ID DSP1_ARATH Reviewed; 215 AA. AC Q9ZVN4; Q0WS70; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Tyrosine-protein phosphatase DSP1 {ECO:0000305}; DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:18433060, ECO:0000269|PubMed:21409566}; DE AltName: Full=Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 1 {ECO:0000303|PubMed:21409566}; DE Short=AtPFA-DSP1 {ECO:0000303|PubMed:21409566}; DE AltName: Full=Tyrosine-protein phosphatase At1g05000 {ECO:0000305}; GN Name=DSP1 {ECO:0000305}; GN Synonyms=PTP135 {ECO:0000312|EMBL:ACU43461.1}; GN OrderedLocusNames=At1g05000; ORFNames=T7A14.14; 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 Gao Z., Jia W.; RT "Arabidopsis thaliana PTP135 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). 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=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 [5] 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 [6] RP FUNCTION, AND MUTAGENESIS OF GLU-117 AND ASP-191. 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP CYS-150 AND HIS-155. 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 X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 52-202. RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019; RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.; RT "Ensemble refinement of protein crystal structures: validation and RT application."; RL Structure 15:1040-1052(2007). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 52-202, FUNCTION, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=18433060; DOI=10.1002/prot.22041; RA Aceti D.J., Bitto E., Yakunin A.F., Proudfoot M., Bingman C.A., RA Frederick R.O., Sreenath H.K., Vojtik F.C., Wrobel R.L., Fox B.G., RA Markley J.L., Phillips G.N.; RT "Structural and functional characterization of a novel phosphatase from the RT Arabidopsis thaliana gene locus At1g05000."; RL Proteins 73:241-253(2008). CC -!- FUNCTION: Possesses phosphotyrosine phosphatase activity in vitro. CC Hydrolyzes para-nitrophenyl phosphate in vitro (PubMed:21409566, CC PubMed:18433060). Hydrolyzes O-methylfluorescein phosphate in vitro CC (PubMed:21409566). Hydrolyzes polyphosphate and ATP in vitro CC (PubMed:18433060). Dephosphorylates the phosphoinositides PI(3,4,5)P3, CC PI(3,5)P2, but not PI(3)P, PI(3,4)P2 or PI(4,5)P2 (PubMed:17976645). CC {ECO:0000269|PubMed:17976645, ECO:0000269|PubMed:18433060, 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:18433060, CC ECO:0000269|PubMed:21409566}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.063 mM for polyphosphate {ECO:0000269|PubMed:18433060}; CC KM=0.38 mM for ATP {ECO:0000269|PubMed:18433060}; CC KM=0.88 mM for phosphotyrosine {ECO:0000269|PubMed:18433060}; CC KM=0.67 mM for para-nitrophenyl phosphate CC {ECO:0000269|PubMed:18433060}; CC pH dependence: CC Optimum pH is 5.0 (with polyphosphate as substrate). CC {ECO:0000269|PubMed:18433060}; CC -!- SUBUNIT: Homomultimer (Probable). Homodimer and homohexamer CC (PubMed:18433060). {ECO:0000269|PubMed:18433060, ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9ZVN4-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Highly expressed in siliques and at lower levels in CC roots, leaves and flowers. {ECO:0000269|PubMed:21409566}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ605097; ACU43461.1; -; Genomic_DNA. DR EMBL; AC005322; AAC97999.1; -; Genomic_DNA. DR EMBL; CP002684; AEE27777.1; -; Genomic_DNA. DR EMBL; AK228069; BAF00029.1; -; mRNA. DR EMBL; BT005210; AAO63274.1; -; mRNA. DR PIR; G86183; G86183. DR RefSeq; NP_171993.1; NM_100379.3. [Q9ZVN4-1] DR PDB; 1XRI; X-ray; 3.30 