ID A0A087WZU1_HUMAN Unreviewed; 2299 AA. AC A0A087WZU1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 13-FEB-2019, entry version 41. DE SubName: Full=Phosphatidylinositol phosphatase PTPRQ {ECO:0000313|Ensembl:ENSP00000482885}; GN Name=PTPRQ {ECO:0000313|Ensembl:ENSP00000482885}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000482885, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000482885, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A., null.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000482885} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000495607} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2018) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] CC + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; CC Evidence={ECO:0000256|SAAS:SAAS01128831}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABBA01053496; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC074031; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083812; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001138498.1; NM_001145026.1. DR UniGene; Hs.539284; -. DR ProteinModelPortal; A0A087WZU1; -. DR IntAct; A0A087WZU1; 8. DR PeptideAtlas; A0A087WZU1; -. DR Ensembl; ENST00000614701; ENSP00000482885; ENSG00000139304. DR Ensembl; ENST00000644991; ENSP00000495607; ENSG00000139304. DR GeneID; 374462; -. DR KEGG; hsa:374462; -. DR UCSC; uc031zgj.2; human. DR CTD; 374462; -. DR EuPathDB; HostDB:ENSG00000139304.12; -. DR HGNC; HGNC:9679; PTPRQ. DR OpenTargets; ENSG00000139304; -. DR GeneTree; ENSGT00940000159215; -. DR KO; K16910; -. DR OrthoDB; 411281at2759; -. DR ChiTaRS; PTPRQ; human. DR GenomeRNAi; 374462; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000139304; Expressed in 77 organ(s), highest expression level in kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0032421; C:stereocilium bundle; IEA:Ensembl. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0060116; P:vestibular receptor cell morphogenesis; IEA:Ensembl. DR CDD; cd00063; FN3; 15. DR Gene3D; 2.60.40.10; -; 14. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTPase_domain. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR Pfam; PF00041; fn3; 12. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 16. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF49265; SSF49265; 8. DR SUPFAM; SSF52799; SSF52799; 1. DR PROSITE; PS50853; FN3; 17. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Hydrolase {ECO:0000256|SAAS:SAAS01031415}; KW Membrane {ECO:0000256|SAAS:SAAS00897767, ECO:0000256|SAM:Phobius}; KW Protein phosphatase {ECO:0000256|SAAS:SAAS01031415}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00897767, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00897767, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 2299 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001832099. FT TRANSMEM 1906 1928 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 57 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 58 153 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 157 252 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 308 396 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 399 497 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 568 663 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 668 757 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 762 852 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 