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UniProtKB/Swiss-Prot O08523 (TECTA_MOUSE)
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June 16, 2009.
Version 76.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Alpha-tectorin | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 2155 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 | One of the major non-collagenous components of the tectorial membrane By similarity. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. |
| Subunit structure | May form homomeric filament after self-association or heteromeric filament after association with beta-tectorin. Ref.1 |
| Subcellular location | Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side Probable. Secreted › extracellular space › extracellular matrix. Note: Found in the non-collagenous matrix of the tectorial membrane. |
| Tissue specificity | Cochlea-specific. Ref.1 |
| Domain | Zona pellucida domain may enable to form filaments. |
| Post-translational modification | 3 products of tectorin seem to exist: HMM, MMM and LMM. They may be generated by active processing or the result of proteolysis occurring between intrachain disulfide bonds. The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment. |
| Sequence similarities | Contains 1 NIDO domain. Contains 3 TIL (trypsin inhibitory-like) domains. Contains 1 VWFC domain. Contains 4 VWFD domains. Contains 1 ZP domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hearing |
| Cellular component | Cell membrane Extracellular matrix Membrane Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Signal |
| PTM | Disulfide bond GPI-anchor Glycoprotein Lipoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell-matrix adhesion Inferred from electronic annotation. Source: InterPro sensory perception of soundTraceable author statement. Source: MGI |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular spaceInferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Ref.1Inferred from direct assay. Source: MGI |
| Molecular function | extracellular matrix structural constituent Ref.1 Inferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O08523-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O08523-2) The sequence of this isoform differs from the canonical sequence as follows: 1659-1663: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Ref.1 | ||||||
| Chain | 25 – 2091 | 2067 | Alpha-tectorin | PRO_0000041737 | |||||
| Propeptide | 2092 – 2155 | 64 | Removed in mature form Potential | PRO_0000041738 | |||||
Regions | |||||||||
| Domain | 98 – 252 | 155 | NIDO | ||||||
| Domain | 260 – 314 | 55 | VWFC | ||||||
| Domain | 321 – 540 | 220 | VWFD 1 | ||||||
| Domain | 597 – 650 | 54 | TIL 1 | ||||||
| Domain | 712 – 929 | 218 | VWFD 2 | ||||||
| Domain | 984 – 1036 | 53 | TIL 2 | ||||||
| Domain | 1099 – 1317 | 219 | VWFD 3 | ||||||
| Domain | 1372 – 1425 | 54 | TIL 3 | ||||||
| Domain | 1486 – 1694 | 209 | VWFD 4 | ||||||
| Domain | 1805 – 2059 | 255 | ZP | ||||||
Amino acid modifications | |||||||||
| Lipidation | 2091 | 1 | GPI-anchor amidated asparagine Potential | ||||||
| Glycosylation | 34 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 187 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 215 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 278 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 455 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 506 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 528 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 560 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 670 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 687 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 813 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 843 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 855 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 898 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 920 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 931 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 949 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1048 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1064 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1235 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1364 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1538 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1565 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1756 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1772 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1794 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1851 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1864 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1880 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1920 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1939 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 1659 – 1663 | 5 | Missing in isoform 2. | VSP_010557 | |||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | "The mouse tectorins. Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system." Legan P.K., Rau A., Keene J.N., Richardson G.P. J. Biol. Chem. 272:8791-8801(1997) [PubMed: 9079715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 25-34, SUBUNIT, SUBCELLULAR LOCATION, POST-TRANSLATIONAL MODIFICATIONS, TISSUE SPECIFICITY. Strain: CD-1. Tissue: Cochlea. |
| [2] | "Mutations in the human alpha-tectorin gene cause autosomal dominant non-syndromic hearing impairment." Verhoeven K., Van Laer L., Kirschhofer K., Legan P.K., Hughes D.C., Schatteman I., Verstreken M., Van Hauwe P., Coucke P., Chen A., Smith R.J.H., Somers T., Offeciers F.E., Van de Heyning P., Richardson G.P., Wachtler F., Kimberling W.J., Willems P.J., Govaerts P.J., Van Camp G. Nat. Genet. 19:60-62(1998) [PubMed: 9590290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X99805 mRNA. Translation: CAA68138.1. | |
| IPI | IPI00114338. IPI00415299. |
| PIR | T30197. |
| RefSeq | NP_033373.1. |
| UniGene | Mm.42209 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CCV based on UniProtKB P56682. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUSG00000037705. Mus musculus. [Contig view] |
| GeneID | 21683. |
| KEGG | mmu:21683. |
Organism-specific databases | |
| MGI | MGI:109575. Tecta. |
Phylogenomic databases | |
| HOGENOM | O08523. |
| HOVERGEN | O08523. |
Gene expression databases | |
| ArrayExpress | O08523. |
| Bgee | O08523. |
| CleanEx | MM_TECTA. |
| GermOnline | ENSMUSG00000037705. Mus musculus. |
Family and domain databases | |
| InterPro | IPR014853. Conserved-cysteine-rich_domain. IPR006210. EGF-like. IPR001507. Endoglin/CD105. IPR017977. Endoglin/CD105_CS. IPR003886. NIDO. IPR018453. Prot_Inh_CR_TIL_sg. IPR001846. von_Willebrand_fac_D. IPR006552. VWC_out. IPR001007. VWF_C. [Graphical view] |
| Pfam | PF08742. C8. 4 hits. PF06119. NIDO. 1 hit. PF01826. TIL. 3 hits. PF00094. VWD. 4 hits. PF00100. Zona_pellucida. 1 hit. [Graphical view] |
| SMART | SM00181. EGF. 1 hit. SM00539. NIDO. 1 hit. SM00214. VWC. 1 hit. SM00215. VWC_out. 1 hit. SM00216. VWD. 4 hits. SM00241. ZP. 1 hit. [Graphical view] |
| PROSITE | PS51220. NIDO. 1 hit. PS50184. VWFC_2. False negative. PS51233. VWFD. 4 hits. PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 300996. |
| SOURCE | Search... |
Entry information
| Entry name | TECTA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O08523 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |
