PTN7_MOUSE
ID PTN7_MOUSE Reviewed; 359 AA.
AC Q8BUM3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
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;
GN Name=Ptpn7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, OXIDATION AT CYS-290, ACTIVITY
RP REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
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 upon FCER1A triggering.
CC {ECO:0000269|PubMed:20157115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20157115}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20157115}. Note=Oxidized
CC form is preferentially associated with actin cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow-derived mast cells.
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; AK083305; BAC38856.1; -; mRNA.
DR EMBL; BC098475; AAH98475.1; -; mRNA.
DR CCDS; CCDS15315.1; -.
DR RefSeq; NP_796055.1; NM_177081.3.
DR RefSeq; XP_006529759.1; XM_006529696.3.
DR RefSeq; XP_006529760.1; XM_006529697.3.
DR RefSeq; XP_006529761.1; XM_006529698.3.
DR AlphaFoldDB; Q8BUM3; -.
DR SMR; Q8BUM3; -.
DR STRING; 10090.ENSMUSP00000045803; -.
DR iPTMnet; Q8BUM3; -.
DR PhosphoSitePlus; Q8BUM3; -.
DR EPD; Q8BUM3; -.
DR jPOST; Q8BUM3; -.
DR MaxQB; Q8BUM3; -.
DR PaxDb; Q8BUM3; -.
DR PRIDE; Q8BUM3; -.
DR ProteomicsDB; 301959; -.
DR Antibodypedia; 20651; 350 antibodies from 30 providers.
DR DNASU; 320139; -.
DR Ensembl; ENSMUST00000049449; ENSMUSP00000045803; ENSMUSG00000031506.
DR Ensembl; ENSMUST00000167080; ENSMUSP00000129474; ENSMUSG00000031506.
DR Ensembl; ENSMUST00000187985; ENSMUSP00000141133; ENSMUSG00000031506.
DR GeneID; 320139; -.
DR KEGG; mmu:320139; -.
DR UCSC; uc007css.1; mouse.
DR CTD; 5778; -.
DR MGI; MGI:2156893; Ptpn7.
DR VEuPathDB; HostDB:ENSMUSG00000031506; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000160979; -.
DR HOGENOM; CLU_001645_10_3_1; -.
DR InParanoid; Q8BUM3; -.
DR OMA; GYDGREK; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q8BUM3; -.
DR TreeFam; TF331016; -.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 320139; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Ptpn7; mouse.
DR PRO; PR:Q8BUM3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BUM3; protein.
DR Bgee; ENSMUSG00000031506; Expressed in thymus and 48 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
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_0000094762"
FT DOMAIN 97..349
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..33
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:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:20157115"
SQ SEQUENCE 359 AA; 40351 MW; E5C62B36E5A77DFD CRC64;
MVQACEGRSR AQLPTLSLGA DMTQPPPTKA PAKKHVRLQE RRGSSVALML DVQSLGTVEP
ICSVNTPREV TLHFLRTAGH PLTRWTLQHQ PPSPKQLEEE FLKIPSNFVN PEDLDIPGHA
SKDRYKTILP NPQSRVCLGR AQSQEDSDYI NANYIRGYDG KEKVYIATQG PMPNTVADFW
EMVWQEDVSL IVMLTQLREG KEKCVHYWPT EEEAYGPFQI RIQDMKEHPE YTVRQLTIQH
QQECRSVKHI LFSAWPDHQT PESAGPLLRL VAEVETPETA ANSGPIVVHC SAGIGRTGCF
IATRIGCQQL KARGEVDILG IVCQLRLDRG GMIQTAEQYQ FLHHTLALYA AQLPPEPNP
