ID DUS4_CHICK Reviewed; 375 AA.
AC Q9PW71;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 133.
DE RecName: Full=Dual specificity protein phosphatase 4;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q13115};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q13115};
DE AltName: Full=Mitogen-activated protein kinase phosphatase 2;
DE Short=MAP kinase phosphatase 2;
DE Short=MKP-2;
GN Name=DUSP4; Synonyms=MKP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=10918612; DOI=10.1038/sj.onc.1203691;
RA Fu S.-L., Waha A., Vogt P.K.;
RT "Identification and characterization of genes upregulated in cells
RT transformed by v-Jun.";
RL Oncogene 19:3537-3545(2000).
CC -!- FUNCTION: Regulates mitogenic signal transduction by dephosphorylating
CC both Thr and Tyr residues on MAP kinases ERK1 and ERK2.
CC {ECO:0000250|UniProtKB:Q13115}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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:0000250|UniProtKB:Q13115};
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:0000250|UniProtKB:Q13115};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13115}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AF167296; AAD46656.1; -; mRNA.
DR RefSeq; NP_990169.1; NM_204838.1.
DR AlphaFoldDB; Q9PW71; -.
DR SMR; Q9PW71; -.
DR STRING; 9031.ENSGALP00000037153; -.
DR PaxDb; 9031-ENSGALP00000037153; -.
DR GeneID; 395642; -.
DR KEGG; gga:395642; -.
DR CTD; 1846; -.
DR VEuPathDB; HostDB:geneid_395642; -.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q9PW71; -.
DR PhylomeDB; Q9PW71; -.
DR Reactome; R-GGA-437980; Activated TAK1 mediates p38 MAP kinase phosphorylation.
DR Reactome; R-GGA-437986; Activated TAK1 mediates Jun kinases (JNK) phosphorylation and activation.
DR PRO; PR:Q9PW71; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990439; F:MAP kinase serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd14640; DSP_DUSP4; 1.
DR CDD; cd01446; DSP_MapKP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF111; DUAL SPECIFICITY PROTEIN PHOSPHATASE 4; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..375
FT /note="Dual specificity protein phosphatase 4"
FT /id="PRO_0000094801"
FT DOMAIN 25..143
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 176..317
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 261
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 375 AA; 41052 MW; 179290D0C2BEEEF1 CRC64;
MVAPEGLREM EGSALRRLVG REEASGGRCL LLDCRPFLAH SAGHIRGALN VRCNTIVRRR
AKGAVSLEQI LPAEGEVRAR LRAGLYTAVV LYDERSPRAE ALRDDSTVAL VLRALRRDMA
RADIRLLAGG YERFASEYPE FCAKTKTLSS ISPPSSAESL DLGFSSCGTP LHDQGGPVEI
LPFLYLGSAY HAARRDMLDA LGITALLNVS SDCPNHFEGH YQYKCIPVED NHKADISSWF
MEAIEYIDSV KECCGRVLVH CQAGISRSAT ICLAYLMMKK RVKLEKAFEF VKQRRSIISP
NFSFMGQLLQ FESQVLATSC AVEAASPSGT LRERGKATST PTSQFVFSFP VSVGVHATPS
SLPYLHSPIT TSPSC
//
