Q9UMZ3 (PTPRQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol phosphatase PTPRQ
EC=3.1.3.-

Alternative name(s):
Receptor-type tyrosine-protein phosphatase Q
Short name=PTP-RQ
Short name=R-PTP-Q
EC=3.1.3.48

Gene names

Name:

PTPRQ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.4
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Membrane; Single-pass type I membrane protein Ref.3.
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. Ref.3 Ref.5
Developmental stage	Expressed at highest levels in fetal kidney, followed by fetal lung and fetal cochlea. Ref.5
Induction	Down-regulated during adipogenesis of mesenchymal stem cells. Ref.4
Involvement in disease	Deafness, autosomal recessive, 84A (DFNB84A) [MIM:613391]: A form of non-syndromic deafness characterized by progressive, sensorineural hearing loss and vestibular dysfunction. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. Contains 18 fibronectin type-III domains. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation Non-syndromic deafness
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inner ear morphogenesis Inferred from electronic annotation. Source: Compara peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of fat cell differentiation Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 2332	2297	Phosphatidylinositol phosphatase PTPRQ		PRO_0000302850
Regions
	Topological domain	36 – 1947	1912	Extracellular Potential
	Transmembrane	1948 – 1968	21	Helical; Potential
	Topological domain	1969 – 2332	364	Cytoplasmic Potential
	Domain	36 – 93	58	Fibronectin type-III 1
	Domain	98 – 192	95	Fibronectin type-III 2
	Domain	197 – 289	93	Fibronectin type-III 3
	Domain	347 – 434	88	Fibronectin type-III 4
	Domain	439 – 531	93	Fibronectin type-III 5
	Domain	514 – 606	93	Fibronectin type-III 6
	Domain	607 – 700	94	Fibronectin type-III 7
	Domain	707 – 796	90	Fibronectin type-III 8
	Domain	801 – 891	91	Fibronectin type-III 9
	Domain	896 – 985	90	Fibronectin type-III 10
	Domain	990 – 1088	99	Fibronectin type-III 11
	Domain	1095 – 1187	93	Fibronectin type-III 12
	Domain	1192 – 1279	88	Fibronectin type-III 13
	Domain	1284 – 1377	94	Fibronectin type-III 14
	Domain	1382 – 1466	85	Fibronectin type-III 15
	Domain	1472 – 1575	104	Fibronectin type-III 16
	Domain	1580 – 1678	99	Fibronectin type-III 17
	Domain	1683 – 1782	100	Fibronectin type-III 18
	Domain	2036 – 2292	257	Tyrosine-protein phosphatase
Sites
	Active site	2233	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Glycosylation	18	1	N-linked (GlcNAc...) Potential
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	202	1	N-linked (GlcNAc...) Potential
	Glycosylation	394	1	N-linked (GlcNAc...) Potential
	Glycosylation	944	1	N-linked (GlcNAc...) Potential
	Glycosylation	1038	1	N-linked (GlcNAc...) Potential
	Glycosylation	1080	1	N-linked (GlcNAc...) Potential
	Glycosylation	1101	1	N-linked (GlcNAc...) Potential
	Glycosylation	1290	1	N-linked (GlcNAc...) Potential
	Glycosylation	1295	1	N-linked (GlcNAc...) Potential
	Glycosylation	1844	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	281	1	R → G in DFNB84A. Ref.5		VAR_063526
	Natural variant	471	1	Q → E. Ref.6 Corresponds to variant rs61729287 [ dbSNP | Ensembl ].		VAR_069041
	Natural variant	1040	1	T → I. Corresponds to variant rs12316867 [ dbSNP | Ensembl ].		VAR_034970
	Natural variant	1098	1	F → L. Corresponds to variant rs6539524 [ dbSNP | Ensembl ].		VAR_034971
	Natural variant	1120	1	A → P. Corresponds to variant rs7975340 [ dbSNP | Ensembl ].		VAR_034972
	Natural variant	1244	1	N → D. Corresponds to variant rs17713202 [ dbSNP | Ensembl ].		VAR_034973
	Natural variant	1734	1	I → T. Corresponds to variant rs7963963 [ dbSNP | Ensembl ].		VAR_034974
	Natural variant	2121	1	R → K. Corresponds to variant rs1163042 [ dbSNP | Ensembl ].		VAR_034975

