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   27-MAR-2024, entry version 157.
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=10.1105/tpc.10.5.849;
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.O82656; -.
DR   iPTMnet; O82656; -.
DR   PaxDb; 3702-AT1G71860-1; -.
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; AT1G71860; PTP1.
DR   eggNOG; KOG0789; Eukaryota.
DR   HOGENOM; CLU_001645_9_7_1; -.
DR   InParanoid; O82656; -.
DR   OMA; YYYKWAD; -.
DR   OrthoDB; 5399547at2759; -.
DR   PhylomeDB; O82656; -.
DR   PRO; PR:O82656; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O82656; baseline and differential.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:TAIR.
DR   GO; GO:0031348; P:negative regulation of defense response; IGI:UniProtKB.
DR   CDD; cd17658; PTPc_plant_PTP1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   Genevisible; O82656; AT.
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
//