MPIP1_BOVIN
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 03-AUG-2022, entry version 95.
DE RecName: Full=M-phase inducer phosphatase 1;
DE EC=3.1.3.48;
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 (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Stimulated by B-type cyclins. Stimulated by PIM1-
CC mediated phosphorylation. {ECO:0000250}.
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 PIM1 (By similarity). Interacts with
CC HSP90AB1; prevents heat shock-mediated CDC25A degradation and
CC contributes to cell cycle progression (By similarity). {ECO:0000250,
CC 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}.
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}.
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}.
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.ENSBTAP00000012611; -.
DR PaxDb; A7MBD1; -.
DR PRIDE; A7MBD1; -.
DR Ensembl; ENSBTAT00000086301; ENSBTAP00000074123; ENSBTAG00000009586.
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; ECEQPLE; -.
DR OrthoDB; 1423329at2759; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000009586; Expressed in conceptus and 102 other tissues.
DR ExpressionAtlas; A7MBD1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
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:0034644; P:cellular response to UV; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF06617; M-inducer_phosp; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 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"
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
