DSP2_ORYSJ
ID DSP2_ORYSJ Reviewed; 204 AA.
AC Q0DX67;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable tyrosine-protein phosphatase DSP2 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044};
DE AltName: Full=Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 2 {ECO:0000303|PubMed:22514699};
DE Short=OsPFA-DSP2 {ECO:0000303|PubMed:22514699};
GN Name=DSP2 {ECO:0000305};
GN OrderedLocusNames=Os02g0771400 {ECO:0000312|EMBL:BAF10171.2},
GN LOC_Os02g53160 {ECO:0000305};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22514699; DOI=10.1371/journal.pone.0034995;
RA He H., Su J., Shu S., Zhang Y., Ao Y., Liu B., Feng D., Wang J., Wang H.;
RT "Two homologous putative protein tyrosine phosphatases, OsPFA-DSP2 and
RT AtPFA-DSP4, negatively regulate the pathogen response in transgenic
RT plants.";
RL PLoS ONE 7:E34995-E34995(2012).
CC -!- FUNCTION: Probable tyrosine-protein phosphatase that acts as negative
CC regulator of defense responses against the fungal pathogen Magnaporthe
CC oryzae. {ECO:0000269|PubMed:22514699}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22514699}. Nucleus
CC {ECO:0000269|PubMed:22514699}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and young panicles.
CC {ECO:0000269|PubMed:22514699}.
CC -!- MISCELLANEOUS: Plants overexpressing DSP2 exhibit increased sensitivity
CC to infection by the fungal pathogen Magnaporthe oryzae.
CC {ECO:0000269|PubMed:22514699}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AP008208; BAF10171.2; -; Genomic_DNA.
DR EMBL; AP014958; BAS81119.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0DX67; -.
DR SMR; Q0DX67; -.
DR STRING; 4530.OS02T0771400-00; -.
DR PaxDb; Q0DX67; -.
DR PRIDE; Q0DX67; -.
DR EnsemblPlants; Os02t0771400-00; Os02t0771400-00; Os02g0771400.
DR Gramene; Os02t0771400-00; Os02t0771400-00; Os02g0771400.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_5_2_1; -.
DR InParanoid; Q0DX67; -.
DR OMA; YSCADEN; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020428; PFA-DSPs.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR004861; Siw14-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF03162; Y_phosphatase2; 1.
DR PRINTS; PR01911; PFDSPHPHTASE.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Plant defense; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..204
FT /note="Probable tyrosine-protein phosphatase DSP2"
FT /id="PRO_0000442996"
FT DOMAIN 51..203
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 204 AA; 23172 MW; 6B0CA67DA1506841 CRC64;
MQLEISPRQR SQQQKEEEGE HQQRAGEEAV GAVFSIEPWV DAAAVLVPPL NFAEVNDGIF
RSGFPAADNF AFLLSLKLRS IVYLCPEPYP EENTRFLEQN GIKLHQFGID GSKELLVNIP
EEKIREALKV ILDVRNQPVL IHCKRGKHRT GCVVGCLRKL QKWCLTSVFD EYQHFAAAKA
RSTDQRFMEL FDTSSLMHLT ASQC