PTP1_ARATH
ID PTP1_ARATH Reviewed; 340 AA.
AC O82656; O65190;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein-tyrosine-phosphatase PTP1;
DE EC=3.1.3.48;
DE AltName: Full=Protein tyrosine phosphatase 1;
DE Short=AtPTP1;
GN Name=PTP1; OrderedLocusNames=At1g71860; ORFNames=F14O23.24;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF ASP-234 AND CYS-265.
RX PubMed=9596642; DOI=10.2307/3870670;
RA Xu Q., Fu H.H., Gupta R., Luan S.;
RT "Molecular characterization of a tyrosine-specific protein phosphatase
RT encoded by a stress-responsive gene in Arabidopsis.";
RL Plant Cell 10:849-857(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10092185; DOI=10.1023/a:1006170902271;
RA Fordham-Skelton A.P., Skipsey M., Eveans I.M., Edwards R., Gatehouse J.A.;
RT "Higher plant tyrosine-specific protein phosphatases (PTPs) contain novel
RT amino-terminal domains: expression during embryogenesis.";
RL Plant Mol. Biol. 39:593-605(1999).
RN [3]
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 [4]
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 [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 FUNCTION.
RX PubMed=10759527; DOI=10.1104/pp.122.4.1301;
RA Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.;
RT "ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is
RT activated in vitro by AtMEK1 through threonine phosphorylation.";
RL Plant Physiol. 122:1301-1310(2000).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=12857797; DOI=10.1104/pp.103.020792;
RA Gupta R., Luan S.;
RT "Redox control of protein tyrosine phosphatases and mitogen-activated
RT protein kinases in plants.";
RL Plant Physiol. 132:1149-1152(2003).
RN [8]
RP FUNCTION, INTERACTION WITH MPK6, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19789277; DOI=10.1105/tpc.109.067678;
RA Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., Hirt H.,
RA Buchala A., Metraux J.P., Peck S.C., Ulm R.;
RT "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors
RT of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis.";
RL Plant Cell 21:2884-2897(2009).
RN [9]
RP INTERACTION WITH KIN10 AND MPK6, MUTAGENESIS OF SER-7 AND SER-8, AND
RP PHOSPHORYLATION.
RX PubMed=27029354; DOI=10.1093/jxb/erw107;
RA Cho H.Y., Wen T.N., Wang Y.T., Shih M.C.;
RT "Quantitative phosphoproteomics of protein kinase SnRK1 regulated protein
RT phosphorylation in Arabidopsis under submergence.";
RL J. Exp. Bot. 67:2745-2760(2016).
CC -!- FUNCTION: Protein-tyrosine-phosphatase that dephosphorylates and
CC probably inhibits MPK6 in non-oxidative stress conditions. In
CC association with MKP1, represses salicylic acid (SA) and camalexin
CC biosynthesis, thus modulating defense response. May also repress MPK3.
CC Dephosphorylates and inactivates MPK4 in vitro.
CC {ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:12857797,
CC ECO:0000269|PubMed:19789277, ECO:0000269|PubMed:9596642}.
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 -!- ACTIVITY REGULATION: Inhibited by hydrogen peroxide.
CC {ECO:0000269|PubMed:12857797}.
CC -!- SUBUNIT: Interacts with MPK6 (PubMed:19789277). Interacts with KIN10
CC (PubMed:27029354). {ECO:0000269|PubMed:19789277,
CC ECO:0000269|PubMed:27029354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19789277}.
CC Nucleus {ECO:0000269|PubMed:19789277}.
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=O82656-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and flowers, and at low
CC levels in leaves. {ECO:0000269|PubMed:9596642}.
CC -!- INDUCTION: By salt treatment. Down-regulated by cold.
CC {ECO:0000269|PubMed:9596642}.
CC -!- PTM: Phosphorylated by KIN10. {ECO:0000269|PubMed:27029354}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19789277}.
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DR EMBL; AF055635; AAC68859.1; -; mRNA.
DR EMBL; AJ006309; CAA06978.1; -; Genomic_DNA.
