DUS12_RAT
ID DUS12_RAT Reviewed; 339 AA.
AC Q9JIM4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dual specificity protein phosphatase 12;
DE EC=3.1.3.16 {ECO:0000269|PubMed:10913113};
DE EC=3.1.3.48 {ECO:0000269|PubMed:10913113};
DE AltName: Full=Glucokinase-associated dual specificity phosphatase;
DE Short=GKAP;
GN Name=Dusp12; Synonyms=Gkap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10913113; DOI=10.1074/jbc.m000841200;
RA Munoz-Alonso M.J., Guillemain G., Kassis N., Girard J., Burnol A.-F.,
RA Leturque A.;
RT "A novel cytosolic dual specificity phosphatase, interacting with
RT glucokinase, increases glucose phosphorylation rate.";
RL J. Biol. Chem. 275:32406-32412(2000).
CC -!- FUNCTION: Dual specificity phosphatase; can dephosphorylate both
CC phosphotyrosine and phosphoserine or phosphothreonine residues. Can
CC dephosphorylate glucokinase (in vitro). Has phosphatase activity with
CC the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and
CC other in vitro substrates. {ECO:0000269|PubMed:10913113}.
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:0000269|PubMed:10913113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:10913113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:10913113};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9UNI6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNI6}. Cytoplasm
CC {ECO:0000269|PubMed:10913113}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9UNI6}. Note=Primarily nuclear. Detected in a
CC mesh-like pattern in the cytosol. {ECO:0000250|UniProtKB:Q9UNI6}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF217233; AAF87971.1; -; mRNA.
DR RefSeq; NP_071584.1; NM_022248.1.
DR AlphaFoldDB; Q9JIM4; -.
DR SMR; Q9JIM4; -.
DR STRING; 10116.ENSRNOP00000004179; -.
DR PaxDb; Q9JIM4; -.
DR Ensembl; ENSRNOT00000004179; ENSRNOP00000004179; ENSRNOG00000003100.
DR GeneID; 64014; -.
DR KEGG; rno:64014; -.
DR UCSC; RGD:68375; rat.
DR CTD; 11266; -.
DR RGD; 68375; Dusp12.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00930000151041; -.
DR HOGENOM; CLU_023312_1_0_1; -.
DR InParanoid; Q9JIM4; -.
DR OMA; RIMLNTQ; -.
DR OrthoDB; 1482182at2759; -.
DR PhylomeDB; Q9JIM4; -.
DR TreeFam; TF105123; -.
DR PRO; PR:Q9JIM4; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003100; Expressed in thymus and 19 other tissues.
DR Genevisible; Q9JIM4; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:RGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; IDA:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR016278; DUSP12.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000941; DUSP12; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1..339
FT /note="Dual specificity protein phosphatase 12"
FT /id="PRO_0000260313"
FT DOMAIN 26..170
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 115..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
SQ SEQUENCE 339 AA; 37196 MW; F2E41DE35F0E2C00 CRC64;
MLEVQSSNHG CERQAPTTSP ASSAGHAVEV RPGLYLGGAA AVAGPDYLRE AGITAVLTVD
SEPAFPAGAG FEGLQSLFVP ALDKPETDLL SHLDRCVAFI GQARSEGRAV LVHCHAGVSR
SVAVVTAFIM KTEQLTFEKA YENLQTIKPE AKMNEGFEWQ LKLYEAMGHE VHTSSAVYKQ
YRLQKVTEKY PELRNLPREL FAVDPTTVSQ GLKDDILYKC RKCRRSLFRR SSILDHSEGS
GPVAFAHKRT GLSSVLTTGN QAQCTSYFIE PVQWMESALL GVMDGQLLCP KCSAKLGSFN
WYGEQCSCGR WITPAFQIHK NRVDEVKTLP ALGSQTKKP
