P0C5E4 (PTPRQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 50.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 2300 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 By similarity. Ref.2 |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
| Subcellular location | Membrane; Single-pass type I membrane protein By similarity. |
| Tissue specificity | In the inner ear of the early postnatal mouse, it is present in hair bundles in the cochlea and in the vestibule. Restricted to the hair bundles and not detected in any other cell type within the inner ear. Restricted to the basal region of the hair bundle (at protein level). Ref.2 |
| Disruption phenotype | Mice show rapid postnatal deterioration in cochlear hair-bundle structure, associated with smaller than normal transducer currents with otherwise normal adaptation properties, a progressive loss of basal-coil cochlear hair cells, and deafness. Ref.2 |
| Sequence similarities | Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. Contains 17 fibronectin type-III domains. Contains 1 tyrosine-protein phosphatase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Disease | 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 mutant phenotype Ref.2. Source: MGI peptidyl-tyrosine dephosphorylationInferred from electronic annotation. Source: GOC regulation of fat cell differentiationInferred from sequence or structural similarity. 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 – 17 | 17 | Potential | ||||||
| Chain | 18 – 2300 | 2283 | Phosphatidylinositol phosphatase PTPRQ | PRO_0000302851 | |||||
Regions | |||||||||
| Topological domain | 18 – 1906 | 1889 | Extracellular Potential | ||||||
| Transmembrane | 1907 – 1927 | 21 | Helical; Potential | ||||||
| Topological domain | 1928 – 2300 | 373 | Cytoplasmic Potential | ||||||
| Domain | 57 – 151 | 95 | Fibronectin type-III 1 | ||||||
| Domain | 156 – 237 | 82 | Fibronectin type-III 2 | ||||||
| Domain | 306 – 393 | 88 | Fibronectin type-III 3 | ||||||
| Domain | 398 – 489 | 92 | Fibronectin type-III 4 | ||||||
| Domain | 497 – 564 | 68 | Fibronectin type-III 5 | ||||||
| Domain | 565 – 658 | 94 | Fibronectin type-III 6 | ||||||
| Domain | 665 – 754 | 90 | Fibronectin type-III 7 | ||||||
| Domain | 759 – 849 | 91 | Fibronectin type-III 8 | ||||||
| Domain | 854 – 943 | 90 | Fibronectin type-III 9 | ||||||
| Domain | 948 – 1046 | 99 | Fibronectin type-III 10 | ||||||
| Domain | 1053 – 1146 | 94 | Fibronectin type-III 11 | ||||||
| Domain | 1151 – 1238 | 88 | Fibronectin type-III 12 | ||||||
| Domain | 1243 – 1336 | 94 | Fibronectin type-III 13 | ||||||
| Domain | 1341 – 1425 | 85 | Fibronectin type-III 14 | ||||||
| Domain | 1431 – 1534 | 104 | Fibronectin type-III 15 | ||||||
| Domain | 1539 – 1637 | 99 | Fibronectin type-III 16 | ||||||
| Domain | 1642 – 1741 | 100 | Fibronectin type-III 17 | ||||||
| Domain | 2004 – 2260 | 257 | Tyrosine-protein phosphatase | ||||||
Sites | |||||||||
| Active site | 2201 | 1 | Phosphocysteine intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 53 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 161 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 168 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 317 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 353 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 388 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 718 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 731 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 744 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 996 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1008 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1038 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1059 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1249 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1254 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1803 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "A receptor-like inositol lipid phosphatase is required for the maturation of developing cochlear hair bundles." Goodyear R.J., Legan P.K., Wright M.B., Marcotti W., Oganesian A., Coats S.A., Booth C.J., Kros C.J., Seifert R.A., Bowen-Pope D.F., Richardson G.P. J. Neurosci. 23:9208-9219(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC021642 Genomic DNA. No translation available. AC123948 Genomic DNA. No translation available. AC155168 Genomic DNA. No translation available. |
| IPI | IPI00674433. |
| RefSeq | NP_001074901.1. NM_001081432.1. |
| UniGene | Mm.391418. |
3D structure databases | |
| ProteinModelPortal | P0C5E4. |
| SMR | P0C5E4. Positions 55-191, 268-296, 358-436, 512-1417, 1497-1576, 1659-1735, 1992-2296. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000058572. |
PTM databases | |
| PhosphoSite | P0C5E4. |
Proteomic databases | |
| PRIDE | P0C5E4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000050702; ENSMUSP00000058572; ENSMUSG00000035916. |
| GeneID | 237523. |
| KEGG | mmu:237523. |
| UCSC | uc007gzb.1. mouse. |
Organism-specific databases | |
| CTD | 374462. |
| MGI | MGI:1096349. Ptprq. |
Phylogenomic databases | |
| eggNOG | COG5599. |
| GeneTree | ENSGT00700000104166. |
| HOGENOM | HOG000115793. |
| HOVERGEN | HBG108308. |
| InParanoid | P0C5E4. |
| OMA | DVELEWE. |
| OrthoDB | EOG4P2Q3H. |
Gene expression databases | |
| Bgee | P0C5E4. |
| CleanEx | MM_PTPRQ. |
| Genevestigator | P0C5E4. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 18 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. 16 hits. SM00194. PTPc. 1 hit. [Graphical view] |
| SUPFAM | SSF49265. FN_III-like. 16 hits. |
| PROSITE | PS50853. FN3. 17 hits. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 383394. |
| SOURCE | Search... |
Entry information
| Entry name | PTPRQ_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P0C5E4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