A; A/B=52-202. DR PDB; 2Q47; X-ray; 3.30 A; A/B=52-202. DR PDB; 7MOD; X-ray; 1.65 A; A/B=49-215. DR PDB; 7MOE; X-ray; 1.70 A; A/B=49-215. DR PDB; 7MOF; X-ray; 1.95 A; A/B=49-215. DR PDB; 7MOG; X-ray; 1.80 A; A/B=49-215. DR PDB; 7MOH; X-ray; 1.90 A; A/B=49-215. DR PDB; 7MOI; X-ray; 1.80 A; A/B=49-215. DR PDB; 7MOJ; X-ray; 1.90 A; A/B=49-215. DR PDB; 7MOK; X-ray; 1.85 A; A/B=49-215. DR PDB; 7MOL; X-ray; 1.90 A; A/B=49-215. DR PDB; 7MOM; X-ray; 1.70 A; A/B=49-215. DR PDBsum; 1XRI; -. DR PDBsum; 2Q47; -. DR PDBsum; 7MOD; -. DR PDBsum; 7MOE; -. DR PDBsum; 7MOF; -. DR PDBsum; 7MOG; -. DR PDBsum; 7MOH; -. DR PDBsum; 7MOI; -. DR PDBsum; 7MOJ; -. DR PDBsum; 7MOK; -. DR PDBsum; 7MOL; -. DR PDBsum; 7MOM; -. DR AlphaFoldDB; Q9ZVN4; -. DR SMR; Q9ZVN4; -. DR BioGRID; 24583; 17. DR STRING; 3702.Q9ZVN4; -. DR ProteomicsDB; 224295; -. [Q9ZVN4-1] DR DNASU; 839348; -. DR EnsemblPlants; AT1G05000.1; AT1G05000.1; AT1G05000. [Q9ZVN4-1] DR GeneID; 839348; -. DR Gramene; AT1G05000.1; AT1G05000.1; AT1G05000. [Q9ZVN4-1] DR KEGG; ath:AT1G05000; -. DR Araport; AT1G05000; -. DR TAIR; AT1G05000; PFA-DSP1. DR HOGENOM; CLU_047845_5_0_1; -. DR InParanoid; Q9ZVN4; -. DR PhylomeDB; Q9ZVN4; -. DR EvolutionaryTrace; Q9ZVN4; -. DR PRO; PR:Q9ZVN4; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9ZVN4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR CDD; cd14528; PFA-DSP_Siw14; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR31126:SF48; TYROSINE-PROTEIN PHOSPHATASE DSP1; 1. DR Pfam; PF03162; Y_phosphatase2; 1. DR PRINTS; PR01911; PFDSPHPHTASE. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q9ZVN4; AT. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Hydrolase; Protein phosphatase; KW Reference proteome. FT CHAIN 1..215 FT /note="Tyrosine-protein phosphatase DSP1" FT /id="PRO_0000094923" FT DOMAIN 58..209 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 150 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MUTAGEN 117 FT /note="E->A: Reduces phosphatase activity toward FT para-nitrophenyl phosphate 2-fold." FT /evidence="ECO:0000269|PubMed:17976645" FT MUTAGEN 150 FT /note="C->S: Abolishes tyrosine-protein phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:21409566" FT MUTAGEN 155 FT /note="H->G,S: Abolishes phosphatase activity toward the FT phosphoinositides PI(3,4,5)P3 and PI(3,5)P2; reduces FT phosphatase activity toward para-nitrophenyl phosphate and FT O-methylfluorescein phosphate." FT /evidence="ECO:0000269|PubMed:21409566" FT MUTAGEN 191 FT /note="D->A: Reduces phosphatase activity toward FT para-nitrophenyl phosphate 2-fold." FT /evidence="ECO:0000269|PubMed:17976645" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:7MOD" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 77..81 FT /evidence="ECO:0007829|PDB:7MOD" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:7MOD" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:7MOD" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:1XRI" FT HELIX 128..139 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:7MOD" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:7MOD" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 172..183 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 189..197 FT /evidence="ECO:0007829|PDB:7MOD" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:7MOD" SQ SEQUENCE 215 AA; 24537 MW; 24BCB3033CBCFA3A CRC64; MKLVEKTTTT EQDNGEDFCR TIIEVSEVNR NVFQAPGGEA DPFRVVSGEE LHLIPPLNFS MVDNGIFRSG FPDSANFSFL QTLGLRSIIY LCPEPYPESN LQFLKSNGIR LFQFGIEGNK EPFVNIPDHK IRMALKVLLD EKNHPVLIHC KRGKHRTGCL VGCLRKLQKW CLTSIFDEYQ RFAAAKARVS DQRFMEIFDV SSFSHIPMSF SCSIR //