857 946 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 951 1051 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1056 1148 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1150 1240 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1245 1338 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1342 1428 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1432 1536 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1541 1639 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 1644 1745 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 2003 2259 Tyrosine-protein phosphatase. FT {ECO:0000259|PROSITE:PS50055}. FT DOMAIN 2179 2250 TYR_PHOSPHATASE_2. FT {ECO:0000259|PROSITE:PS50056}. FT ACT_SITE 2200 2200 Phosphocysteine intermediate. FT {ECO:0000256|PROSITE-ProRule:PRU00160}. SQ SEQUENCE 2299 AA; 257263 MW; 8F4F19B947ED83F9 CRC64; MDFLIIFLLL FIGTSETQVD VSNVVPGTRY DITISSISTT YTSPVTRIVT TNVTKPGPPV FLAGERVGSA GILLSWNTPP NPNGRIISYI VKYKEVCPWM QTVYTQVRSK PDSLEVLLTN LNPGTTYEIK VAAENSAGIG VFSDPFLFQT AESAPGKVVN LTVEAYNASA VKLIWYLPRQ PNGKITSFKI SVKHARSGIV VKDVSIRVED ILTGKLPECN ENSESFLWST ASPSPTLGRV TPPSRTTHSS STLTQNEISS VWKEPISFVV THLRPYTTYL FEVSAATTEA GYIDSTIVRT PESVPEGPPQ NCVTGNITGK SFSILWDPPT IVTGKFSYRV ELYGPSGRIL DNSTKDLKFA FTNLTPFTMY DVYIAAETSA GTGPKSNISV FTPPDVPGAV FDLQLAEVES TQVRITWKKP RQPNGIINQY RVKVLVPETG IILENTLLTG NNEYINDPMA PEIVNIVEPM VGLYEGSAEM SSDLHSLATF IYNSHPDKNF PARNRAEDQT SPVVTTRNQY ITDIAAEQLS YVIRRLVPFT EHMISVSAFT IMGEGPPTVL SVRTRQQVPS SIKIINYKNI SSSSILLYWD PPEYPNGKIT HYTIYAMELD TNRAFQITTI DNSFLITGLK KYTKYKMRVA ASTHVGESSL SEENDIFVRT SEDEPESSPQ DVEVIDVTAD EIRLKWSPPE KPNGIIIAYE VLYKNIDTLY MKNTSTTDII LRNLRPHTLY NISVRSYTRF GHGNQVSSLL SVRTSETVPD SAPENITYKN ISSGEIELSF LPPSSPNGII QKYTIYLKRS NGNEERTINT TSLTQNIKVL KKYTQYIIEV SASTLKGEGV RSAPISILTE EDAPDSPPQD FSVKQLSGVT VKLSWQPPLE PNGIILYYTV YVWNRSSLKT INVTETSLEL SDLDYNVEYS AYVTASTRFG DGKTRSNIIS FQTPEGAPSD PPKDVYYANL SSSSIILFWT PPSKPNGIIQ YYSVYYRNTS GTFMQNFTLH EVTNDFDNMT VSTIIDKLTI FSYYTFWLTA STSVGNGNKS SDIIEVYTDQ DIPEGFVGNL TYESISSTAI NVSWVPPAQP NGLVFYYVSL ILQQTPRHVR PPLVTYERSI YFDNLEKYTD YILKITPSTE KGFSDTYTAQ LYIKTEEDVP ETSPIINTFK NLSSTSVLLS WDPPVKPNGA IISYDLTLQG PNENYSFITS DNYIILEELS PFTLYSFFAA ARTRKGLGPS SILFFYTDES VPLAPPQNLT LINCTSDFVW LKWSPSPLPG GIVKVYSFKI HEHETDTIYY KNISGFKTEA KLVGLEPVST YSIRVSAFTK VGNGNQFSNV VKFTTQESVP DVVQNMQCMA TSWQSVLVKW DPPKKANGII TQYMVTVERN STKVSPQDHM YTFIKLLANT SYVFKVRAST SAGEGDESTC HVSTLPETVP SVPTNIAFSD VQSTSATLTW IRPDTILGYF QNYKITTQLR AQKCKEWESE ECVEYQKIQY LYEAHLTEET VYGLKKFRWY RFQVAASTNA GYGNASNWIS TKTLPGPPDG PPENVHVVAT SPFSISISWS EPAVITGPTC YLIDVKSVDN DEFNISFIKS NEENKTIEIK DLEIFTRYSV VITAFTGNIS AAYVEGKSSA EMIVTTLESA PKDPPNNMTF QKIPDEVTKF QLTFLPPSQP NGNIQVYQAL VYREDDPTAV QIHNLSIIQK TNTFVIAMLE GLKGGHTYNI SVYAVNSAGA GPKVPMRITM DIKAPARPKT KPTPIYDATG KLLVTSTTIT IRMPICYYSD DHGPIKNVQV LVTETGAQHD GNVTKWYDAY FNKARPYFTN EGFPNPPCTE GKTKFSGNEE IYIIGADNAC MIPGNEDKIC NGPLKPKKQY LFKFRATNIM GQFTDSDYSD PVKTLGEGLS ERTVEIILSV TLCILSIILL GTAIFAFARI RQKQKEGGTY SPQDAEIIDT KLKLDQLITV ADLELKDERL TRLLSYRKSI KPISKKSFLQ HVEELCTNNN LKFQEEFSEL PKFLQDLSST DADLPWNRAK NRFPNIKPYN NNRVKLIADA SVPGSDYINA SYISGYLCPN EFIATQGPLP GTVGDFWRMV WETRAKTLVM LTQCFEKGRI RCHQYWPEDN KPVTVFGDIV ITKLMEDVQI DWTIRDLKIE RHGDCMTVRQ CNFTAWPEHG VPENSAPLIH FVKLVRASRA HDTTPMIVHC SAGVGRTGVF IALDHLTQHI NDHDFVDIYG LVAELRSERM CMVQNLAQYI FLHQCILDLL SNKGSNQPIC FVNYSALQKM DSLDAMEGDV ELEWEETTM //