PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ

PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ » Receptor-type tyrosine-protein phosphatase Q;PTP-RQ; R-PTP-Q;
Hydrophobic Thickness 39.2 ± 4.6 Å
Tilt Angle 12 ± 9°
ΔGtransfer -28.3 kcal/mol
ΔGfold -21.3 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1945-1970 (1943-1978)
Pathways none
PDB 4ikc (A=2015-2293)
OPM none
Complexes none
Interactions

CADH2, Complex: PTPRQ:CADH2, PubMed

Domains

AA: 9-88, PDBID: 1TDQ, Subunit A, Seq Identity:31%, Fibronectin type III domain

AA: 99-185, PDBID: 2EDY, Subunit A, Seq Identity:35%, Fibronectin type III domain

AA: 612-693, PDBID: 1X5G, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 709-787, PDBID: 2EDY, Subunit A, Seq Identity:34%, Fibronectin type III domain

AA: 803-884, PDBID: 2EDY, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 898-977, PDBID: 2EDY, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 992-1082, PDBID: 2DLH, Subunit A, Seq Identity:31%, Fibronectin type III domain

AA: 1195-1273, PDBID: 2EDY, Subunit A, Seq Identity:37%, Fibronectin type III domain

AA: 1286-1370, PDBID: 4O00, Subunit B, Seq Identity:31%, Fibronectin type III domain

AA: 1383-1460, PDBID: 4BK4, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 1473-1568, PDBID: 2ED9, Subunit A, Seq Identity:28%, Fibronectin type III domain

AA: 1582-1663, PDBID: 2ED8, Subunit A, Seq Identity:30%, Fibronectin type III domain

AA: 1685-1775, PDBID: 1X5L, Subunit A, Seq Identity:28%, Fibronectin type III domain

AA: 2060-2291, PDBID: 4IKC, Subunit A, Seq Identity:100%, Protein-tyrosine phosphatase

UniProt annotation for PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ
FUNCTION: Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells.

CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

TISSUE SPECIFICITY: In developing kidney, it localizes to the basal membrane of podocytes, beginning when podocyte progenitors can first be identified in the embryonic kidney (at protein level). Expressed in lung and kidney.

DEVELOPMENTAL STAGE: Expressed at highest levels in fetal kidney, followed by fetal lung and fetal cochlea.

INDUCTION: Down-regulated during adipogenesis of mesenchymal stem cells.

DISEASE: Deafness, autosomal recessive, 84A (DFNB84A) OMIM: A form of non-syndromic deafness characterized by progressive, sensorineural hearing loss and vestibular dysfunction. mutations affecting the gene represented in this entry.

UniProt features for PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ
SIGNAL 1 35 Potential.
CHAIN 36 2332 Phosphatidylinositol phosphatase PTPRQ.
DOMAIN 36 93 Fibronectin type-III 1.
DOMAIN 98 192 Fibronectin type-III 2.
DOMAIN 197 289 Fibronectin type-III 3.
DOMAIN 347 434 Fibronectin type-III 4.
DOMAIN 439 531 Fibronectin type-III 5.
DOMAIN 514 606 Fibronectin type-III 6.
DOMAIN 607 700 Fibronectin type-III 7.
DOMAIN 707 796 Fibronectin type-III 8.
DOMAIN 801 891 Fibronectin type-III 9.
DOMAIN 896 985 Fibronectin type-III 10.
DOMAIN 990 1088 Fibronectin type-III 11.
DOMAIN 1095 1187 Fibronectin type-III 12.
DOMAIN 1192 1279 Fibronectin type-III 13.
DOMAIN 1284 1377 Fibronectin type-III 14.
DOMAIN 1382 1466 Fibronectin type-III 15.
DOMAIN 1472 1575 Fibronectin type-III 16.
DOMAIN 1580 1678 Fibronectin type-III 17.
DOMAIN 1683 1782 Fibronectin type-III 18.
DOMAIN 2036 2292 Tyrosine-protein phosphatase.
ACT_SITE 2233 2233 Phosphocysteine intermediate (By similarity).
Amino Acid Sequence for PTPRQ_HUMAN » Phosphatidylinositol phosphatase PTPRQ
MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT IRDLGGGEYQ VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP PVFLAGERVG SAGILLSWNT PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR SKPDSLEVLL TNLNPGTTYE IKVAAENSAG IGVFSDPFLF QTAESAPGKV VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG IVVKDVSIRV EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP PQNCVTGNIT GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK FAFTNLTPFT MYDVYIAAET SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV ESTQVRITWK KPRQPNGIIN QYRVKVLVPE TGIILENTLL TGNNEYINDP MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK NFPARNRAED QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME LDTNRAFQIT TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV RTSEDEPESS PQDVEVIDVT ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT LYMKNTSTTD IILRNLRPHT LYNISVRSYT RFGHGNQVSS LLSVRTSETV PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK RSNGNEERTI NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL ELSDLDYNVE YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA NLSSSSIILF WTPPSKPNGI IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN MTVSTIIDKL TIFSYYTFWL TASTSVGNGN KSSDIIEVYT DQDIPEGFVG NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH VRPPLVTYER SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE LSPFTLYSFF AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF VWLKWSPSPL PGGIVKVYSF KIHEHETDTI YYKNISGFKT EAKLVGLEPV STYSIRVSAF TKVGNGNQFS NVVKFTTQES VPDVVQNMQC MATSWQSVLV KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA NTSYVFKVRA STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR WYRFQVAAST NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS WSEPAVITGP TCYLIDVKSV DNDEFNISFI KSNEENKTIE IKDLEIFTRY SVVITAFTGN ISAAYVEGKS SAEMIVTTLE SAPKDPPNNM TFQKIPDEVT KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII QKTNTFVIAM LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD AYFNKARPYF TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK ICNGPLKPKK QYLFKFRATN IMGQFTDSDY SDPVKTLGEG LSERTVEIIL SVTLCILSII LLGTAIFAFA RIRQKQKEGG TYSPQDAEII DTKLKLDQLI TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF SELPKFLQDL SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP EHGVPENSAP LIHFVKLVRA SRAHDTTPMI VHCSAGVGRT GVFIALDHLT QHINDHDFVD IYGLVAELRS ERMCMVQNLA QYIFLHQCIL DLLSNKGSNQ PICFVNYSAL QKMDSLDAME GDVELEWEET TM