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Database: UniProt
Entry: A0A3Q3FMV0_9LABR
LinkDB: A0A3Q3FMV0_9LABR
Original site: A0A3Q3FMV0_9LABR 
ID   A0A3Q3FMV0_9LABR        Unreviewed;       383 AA.
AC   A0A3Q3FMV0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dual specificity protein phosphatase {ECO:0000256|PIRNR:PIRNR000939};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000939};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000939};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000021057.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000021057.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR000939};
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|PIRNR:PIRNR000939};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601, ECO:0000256|PIRNR:PIRNR000939}.
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DR   AlphaFoldDB; A0A3Q3FMV0; -.
DR   Ensembl; ENSLBET00000022186.1; ENSLBEP00000021057.1; ENSLBEG00000016186.1.
DR   GeneTree; ENSGT00940000157262; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14643; DSP_DUSP7; 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; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF305; DUAL SPECIFICITY PROTEIN PHOSPHATASE 7; 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; 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; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000939};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000939};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          32..150
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          205..348
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          269..329
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          177..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        292
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000939-1"
SQ   SEQUENCE   383 AA;  42602 MW;  7991DE1D6E5BD5D7 CRC64;
     MSDTFSRGSV IVTTMMMSSK SVEWLQEELE SGAGSLLLLD CRPHELYESS HIESAINLAI
     PGLMLRRLKK GNLPIRSIIP NNEDKEKFVK RCKTDVVVLY DEASPERQES GLGSSVLGLL
     LQKLRDDGCK AFFLDGGFNK FQSEYPEHCE TNLDCSCPSS SPPSSVLGLG GLRISSDCSD
     GESDREPGSA TESEGSPLPN NQPAFPVQIL PYLYLGCAKD STNLDVLSKY NIKYILNVTP
     NLPNMFEHEG DFKYKQIPIS DHWSQNLSQF FPEAISFIDE ARSKKCGILV HCLAGISRSV
     TVTVAYLMQK LNLSLNDAYD FVKRKKSNIS PNFNFMGQLL DFERTLGLNS PCDNHSTSPT
     HDQLFFTTPT NHNVFQLDTL EST
//
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