Q80YX1 (TENA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 88.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tenascin Short name=TN Alternative name(s): Hexabrachion Tenascin-C Short name=TN-C | ||||
| Gene names |
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| 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 | 2110 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 | Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth when provided to neurons in culture. May play a role in supporting the growth of epithelial tumors. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. Ref.4 UniProtKB P24821 |
| Subunit structure | Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule. Interacts with CSPG4 By similarity. UniProtKB P24821 |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Tissue specificity | High levels of isoform 2 in lung and brain of newborn mice. High levels of isoform 5 in thymus, moderate levels in brain of newborn and adult mice. Low level of isoform 2 in adult brain. Ref.1 |
| Developmental stage | In kidney, isoform 2 is expressed at birth and isoform 5 at 2 weeks of age. In intestine, isoform 5 is expressed in day 13 embryos and isoform 2 at birth. In cerebellum, high levels of isoform 2 in day 17 embryos are down-regulated to moderate levels in newborn mice and undetectable levels in adult mice. Similarly, moderate levels of isoform 2 expressed in cerebrum of day 17 embryos are gradually down-regulated to undetectable levels in adult mice. Ref.1 Ref.2 |
| Post-translational modification | N-glycosylated. Ref.2 |
| Disruption phenotype | Mice show enhanced novelty-induced activity, reduced anxiety, delayed resynchronization to daylight reversal and weaker muscle strength. Ref.4 |
| Sequence similarities | Belongs to the tenascin family. Contains 15 EGF-like domains. Contains 1 fibrinogen C-terminal domain. Contains 14 fibronectin type-III domains. |
Ontologies
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 Ref.3 (identifier: Q80YX1-1) 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 Ref.1 (identifier: Q80YX1-2) The sequence of this isoform differs from the canonical sequence as follows: 1436-1526: Missing. | ||||||
| Isoform 3 Ref.1 (identifier: Q80YX1-3) The sequence of this isoform differs from the canonical sequence as follows: 1254-1616: Missing. | ||||||
| Isoform 4 Ref.1 (identifier: Q80YX1-4) The sequence of this isoform differs from the canonical sequence as follows: 1163-1616: Missing. | ||||||
| Isoform 5 Ref.1 (identifier: Q80YX1-5) The sequence of this isoform differs from the canonical sequence as follows: 1072-1616: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | By similarity UniProtKB P24821 | ||||||||
| Chain | 23 – 2110 | 2088 | Tenascin By similarity UniProtKB P24821 | PRO_0000248607 | |||||||
Regions | |||||||||||
| Domain | 174 – 185 | 12 | EGF-like 1; incomplete | ||||||||
| Domain | 186 – 216 | 31 | EGF-like 2 | ||||||||
| Domain | 217 – 247 | 31 | EGF-like 3 | ||||||||
| Domain | 248 – 279 | 32 | EGF-like 4 | ||||||||
| Domain | 280 – 310 | 31 | EGF-like 5 | ||||||||
| Domain | 311 – 341 | 31 | EGF-like 6 | ||||||||
| Domain | 342 – 372 | 31 | EGF-like 7 | ||||||||
| Domain | 373 – 403 | 31 | EGF-like 8 | ||||||||
| Domain | 404 – 434 | 31 | EGF-like 9 | ||||||||
| Domain | 435 – 465 | 31 | EGF-like 10 | ||||||||
| Domain | 466 – 496 | 31 | EGF-like 11 | ||||||||
| Domain | 497 – 527 | 31 | EGF-like 12 | ||||||||
| Domain | 528 – 558 | 31 | EGF-like 13 | ||||||||
| Domain | 559 – 589 | 31 | EGF-like 14 | ||||||||
| Domain | 590 – 621 | 32 | EGF-like 15 | ||||||||
| Domain | 622 – 710 | 89 | Fibronectin type-III 1 | ||||||||
| Domain | 713 – 801 | 89 | Fibronectin type-III 2 | ||||||||
| Domain | 802 – 891 | 90 | Fibronectin type-III 3 | ||||||||
| Domain | 892 – 983 | 92 | Fibronectin type-III 4 | ||||||||
| Domain | 984 – 1071 | 88 | Fibronectin type-III 5 | ||||||||
| Domain | 1073 – 1164 | 92 | Fibronectin type-III 6 | ||||||||
| Domain | 1166 – 1253 | 88 | Fibronectin type-III 7 | ||||||||
| Domain | 1257 – 1344 | 88 | Fibronectin type-III 8 | ||||||||
| Domain | 1348 – 1435 | 88 | Fibronectin type-III 9 | ||||||||
| Domain | 1437 – 1526 | 90 | Fibronectin type-III 10 | ||||||||
| Domain | 1528 – 1617 | 90 | Fibronectin type-III 11 | ||||||||
