ID H3B1I0_LATCH Unreviewed; 368 AA.
AC H3B1I0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
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};
GN Name=DUSP1 {ECO:0000313|Ensembl:ENSLACP00000015751.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000015751.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000015751.1}
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|ARBA:ARBA00001490,
CC ECO:0000256|PIRNR:PIRNR000939};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 EMBL; AFYH01040193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01040194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005992564.1; XM_005992502.2.
DR AlphaFoldDB; H3B1I0; -.
DR STRING; 7897.ENSLACP00000015751; -.
DR Ensembl; ENSLACT00000015861.1; ENSLACP00000015751.1; ENSLACG00000013873.1.
DR GeneID; 102364866; -.
DR KEGG; lcm:102364866; -.
DR CTD; 1843; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159044; -.
DR HOGENOM; CLU_027074_0_2_1; -.
DR InParanoid; H3B1I0; -.
DR OMA; PSCSPCN; -.
DR OrthoDB; 2901840at2759; -.
DR TreeFam; TF105122; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000013873; Expressed in pectoral fin and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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:SF309; DUAL SPECIFICITY PROTEIN PHOSPHATASE 1; 1.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000939};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|PIRNR:PIRNR000939};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 21..138
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 175..316
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 237..294
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 260
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000939-1"
SQ SEQUENCE 368 AA; 40135 MW; 4C1A594C20221E02 CRC64;
MVIMEVSNVD SFTFKGLLED DAAKCLVLDC RSFFSFNSSH VMNSANVRFS TIVRRRAKGA
MGLEHIVPNE ELRNKLISGL YQAIVVLDER TSDFELIKKD STVMLVVNTL NRESCGTKIY
FLGGGFESFS SAFPEFCTKP SPPAGLSLPL SGNSVPGSAE SGCSSCATPL YDQGGPVEIL
PFLYLGSAFH ASRKDMLDTL GITALINVSA NCPNHFEGHY QYKSIPVEDN HKADISSWFN
EAIEFIDSAK KAGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
FSFMGQLLQF ESQVLAPSCS AEASSPARAV LDRGTPTTTV FNFPVSIPVH SAANSLSYLH
SPIASPSY
//
