F-
CC       box proteins when phosphorylated. Putative phosphorylation sites at
CC       Ser-78 and Ser-81 appear to be essential for this interaction (By
CC       similarity). {ECO:0000250|UniProtKB:P30304}.
CC   -!- PTM: Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-177, Ser-279, Ser-
CC       293 and Thr-508 during checkpoint mediated cell cycle arrest. Also
CC       phosphorylated by CHEK2 on Ser-123, Ser-279, and Ser-293 during
CC       checkpoint mediated cell cycle arrest. Phosphorylation on Ser-177 and
CC       Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits
CC       CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-177, Ser-279 and Ser-
CC       293 may also promote ubiquitin-dependent proteolysis of CDC25A by the
CC       SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for
CC       subsequent phosphorylation at Ser-78, Ser-81 and Ser-87 by NEK11.
CC       Phosphorylation by NEK11 is required for BTRC-mediated
CC       polyubiquitination and degradation. Phosphorylation by PIM1 leads to an
CC       increase in phosphatase activity. Phosphorylated by PLK3 following DNA
CC       damage, leading to promote its ubiquitination and degradation (By
CC       similarity). {ECO:0000250|UniProtKB:P30304}.
CC   -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C)
CC       ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase
CC       leading to its degradation by the proteasome. Ubiquitinated by a SCF
CC       complex containing BTRC and FBXW11 during S phase leading to its
CC       degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads
CC       to its stabilization (By similarity). {ECO:0000250|UniProtKB:P30304}.
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; BC151493; AAI51494.1; -; mRNA.
DR   RefSeq; NP_001094570.1; NM_001101100.2.
DR   AlphaFoldDB; A7MBD1; -.
DR   SMR; A7MBD1; -.
DR   STRING; 9913.ENSBTAP00000074123; -.
DR   PaxDb; 9913-ENSBTAP00000012611; -.
DR   Ensembl; ENSBTAT00000086301.1; ENSBTAP00000074123.1; ENSBTAG00000009586.6.
DR   GeneID; 520188; -.
DR   KEGG; bta:520188; -.
DR   CTD; 993; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009586; -.
DR   VGNC; VGNC:27062; CDC25A.
DR   eggNOG; KOG3772; Eukaryota.
DR   GeneTree; ENSGT00940000160737; -.
DR   HOGENOM; CLU_014464_0_1_1; -.
DR   InParanoid; A7MBD1; -.
DR   OMA; NSAPAQM; -.
DR   OrthoDB; 12481at2759; -.
DR   TreeFam; TF101056; -.
DR   Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR   Reactome; R-BTA-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-BTA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-BTA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-BTA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000009586; Expressed in conceptus and 102 other cell types or tissues.
DR   ExpressionAtlas; A7MBD1; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Hydrolase; Mitosis; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Ubl conjugation.
FT   CHAIN           1..525
FT                   /note="M-phase inducer phosphatase 1"
FT                   /id="PRO_0000365161"
FT   DOMAIN          377..483
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          179..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           73..83
FT                   /note="Phosphodegron"
FT   MOTIF           140..142
FT                   /note="KEN box"
FT   COMPBIAS        274..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         75
FT                   /note="Phosphoserine; by CHEK1"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         78
FT                   /note="Phosphoserine; by NEK11"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         81
FT                   /note="Phosphoserine; by NEK11"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         87
FT                   /note="Phosphoserine; by NEK11"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         123
FT                   /note="Phosphoserine; by CHEK1 and CHEK2"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         177
FT                   /note="Phosphoserine; by CHEK1"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         279
FT                   /note="Phosphoserine; by CHEK1 and CHEK2"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         293
FT                   /note="Phosphoserine; by CHEK1 and CHEK2"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         508
FT                   /note="Phosphothreonine; by CHEK1"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         514
FT                   /note="Phosphoserine; by PLK3"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
FT   MOD_RES         520
FT                   /note="Phosphoserine; by PLK3"
FT                   /evidence="ECO:0000250|UniProtKB:P30304"
SQ   SEQUENCE   525 AA;  59142 MW;  3608ED70EE8293BB CRC64;
     MELGPEPPHR RRLLFACSPP PAPQPVVKAL FGTPAAGGLS PVTNLTVTMD QLQGLGSEYE
     QPIEVKNSSL QRMGSSESTD SGFCLDSPGP LDSKENLENP MRRINSLPQK LLGCSPALKR
     SHSDSLDHDV FQLIDQDENK ENQVFEFKKP IRPASRGCLH VHGLEEGKDV FTQRQNSAPA
     RMLSSNERDG NEPGNSIPFM PQSPVTPTLS DEDDGFMDLL DGENLKNDEE TPSCMASLWT
     APLVMRRTNN LGNRCKLFDS PSASCSSTIR SMLKRPDRSL EESPGGSRKR RKSVAGASPE
     EAASPEKPQE ILHHQSLSLA SSPKGTIENI LDNDPRDLIG DFSKGYLFHT VAGKHQDLKY
     ISPEIITSVL NGKFANLIKE FVIIDCRYPY EYEGGHIKGA VNLHMEEEVE EFLLKKPIVP
     TDGKRVIVVF HCEFSSERGP RMCRYVRERD RLGNEYPKLH YPELYVLKGG YKEFFLKCQS
     HCEPPSYRPM HHEDFKEDLK KFRTKSRTWA GEKSKREMYS RLKKL
//