| Domain | 1618 – 1706 | 89 | Fibronectin type-III 12 | ||||||||
| Domain | 1707 – 1794 | 88 | Fibronectin type-III 13 | ||||||||
| Domain | 1795 – 1882 | 88 | Fibronectin type-III 14 | ||||||||
| Domain | 1884 – 2099 | 216 | Fibrinogen C-terminal | ||||||||
| Coiled coil | 118 – 142 | 25 | Potential | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 70 | 1 | Phosphoserine Ref.7 | ||||||||
| Modified residue | 72 | 1 | Phosphoserine Ref.6 Ref.7 | ||||||||
| Glycosylation | 38 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 166 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 184 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 327 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 788 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1018 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1079 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1093 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1119 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1184 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1210 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1275 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1301 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1354 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1364 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1394 | 1 | N-linked (GlcNAc...) Ref.5 | ||||||||
| Glycosylation | 1443 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1718 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1969 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2071 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 190 ↔ 200 | By similarity | |||||||||
| Disulfide bond | 194 ↔ 205 | By similarity | |||||||||
| Disulfide bond | 207 ↔ 216 | By similarity | |||||||||
| Disulfide bond | 221 ↔ 231 | By similarity | |||||||||
| Disulfide bond | 225 ↔ 236 | By similarity | |||||||||
| Disulfide bond | 238 ↔ 247 | By similarity | |||||||||
| Disulfide bond | 252 ↔ 263 | By similarity | |||||||||
| Disulfide bond | 256 ↔ 268 | By similarity | |||||||||
| Disulfide bond | 270 ↔ 279 | By similarity | |||||||||
| Disulfide bond | 284 ↔ 294 | By similarity | |||||||||
| Disulfide bond | 288 ↔ 299 | By similarity | |||||||||
| Disulfide bond | 301 ↔ 310 | By similarity | |||||||||
| Disulfide bond | 315 ↔ 325 | By similarity | |||||||||
| Disulfide bond | 319 ↔ 330 | By similarity | |||||||||
| Disulfide bond | 332 ↔ 341 | By similarity | |||||||||
| Disulfide bond | 346 ↔ 356 | By similarity | |||||||||
| Disulfide bond | 350 ↔ 361 | By similarity | |||||||||
| Disulfide bond | 363 ↔ 372 | By similarity | |||||||||
| Disulfide bond | 377 ↔ 387 | By similarity | |||||||||
| Disulfide bond | 381 ↔ 392 | By similarity | |||||||||
| Disulfide bond | 394 ↔ 403 | By similarity | |||||||||
| Disulfide bond | 408 ↔ 418 | By similarity | |||||||||
| Disulfide bond | 412 ↔ 423 | By similarity | |||||||||
| Disulfide bond | 425 ↔ 434 | By similarity | |||||||||
| Disulfide bond | 439 ↔ 449 | By similarity | |||||||||
| Disulfide bond | 443 ↔ 454 | By similarity | |||||||||
| Disulfide bond | 456 ↔ 465 | By similarity | |||||||||
| Disulfide bond | 470 ↔ 480 | By similarity | |||||||||
| Disulfide bond | 474 ↔ 485 | By similarity | |||||||||
| Disulfide bond | 487 ↔ 496 | By similarity | |||||||||
| Disulfide bond | 501 ↔ 511 | By similarity | |||||||||
| Disulfide bond | 505 ↔ 516 | By similarity | |||||||||
| Disulfide bond | 518 ↔ 527 | By similarity | |||||||||
| Disulfide bond | 532 ↔ 542 | By similarity | |||||||||
| Disulfide bond | 536 ↔ 547 | By similarity | |||||||||
| Disulfide bond | 549 ↔ 558 | By similarity | |||||||||
| Disulfide bond | 563 ↔ 573 | By similarity | |||||||||
| Disulfide bond | 567 ↔ 578 | By similarity | |||||||||
| Disulfide bond | 580 ↔ 589 | By similarity | |||||||||
| Disulfide bond | 594 ↔ 604 | By similarity | |||||||||
| Disulfide bond | 598 ↔ 609 | By similarity | |||||||||
| Disulfide bond | 611 ↔ 620 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1072 – 1616 | 545 | Missing in isoform 5. Ref.1 | VSP_052144 | |||||||
| Alternative sequence | 1163 – 1616 | 454 | Missing in isoform 4. Ref.1 | VSP_052145 | |||||||
| Alternative sequence | 1254 – 1616 | 363 | Missing in isoform 3. Ref.1 | VSP_052146 | |||||||
