ID W5MAQ1_LEPOC Unreviewed; 195 AA.
AC W5MAQ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Dual specificity protein phosphatase {ECO:0000256|RuleBase:RU366038};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366038};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU366038};
GN Name=DUSP13 {ECO:0000313|Ensembl:ENSLOCP00000005460.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005460.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005460.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC phosphotyrosine, phosphoserine and phosphothreonine residues, with a
CC preference for phosphotyrosine as a substrate.
CC {ECO:0000256|RuleBase:RU366038}.
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:0000256|ARBA:ARBA00001512,
CC ECO:0000256|RuleBase:RU366038};
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:0000256|ARBA:ARBA00001482,
CC ECO:0000256|RuleBase:RU366038};
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:0000256|RuleBase:RU366038};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|RuleBase:RU366038}.
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DR EMBL; AHAT01025196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015201835.1; XM_015346349.1.
DR RefSeq; XP_015201836.1; XM_015346350.1.
DR AlphaFoldDB; W5MAQ1; -.
DR STRING; 7918.ENSLOCP00000005460; -.
DR Ensembl; ENSLOCT00000005468.1; ENSLOCP00000005460.1; ENSLOCG00000004561.1.
DR GeneID; 107077303; -.
DR KEGG; loc:107077303; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000154628; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; W5MAQ1; -.
DR OMA; CAYETPS; -.
DR OrthoDB; 1082488at2759; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000004561; Expressed in muscle tissue and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; AGAP008228-PA; 1.
DR PANTHER; PTHR45682:SF10; DUAL SPECIFICITY PROTEIN PHOSPHATASE 13 ISOFORM B; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366038};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU366038};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 37..184
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 106..163
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 129
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR620405-1"
SQ SEQUENCE 195 AA; 22109 MW; A8EFD089D5CA9A66 CRC64;
MALKKEKEVV ASKGEYEPPP LSELQNLLWM NRHSTGHVNE VWPNLYIGDS YTARDKGALF
NLGITHIVNA ADGRYHVNTG ARFYSDMPVL YYGVEADDHP EFDLSLFFYP TARFIRSALS
QKGRVFVHCA MGISRSAALV LAFLMICENL TLVDAIKTVR KHRDVCPNSG FLSQLRELDL
ALMLERKRKA ALYKL
//
