PDSP4_ARATH
ID PDSP4_ARATH Reviewed; 198 AA.
AC Q940L5; O81513;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable tyrosine-protein phosphatase DSP4 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044};
DE AltName: Full=Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 4 {ECO:0000303|PubMed:21409566};
DE Short=AtPFA-DSP4 {ECO:0000303|PubMed:21409566};
GN Name=DSP4 {ECO:0000305}; Synonyms=PN18 {ECO:0000312|EMBL:ACU43462.1};
GN OrderedLocusNames=At4g03960 {ECO:0000312|Araport:AT4G03960};
GN ORFNames=T24M8.4 {ECO:0000312|EMBL:AAC28219.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Xie M., Jia W.;
RT "Arabidopsis thaliana PN18 gene, complete cds.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21409566; DOI=10.1007/s00438-011-0611-6;
RA Roma-Mateo C., Sacristan-Reviriego A., Beresford N.J.,
RA Caparros-Martin J.A., Culianez-Macia F.A., Martin H., Molina M.,
RA Tabernero L., Pulido R.;
RT "Phylogenetic and genetic linkage between novel atypical dual-specificity
RT phosphatases from non-metazoan organisms.";
RL Mol. Genet. Genomics 285:341-354(2011).
RN [8]
RP FUNCTION.
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 bacterial pathogen
CC Pseudomonas syringae pv tomato strain DC3000.
CC {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 -!- TISSUE SPECIFICITY: Highly expressed in flowers and at lower levels in
CC roots, leaves, stems and siliques. {ECO:0000269|PubMed:21409566}.
CC -!- MISCELLANEOUS: Plants overexpressing DSP4 exhibit increased sensitivity
CC to infection by the bacterial pathogen Pseudomonas syringae pv tomato
CC strain DC3000. {ECO:0000269|PubMed:22514699}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80819.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ605098; ACU43462.1; -; Genomic_DNA.
DR EMBL; AF077409; AAC28219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161498; CAB80819.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82361.1; -; Genomic_DNA.
DR EMBL; AK118704; BAC43298.1; -; mRNA.
DR EMBL; AF458342; AAL51114.1; -; mRNA.
DR EMBL; AY054279; AAL06938.1; -; mRNA.
DR EMBL; AY086713; AAM63767.1; -; mRNA.
DR PIR; T01867; T01867.
DR RefSeq; NP_567261.1; NM_116634.4.
DR AlphaFoldDB; Q940L5; -.
DR SMR; Q940L5; -.
DR STRING; 3702.AT4G03960.1; -.
DR PaxDb; Q940L5; -.
DR PRIDE; Q940L5; -.
DR ProteomicsDB; 251350; -.
DR EnsemblPlants; AT4G03960.1; AT4G03960.1; AT4G03960.
DR GeneID; 825706; -.
DR Gramene; AT4G03960.1; AT4G03960.1; AT4G03960.
DR KEGG; ath:AT4G03960; -.
DR Araport; AT4G03960; -.
DR TAIR; locus:2136718; AT4G03960.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_5_0_1; -.
DR InParanoid; Q940L5; -.
DR OMA; PQSENSM; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q940L5; -.
DR PRO; PR:Q940L5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q940L5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:1900424; P:regulation of defense response to bacterium; IMP:TAIR.
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; IPR000387; Tyr_Pase_dom.
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; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Plant defense; Protein phosphatase; Reference proteome.
FT CHAIN 1..198
FT /note="Probable tyrosine-protein phosphatase DSP4"
FT /id="PRO_0000442994"
FT DOMAIN 34..188
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 198 AA; 22640 MW; 7A18DF8AB29EBA3B CRC64;
MTLESYAGDV HTVPQSENSM EERGGGELFV PPLNFAMVDN GIFRSGFPEP VSFSFLQSLR
LKSIIYLCPE AYPEVNREFA KSNGIQVFQF GIERCKEPFV NIPDEVIREA LQVLLDTENH
PVLIHCKSGK HRTGCLVGCV RKIQRWCLSS IFDEYQRFAA AKARISDQRF MELFDISNLK
HTPLSFSCSK RYTNTIDY