DR EMBL; AC012654; AAF43239.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35242.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35243.1; -; Genomic_DNA.
DR EMBL; AY070403; AAL49899.1; -; mRNA.
DR EMBL; AY117240; AAM51315.1; -; mRNA.
DR PIR; C96741; C96741.
DR PIR; T51846; T51846.
DR RefSeq; NP_001031266.1; NM_001036189.1. [O82656-1]
DR RefSeq; NP_177331.1; NM_105844.4. [O82656-1]
DR PDB; 6KRW; X-ray; 1.40 A; A=29-334.
DR PDB; 6KRX; X-ray; 1.70 A; A=1-340.
DR PDBsum; 6KRW; -.
DR PDBsum; 6KRX; -.
DR AlphaFoldDB; O82656; -.
DR SMR; O82656; -.
DR BioGRID; 28736; 4.
DR IntAct; O82656; 1.
DR MINT; O82656; -.
DR STRING; 3702.AT1G71860.1; -.
DR iPTMnet; O82656; -.
DR PaxDb; O82656; -.
DR PRIDE; O82656; -.
DR ProteomicsDB; 226435; -. [O82656-1]
DR EnsemblPlants; AT1G71860.1; AT1G71860.1; AT1G71860. [O82656-1]
DR EnsemblPlants; AT1G71860.3; AT1G71860.3; AT1G71860. [O82656-1]
DR GeneID; 843516; -.
DR Gramene; AT1G71860.1; AT1G71860.1; AT1G71860. [O82656-1]
DR Gramene; AT1G71860.3; AT1G71860.3; AT1G71860. [O82656-1]
DR KEGG; ath:AT1G71860; -.
DR Araport; AT1G71860; -.
DR TAIR; locus:2012991; AT1G71860.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_001645_9_7_1; -.
DR InParanoid; O82656; -.
DR OMA; HFYFDQW; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O82656; -.
DR PRO; PR:O82656; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O82656; baseline and differential.
DR Genevisible; O82656; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IGI:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Plant defense; Protein phosphatase; Reference proteome.
FT CHAIN 1..340
FT /note="Protein-tyrosine-phosphatase PTP1"
FT /id="PRO_0000417329"
FT DOMAIN 58..326
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 265
FT /note="Phosphocysteine intermediate"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 265..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 7
FT /note="S->D: Disrupt binding to MPK6; when associated with
FT D-8."
FT /evidence="ECO:0000269|PubMed:27029354"
FT MUTAGEN 8
FT /note="S->D: Disrupt binding to MPK6; when associated with
FT D-7."
FT /evidence="ECO:0000269|PubMed:27029354"
FT MUTAGEN 234
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9596642"
FT MUTAGEN 265
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9596642"
FT CONFLICT 147
FT /note="D -> A (in Ref. 1; AAC68859)"
FT /evidence="ECO:0000305"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6KRW"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6KRW"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 206..216
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6KRW"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 270..287
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:6KRW"
FT HELIX 313..331
FT /evidence="ECO:0007829|PDB:6KRW"
SQ SEQUENCE 340 AA; 37799 MW; 7885C03A664CA02D CRC64;
MATGKTSSAA NLFTGSTRFD LSSADSPPSK LSLSSDQLNH CHQALGVFRG KIQNPDSIAH
EFTGLQANRM WPSELLLNST VAMNSVNVEK NRYSDVVPFD KNRIVLNPCK DSSAKGYVNA
SLIKTSESES ISQFIATQGP LPHTMEDFWE MVIQQHCPII VMLTRLVDNN RTVKCGDYFQ
DEDGPREFGN ISLTTKWIKT TDTSLMLRNL EVNYKETEDQ PMSVLHIQYP EWPDHGVPKD
TVAVREILKR LYQVPPSLGP IIVHCSAGIG RTGTYCAIHN TIQRILAGDM SALDLAKTVA
LFRKQRIGMV QTMDQYFFCY NAIVDELEDL TAGTNAGTSS