Sequences

	Sequence		Length	Mass (Da)
	Q9UMZ3 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 999D87AA00BA04C2	FASTA	2,332	260,924
	10 20 30 40 50 60 MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT IRDLGGGEYQ 70 80 90 100 110 120 VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP PVFLAGERVG SAGILLSWNT 130 140 150 160 170 180 PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR SKPDSLEVLL TNLNPGTTYE IKVAAENSAG 190 200 210 220 230 240 IGVFSDPFLF QTAESAPGKV VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG 250 260 270 280 290 300 IVVKDVSIRV EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI 310 320 330 340 350 360 SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP PQNCVTGNIT 370 380 390 400 410 420 GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK FAFTNLTPFT MYDVYIAAET 430 440 450 460 470 480 SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV ESTQVRITWK KPRQPNGIIN QYRVKVLVPE 490 500 510 520 530 540 TGIILENTLL TGNNEYINDP MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK 550 560 570 580 590 600 NFPARNRAED QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT 610 620 630 640 650 660 VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME LDTNRAFQIT 670 680 690 700 710 720 TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV RTSEDEPESS PQDVEVIDVT 730 740 750 760 770 780 ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT LYMKNTSTTD IILRNLRPHT LYNISVRSYT 790 800 810 820 830 840 RFGHGNQVSS LLSVRTSETV PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK 850 860 870 880 890 900 RSNGNEERTI NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP 910 920 930 940 950 960 QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL ELSDLDYNVE 970 980 990 1000 1010 1020 YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA NLSSSSIILF WTPPSKPNGI 1030 1040 1050 1060 1070 1080 IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN MTVSTIIDKL TIFSYYTFWL TASTSVGNGN 1090 1100 1110 1120 1130 1140 KSSDIIEVYT DQDIPEGFVG NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH 1150 1160 1170 1180 1190 1200 VRPPLVTYER SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT 1210 1220 1230 1240 1250 1260 FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE LSPFTLYSFF 1270 1280 1290 1300 1310 1320 AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF VWLKWSPSPL PGGIVKVYSF 1330 1340 1350 1360 1370 1380 KIHEHETDTI YYKNISGFKT EAKLVGLEPV STYSIRVSAF TKVGNGNQFS NVVKFTTQES 1390 1400 1410 1420 1430 1440 VPDVVQNMQC MATSWQSVLV KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA 1450 1460 1470 1480 1490 1500 NTSYVFKVRA STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG 1510 1520 1530 1540 1550 1560 YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR WYRFQVAAST 1570 1580 1590 1600 1610 1620 NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS WSEPAVITGP TCYLIDVKSV 1630 1640 1650 1660 1670 1680 DNDEFNISFI KSNEENKTIE IKDLEIFTRY SVVITAFTGN ISAAYVEGKS SAEMIVTTLE 1690 1700 1710 1720 1730 1740 SAPKDPPNNM TFQKIPDEVT KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII 1750 1760 1770 1780 1790 1800 QKTNTFVIAM LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA 1810 1820 1830 1840 1850 1860 TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD AYFNKARPYF 1870 1880 1890 1900 1910 1920 TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK ICNGPLKPKK QYLFKFRATN 1930 1940 1950 1960 1970 1980 IMGQFTDSDY SDPVKTLGEG LSERTVEIIL SVTLCILSII LLGTAIFAFA RIRQKQKEGG 1990 2000 2010 2020 2030 2040 TYSPQDAEII DTKLKLDQLI TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF 2050 2060 2070 2080 2090 2100 SELPKFLQDL SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL 2110 2120 2130 2140 2150 2160 CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG 2170 2180 2190 2200 2210 2220 DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP EHGVPENSAP LIHFVKLVRA 2230 2240 2250 2260 2270 2280 SRAHDTTPMI VHCSAGVGRT GVFIALDHLT QHINDHDFVD IYGLVAELRS ERMCMVQNLA 2290 2300 2310 2320 2330 QYIFLHQCIL DLLSNKGSNQ PICFVNYSAL QKMDSLDAME GDVELEWEET TM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Differential expression of PTPase RNAs resulting from K562 differentiation induced by PMA." Dayton M.A., Blanchard K.L. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2133-2266.
[3]	"PTPRQ is a novel phosphatidylinositol phosphatase that can be expressed as a cytoplasmic protein or as a subcellularly localized receptor-like protein." Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M., Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F. Exp. Cell Res. 287:374-386(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"Involvement of PTP-RQ in differentiation during adipogenesis of human mesenchymal stem cells." Jung H., Kim W.K., Kim do H., Cho Y.S., Kim S.J., Park S.G., Park B.C., Lim H.M., Bae K.H., Lee S.C. Biochem. Biophys. Res. Commun. 383:252-257(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[5]	"Mutations in PTPRQ are a cause of autosomal-recessive nonsyndromic hearing impairment DFNB84 and associated with vestibular dysfunction." Schraders M., Oostrik J., Huygen P.L., Strom T.M., van Wijk E., Kunst H.P., Hoefsloot L.H., Cremers C.W., Admiraal R.J., Kremer H. Am. J. Hum. Genet. 86:604-610(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT DFNB84A GLY-281.
[6]	"Nonsense mutation of the stereociliar membrane protein gene PTPRQ in human hearing loss DFNB84." Shahin H., Rahil M., Abu Rayan A., Avraham K.B., King M.C., Kanaan M., Walsh T. J. Med. Genet. 47:643-645(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DFNB84A, VARIANT GLU-471.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC083812 Genomic DNA. No translation available. AC074031 Genomic DNA. No translation available. AF169351 mRNA. Translation: AAD50277.1.
IPI	IPI00741536.
UniGene	Hs.539284.
3D structure databases
ProteinModelPortal	Q9UMZ3.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000393751.
PTM databases
PhosphoSite	Q9UMZ3.
Polymorphism databases
DMDM	158563998.
Proteomic databases
PaxDb	Q9UMZ3.
PRIDE	Q9UMZ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266688; ENSP00000266688; ENSG00000139304.
UCSC	uc001sze.2. human.
Organism-specific databases
GeneCards	GC12P080837.
H-InvDB	HIX0201920.
HGNC	HGNC:9679. PTPRQ.
HPA	HPA053245.
MIM	603317. gene. 613391. phenotype.
neXtProt	NX_Q9UMZ3.
Orphanet	90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5599.
HOGENOM	HOG000115793.
HOVERGEN	HBG108308.
InParanoid	Q9UMZ3.
Gene expression databases
ArrayExpress	Q9UMZ3.
Bgee	Q9UMZ3.
CleanEx	HS_PTPRQ.
Genevestigator	Q9UMZ3.
Family and domain databases
Gene3D	2.60.40.10. 19 hits.
InterPro	IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00041. fn3. 14 hits. PF00102. Y_phosphatase. 1 hit. [Graphical view]
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00060. FN3. 17 hits. SM00194. PTPc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 17 hits.
PROSITE	PS50853. FN3. 18 hits. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

PTPRQ_HUMAN

Accession

Primary (citable) accession number: Q9UMZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	May 29, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.