DSP1_ARATH
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 03-AUG-2022, entry version 125.
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}; 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}.
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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 PRIDE; 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 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 Genevisible; Q9ZVN4; AT.
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: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; 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 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 para-
FT 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 para-
FT nitrophenyl phosphate 2-fold."
FT /evidence="ECO:0000269|PubMed:17976645"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1XRI"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1XRI"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1XRI"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1XRI"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1XRI"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1XRI"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1XRI"
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
