PTN7_RAT
ID PTN7_RAT Reviewed; 359 AA.
AC P49445;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 7;
DE EC=3.1.3.48;
DE AltName: Full=Hematopoietic protein-tyrosine phosphatase;
DE Short=HEPTP;
DE AltName: Full=Protein-tyrosine phosphatase LC-PTP;
GN Name=Ptpn7; Synonyms=Lcptp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7545170; DOI=10.1074/jbc.270.37.21902;
RA Swieter M., Berenstein E.H., Swaim W.D., Siraganian R.P.;
RT "Aggregation of IgE receptors in rat basophilic leukemia 2H3 cells induces
RT tyrosine phosphorylation of the cytosolic protein-tyrosine phosphatase
RT HePTP.";
RL J. Biol. Chem. 270:21902-21906(1995).
RN [2]
RP SUBCELLULAR LOCATION, OXIDATION AT CYS-290, AND ACTIVITY REGULATION.
RX PubMed=20157115; DOI=10.1074/jbc.m109.052555;
RA Heneberg P., Draberova L., Bambouskova M., Pompach P., Draber P.;
RT "Down-regulation of protein-tyrosine phosphatases activates an immune
RT receptor in the absence of its translocation into lipid rafts.";
RL J. Biol. Chem. 285:12787-12802(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in the regulation of T and B-lymphocyte
CC development and signal transduction. {ECO:0000250}.
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 in cells after FCER1A triggering.
CC {ECO:0000269|PubMed:20157115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20157115}.
CC -!- PTM: Oxidized at active site cysteine. Treatment with pervanadate
CC (vanadate and H(2)O(2)) or with antigen enhanced oxidation of active
CC site cysteine. {ECO:0000269|PubMed:20157115}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; U28356; AAA84443.1; -; mRNA.
DR RefSeq; NP_663716.1; NM_145683.1.
DR RefSeq; XP_006249883.1; XM_006249821.3.
DR AlphaFoldDB; P49445; -.
DR SMR; P49445; -.
DR STRING; 10116.ENSRNOP00000007833; -.
DR iPTMnet; P49445; -.
DR PhosphoSitePlus; P49445; -.
DR PaxDb; P49445; -.
DR Ensembl; ENSRNOT00000007833; ENSRNOP00000007833; ENSRNOG00000005807.
DR GeneID; 246781; -.
DR KEGG; rno:246781; -.
DR UCSC; RGD:708516; rat.
DR CTD; 5778; -.
DR RGD; 708516; Ptpn7.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000160979; -.
DR HOGENOM; CLU_001645_10_3_1; -.
DR InParanoid; P49445; -.
DR OMA; GYDGREK; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P49445; -.
DR TreeFam; TF331016; -.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P49445; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000005807; Expressed in thymus and 19 other tissues.
DR Genevisible; P49445; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
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 InterPro; IPR008356; Tyr_Pase_KIM-con.
DR PANTHER; PTHR46198; PTHR46198; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR01778; KIMPTPASE.
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 Cytoplasm; Cytoskeleton; Hydrolase; Oxidation; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..359
FT /note="Tyrosine-protein phosphatase non-receptor type 7"
FT /id="PRO_0000094763"
FT DOMAIN 97..349
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..51
FT /note="Interaction with MAP kinases"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290..296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35236"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35236"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35236"
FT MOD_RES 290
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:20157115"
SQ SEQUENCE 359 AA; 40314 MW; 5B98E196DB633677 CRC64;
MVQACEGRSR AQLPTLSLGA DMTQPPPAKA PAKKHVRLQE RRGSSVALML DVRSLGTVEP
ICSVNTPREV TLHFLRTAGH PLTRWTLQHQ PPSPKQLEEE FLKIPSNFVN PEDLDIPGHA
SKDRYKTILP NPQSRVCLGR AHSQEDSDYI NANYIRGYDG KEKVYIATQG PMPNTVADFW
EMVWQEDVSL IVMLTQLREG KEKCVHYWPT EEEAYGPFQI RIQGMKEHPE YTVRHLTIQH
QQECRSVKHI LFSAWPDHQT PESAGPLLRL VAEVETPETA ANSGPIVVHC SAGIGRTGCF
IATRIGCQQL KARGEVDILG IVCQLRLDRG GMIQTAEQYQ FLHHTLALYA AQLPPETDP
