DSP2_ARATH
ID DSP2_ARATH Reviewed; 257 AA.
AC Q84MD6; O48769;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tyrosine-protein phosphatase DSP2 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:21409566};
DE AltName: Full=Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 2 {ECO:0000303|PubMed:21409566};
DE Short=AtPFA-DSP2 {ECO:0000303|PubMed:21409566};
GN Name=DSP2 {ECO:0000305};
GN OrderedLocusNames=At2g32960 {ECO:0000312|Araport:AT2G32960};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17976645; DOI=10.1016/j.jmb.2007.10.008;
RA Roma-Mateo C., Rios P., Tabernero L., Attwood T.K., Pulido R.;
RT "A novel phosphatase family, structurally related to dual-specificity
RT phosphatases, that displays unique amino acid sequence and substrate
RT specificity.";
RL J. Mol. Biol. 374:899-909(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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).
CC -!- FUNCTION: Possesses phosphotyrosine phosphatase activity in vitro
CC (PubMed:21409566). Hydrolyzes para-nitrophenyl phosphate in vitro
CC (PubMed:17976645, PubMed:21409566). Hydrolyzes O-methylfluorescein
CC phosphate in vitro. Dephosphorylates the phosphoinositides PI(3,5)P2
CC (PubMed:21409566). {ECO:0000269|PubMed:17976645,
CC ECO:0000269|PubMed:21409566}.
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, ECO:0000269|PubMed:21409566};
CC -!- INTERACTION:
CC Q84MD6; Q17TI5: BRX; NbExp=6; IntAct=EBI-4424266, EBI-4426649;
CC Q84MD6; Q84MD6: DSP2; NbExp=3; IntAct=EBI-4424266, EBI-4424266;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:21409566}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB91974.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003033; AAB91974.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08767.1; -; Genomic_DNA.
DR EMBL; BT006379; AAP21187.1; -; mRNA.
DR EMBL; AK227524; BAE99524.1; -; mRNA.
DR PIR; T01111; T01111.
DR RefSeq; NP_180855.2; NM_128856.5.
DR AlphaFoldDB; Q84MD6; -.
DR SMR; Q84MD6; -.
DR IntAct; Q84MD6; 2.
DR STRING; 3702.AT2G32960.1; -.
DR PaxDb; Q84MD6; -.
DR PRIDE; Q84MD6; -.
DR ProteomicsDB; 221912; -.
DR EnsemblPlants; AT2G32960.1; AT2G32960.1; AT2G32960.
DR GeneID; 817858; -.
DR Gramene; AT2G32960.1; AT2G32960.1; AT2G32960.
DR KEGG; ath:AT2G32960; -.
DR Araport; AT2G32960; -.
DR TAIR; locus:2059349; AT2G32960.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_5_0_1; -.
DR InParanoid; Q84MD6; -.
DR OMA; FHTIEVA; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q84MD6; -.
DR PRO; PR:Q84MD6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84MD6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
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 1: Evidence at protein level;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..257
FT /note="Tyrosine-protein phosphatase DSP2"
FT /id="PRO_0000442992"
FT DOMAIN 66..251
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 192
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 257 AA; 29159 MW; AD7441B8DD528907 CRC64;
MKLIEKTMSM NQFRTMEEEK QDGGELFHTI EVAKVDRNNV SQPPPAATAA LLEVPGDELN
LIPPLNFSMV DNGIFRSGFP DSANFSFIKT LGLRSIISLC PEPYPENNMQ FLKSNGISLF
QFGIEGSKSK CLPGLENEVW LHIWSSKHQK EDFYTNGNSK TSEPFVDILD QKIREALKVL
LDEKNHPLLI HCKRGKHRTG CLVGCMRKLQ KWCITSILDE YKRFAAAKAR VSDQRFLESF
DVSGLKHTPM SFSCSNR