| Alternative sequence | 1436 – 1526 | 91 | Missing in isoform 2. Ref.1 | VSP_052147 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 202 | 1 | D → E in CAA39751. Ref.2 | ||||||||
| Sequence conflict | 318 | 1 | D → S in CAA39751. Ref.2 | ||||||||
| Sequence conflict | 1019 | 1 | Y → S in CAA39751. Ref.2 | ||||||||
| Sequence conflict | 1025 | 1 | Q → H in CAA39751. Ref.2 | ||||||||
| Sequence conflict | 1306 | 1 | G → S in CAA39751. Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Murine tenascin: cDNA cloning, structure and temporal expression of isoforms." Saga Y., Tsukamoto T., Jing N., Kusakabe M., Sakakura T. Gene 104:177-185(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: GRS. Tissue: Mammary tumor. |
| [2] | "Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis." Weller A., Beck S., Ekblom P. J. Cell Biol. 112:355-362(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), DEVELOPMENTAL STAGE, GLYCOSYLATION. Strain: NMRI X 129. Tissue: Embryo. |
| [3] | "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. |
| [4] | "Enhanced novelty-induced activity, reduced anxiety, delayed resynchronization to daylight reversal and weaker muscle strength in tenascin-C-deficient mice." Morellini F., Schachner M. Eur. J. Neurosci. 23:1255-1268(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. |
| [5] | "Proteome-wide characterization of N-glycosylation events by diagonal chromatography." Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K. J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1394, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma. |
| [6] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [7] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-72, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D90343 mRNA. Translation: BAA14355.1. X56304 mRNA. Translation: CAA39751.1. AL732556 Genomic DNA. Translation: CAD83047.1. AL732556 Genomic DNA. Translation: CAD83048.1. |
| IPI | IPI00403938. IPI00420656. IPI00785310. IPI00785346. IPI00785360. |
| PIR | JQ1322. |
| RefSeq | NP_035737.2. NM_011607.3. |
| UniGene | Mm.454219. Mm.980. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TEN based on UniProtKB P24821. |
| ProteinModelPortal | Q80YX1. |
| SMR | Q80YX1. Positions 116-143, 158-2098. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q80YX1. |
Proteomic databases | |
| PaxDb | Q80YX1. |
| PRIDE | Q80YX1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000030056; ENSMUSP00000030056; ENSMUSG00000028364. ENSMUST00000107372; ENSMUSP00000102995; ENSMUSG00000028364. ENSMUST00000107377; ENSMUSP00000103000; ENSMUSG00000028364. |
| GeneID | 21923. |
| KEGG | mmu:21923. |
| UCSC | uc008thg.2. mouse. |
Organism-specific databases | |
| CTD | 3371. |
| MGI | MGI:101922. Tnc. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00690000102056. |
| HOGENOM | HOG000234355. |
| HOVERGEN | HBG008949. |
| InParanoid | Q80YX1. |
| KO | K06252. |
| OMA | GQRSCPN. |
| OrthoDB | EOG4MSCX9. |
Gene expression databases | |
| ArrayExpress | Q80YX1. |
| Bgee | Q80YX1. |
| CleanEx | MM_TNC. |
| Genevestigator | Q80YX1. |
| GermOnline | ENSMUSG00000028364. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 14 hits. 3.90.215.10. 1 hit. 4.10.530.10. 1 hit. |
| InterPro | IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR013111. EGF_extracell. IPR014716. Fibrinogen_a/b/g_C_1. IPR014715. Fibrinogen_a/b/g_C_2. IPR002181. Fibrinogen_a/b/g_C_dom. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. [Graphical view] |
| Pfam | PF07974. EGF_2. 7 hits. PF00147. Fibrinogen_C. 1 hit. PF00041. fn3. 14 hits. PF12661. hEGF. 2 hits. [Graphical view] |
| SMART | SM00181. EGF. 12 hits. SM00186. FBG. 1 hit. SM00060. FN3. 14 hits. [Graphical view] |
| SUPFAM | SSF56496. Fibrinogen_a/b/g_C. 1 hit. SSF49265. FN_III-like. 14 hits. |
| PROSITE | PS00022. EGF_1. 15 hits. PS01186. EGF_2. 14 hits. PS50026. EGF_3. 5 hits. PS00514. FIBRINOGEN_C_1. False negative. PS51406. FIBRINOGEN_C_2. 1 hit. PS50853. FN3. 14 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 301496. |
| SOURCE | Search... |
Entry information
| Entry name | TENA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q80YX1 Secondary accession number(s): Q64706, Q80YX2 | ||||||||
| Entry history |
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| 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
