ID A0A3B5B280_9TELE Unreviewed; 195 AA.
AC A0A3B5B280;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=DUSP26 {ECO:0000313|Ensembl:ENSSPAP00000027275.1};
GN Synonyms=LOC103367618 {ECO:0000313|RefSeq:XP_008293925.1,
GN ECO:0000313|RefSeq:XP_008293926.1, ECO:0000313|RefSeq:XP_008293927.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000027275.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000027275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008293925.1, ECO:0000313|RefSeq:XP_008293926.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- SUBUNIT: Interacts with HSF4. {ECO:0000256|ARBA:ARBA00038621}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 RefSeq; XP_008293925.1; XM_008295703.1.
DR RefSeq; XP_008293926.1; XM_008295704.1.
DR RefSeq; XP_008293927.1; XM_008295705.1.
DR AlphaFoldDB; A0A3B5B280; -.
DR STRING; 144197.ENSSPAP00000027275; -.
DR Ensembl; ENSSPAT00000027719.1; ENSSPAP00000027275.1; ENSSPAG00000020566.1.
DR GeneID; 103367618; -.
DR GeneTree; ENSGT00940000158107; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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:SF8; DUAL SPECIFICITY PROTEIN PHOSPHATASE 26; 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 Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000694891}.
FT DOMAIN 47..192
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 114..171
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 137
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR620405-1"
SQ SEQUENCE 195 AA; 21824 MW; 75DFA1AD16AD98BB CRC64;
MSYTSKLPAS WNDERPPRKV EIDLSSPGLA VFELERLLFT GKAIISHANE VWPRLYIGDQ
DSAENRADLS MHRITHILNA AHSKRRGRPE IYEGMRITYM GIEAHDSCGF DMSVNFQAAA
DFIQSALSRG GKVLVHCHVG VSRSATLVLA YLMLKQNLTL VEAICAVKDN RGVIPNRGFL
RQLIKLDGQL FGKHH
//
