MPIP3_PIG
ID MPIP3_PIG Reviewed; 502 AA.
AC Q29029;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=M-phase inducer phosphatase 3;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25C;
GN Name=CDC25C;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=7601801; DOI=10.2527/1995.732630x;
RA Cui H., Xu W., Powell D., Newman B.J.;
RT "Cloning and sequencing of a pig cdc25 tyrosine phosphatase cDNA.";
RL J. Anim. Sci. 73:630-630(1995).
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. Directly dephosphorylates CDK1 and activates its kinase
CC activity. When phosphorylated, highly effective in activating G2 cells
CC into prophase (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 -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated
CC at Ser-122 and/or Thr-123, interacts with PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-245. This
CC phosphorylation creates a binding site for 14-3-3 protein and inhibits
CC the phosphatase (By similarity). Phosphorylated by PLK4. Phosphorylated
CC by PLK1, leading to activate the phosphatase activity. Phosphorylation
CC by PLK3 at Ser-217 promotes nuclear translocation. Ser-224 is a minor
CC phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at
CC G2 and G2-M transition and leads to increased activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; X78317; CAA55123.1; -; Genomic_DNA.
DR PIR; S43123; S43123.
DR RefSeq; NP_001116567.1; NM_001123095.1.
DR RefSeq; XP_005661723.1; XM_005661666.2.
DR RefSeq; XP_005661725.1; XM_005661668.2.
DR RefSeq; XP_013850591.1; XM_013995137.1.
DR RefSeq; XP_013850592.1; XM_013995138.1.
DR RefSeq; XP_013850593.1; XM_013995139.1.
DR RefSeq; XP_013850594.1; XM_013995140.1.
DR AlphaFoldDB; Q29029; -.
DR SMR; Q29029; -.
DR STRING; 9823.ENSSSCP00000015242; -.
DR PaxDb; Q29029; -.
DR PRIDE; Q29029; -.
DR Ensembl; ENSSSCT00005002944; ENSSSCP00005001686; ENSSSCG00005001613.
DR Ensembl; ENSSSCT00005002986; ENSSSCP00005001720; ENSSSCG00005001613.
DR Ensembl; ENSSSCT00015036066; ENSSSCP00015014350; ENSSSCG00015026640.
DR Ensembl; ENSSSCT00025071692; ENSSSCP00025031053; ENSSSCG00025052302.
DR Ensembl; ENSSSCT00030054043; ENSSSCP00030024676; ENSSSCG00030038696.
DR Ensembl; ENSSSCT00035058082; ENSSSCP00035023347; ENSSSCG00035043663.
DR Ensembl; ENSSSCT00040102444; ENSSSCP00040046278; ENSSSCG00040073965.
DR Ensembl; ENSSSCT00045059041; ENSSSCP00045041338; ENSSSCG00045033315.
DR Ensembl; ENSSSCT00045059238; ENSSSCP00045041505; ENSSSCG00045033315.
DR Ensembl; ENSSSCT00050049786; ENSSSCP00050020784; ENSSSCG00050036959.
DR Ensembl; ENSSSCT00055058218; ENSSSCP00055046573; ENSSSCG00055029147.
DR Ensembl; ENSSSCT00060025764; ENSSSCP00060010899; ENSSSCG00060019102.
DR Ensembl; ENSSSCT00065088478; ENSSSCP00065038687; ENSSSCG00065064427.
DR Ensembl; ENSSSCT00070044280; ENSSSCP00070037309; ENSSSCG00070022197.
DR Ensembl; ENSSSCT00070044285; ENSSSCP00070037314; ENSSSCG00070022197.
DR GeneID; 100144474; -.
DR KEGG; ssc:100144474; -.
DR CTD; 995; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_014464_4_0_1; -.
DR InParanoid; Q29029; -.
DR OrthoDB; 1423329at2759; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR Genevisible; Q29029; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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; 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 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; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Hydrolase; Mitosis; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..502
FT /note="M-phase inducer phosphatase 3"
FT /id="PRO_0000198650"
FT DOMAIN 350..457
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 126..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 40
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 60
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 115
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 194
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 217
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 224
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 243
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 245
FT /note="Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
SQ SEQUENCE 502 AA; 56639 MW; 02E28CE42C0EDA70 CRC64;
MAEGGRPGSG PSFRSNHRKI LNLLLERETS FSMSSDRPGT PLKKKLFGDS ANLSILSGGT
PKRCLDLSNL SSGEMSATQF TTSADLDETG HLDSTGSEEI QLAGMSYHQH LLKCSPAQLL
CSTPNALDHG RRKKDAICSS SENKENENNT SKPLEWWAHR NLLFQKRPGG PYMSPLSLLD
NGNLVEGEMK HLGSPITAVS KLDKNPERGE DQAEEISDEL MEFSLEDQEE AKVSLNTSCL
YRSFSLPDSL NSPGLKQVVK FKDHTLPDKV KKKYCSSHEE LRKGLGVKKM VSLCNINMIQ
MLEEDSNQGP LIGDFSKVCA LPTVSGRHQD LKYVNPETVA ALLSGKFQGL IEKFYIIDCR
YPYEYLGGHI QGALNLYSQE ELCNFFLKKP IIPLDTQKRI IVVFHCEFSS ERGPRMCRSL
REEDRALNQY PALYYPELYI LKGGYRDFFP EYMELCEPQS YCPMHHQDHK AELLRCRSQN
KAWEGERQLQ EQIALLVKDV SP
