Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q80YX1 (TENA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tenascin

Short name=TN
Alternative name(s):
Hexabrachion
Tenascin-C
Short name=TN-C
Gene names
Name:Tnc
Synonyms:Hxb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2110 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbud outgrowth involved in lung branching

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to prostaglandin D stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin D

Inferred from electronic annotation. Source: Ensembl

mesenchymal-epithelial cell signaling involved in prostate gland development

Inferred from mutant phenotype PubMed 18950615. Source: MGI

negative regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from mutant phenotype PubMed 9593587. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system axon regeneration

Inferred from mutant phenotype PubMed 16262655. Source: MGI

positive regulation of cell proliferation

Inferred from direct assay PubMed 19690384. Source: MGI

positive regulation of gene expression

Inferred from direct assay PubMed 19690384. Source: MGI

prostate gland epithelium morphogenesis

Inferred from mutant phenotype PubMed 18950615. Source: MGI

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to fibroblast growth factor

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 18950615PubMed 7687262PubMed 9013311. Source: MGI

extracellular region

Inferred from direct assay PubMed 8856503. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

interstitial matrix

Inferred from direct assay PubMed 11767049. Source: MGI

   Molecular_functionsyndecan binding

Inferred from sequence orthology PubMed 8769660. Source: MGI

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity UniProtKB P24821
Chain23 – 21102088Tenascin By similarity UniProtKB P24821
PRO_0000248607

Regions

Domain174 – 18512EGF-like 1; incomplete
Domain186 – 21631EGF-like 2
Domain217 – 24731EGF-like 3
Domain248 – 27932EGF-like 4
Domain280 – 31031EGF-like 5
Domain311 – 34131EGF-like 6
Domain342 – 37231EGF-like 7
Domain373 – 40331EGF-like 8
Domain404 – 43431EGF-like 9
Domain435 – 46531EGF-like 10
Domain466 – 49631EGF-like 11
Domain497 – 52731EGF-like 12
Domain528 – 55831EGF-like 13
Domain559 – 58931EGF-like 14
Domain590 – 62132EGF-like 15
Domain625 – 71591Fibronectin type-III 1
Domain716 – 80489Fibronectin type-III 2
Domain805 – 89490Fibronectin type-III 3
Domain895 – 98894Fibronectin type-III 4
Domain989 – 107789Fibronectin type-III 5
Domain1078 – 116588Fibronectin type-III 6
Domain1167 – 125993Fibronectin type-III 7
Domain1260 – 134889Fibronectin type-III 8
Domain1349 – 144092Fibronectin type-III 9
Domain1442 – 153089Fibronectin type-III 10
Domain1531 – 162090Fibronectin type-III 11
Domain1621 – 171090Fibronectin type-III 12
Domain1711 – 179787Fibronectin type-III 13
Domain1798 – 188689Fibronectin type-III 14
Domain1884 – 2099216Fibrinogen C-terminal
Coiled coil118 – 14225 Potential

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation7881N-linked (GlcNAc...) Potential
Glycosylation10181N-linked (GlcNAc...) Potential
Glycosylation10791N-linked (GlcNAc...) Potential
Glycosylation10931N-linked (GlcNAc...) Potential
Glycosylation11191N-linked (GlcNAc...) Potential
Glycosylation11841N-linked (GlcNAc...) Potential
Glycosylation12101N-linked (GlcNAc...) Potential
Glycosylation12751N-linked (GlcNAc...) Potential
Glycosylation13011N-linked (GlcNAc...) Potential
Glycosylation13541N-linked (GlcNAc...) Potential
Glycosylation13641N-linked (GlcNAc...) Potential
Glycosylation13941N-linked (GlcNAc...) Ref.5
Glycosylation14431N-linked (GlcNAc...) Potential
Glycosylation17181N-linked (GlcNAc...) Potential
Glycosylation19691N-linked (GlcNAc...) Potential
Glycosylation20711N-linked (GlcNAc...) Potential
Disulfide bond190 ↔ 200 By similarity
Disulfide bond194 ↔ 205 By similarity
Disulfide bond207 ↔ 216 By similarity
Disulfide bond221 ↔ 231 By similarity
Disulfide bond225 ↔ 236 By similarity
Disulfide bond238 ↔ 247 By similarity
Disulfide bond252 ↔ 263 By similarity
Disulfide bond256 ↔ 268 By similarity
Disulfide bond270 ↔ 279 By similarity
Disulfide bond284 ↔ 294 By similarity
Disulfide bond288 ↔ 299 By similarity
Disulfide bond301 ↔ 310 By similarity
Disulfide bond315 ↔ 325 By similarity
Disulfide bond319 ↔ 330 By similarity
Disulfide bond332 ↔ 341 By similarity
Disulfide bond346 ↔ 356 By similarity
Disulfide bond350 ↔ 361 By similarity
Disulfide bond363 ↔ 372 By similarity
Disulfide bond377 ↔ 387 By similarity
Disulfide bond381 ↔ 392 By similarity
Disulfide bond394 ↔ 403 By similarity
Disulfide bond408 ↔ 418 By similarity
Disulfide bond412 ↔ 423 By similarity
Disulfide bond425 ↔ 434 By similarity
Disulfide bond439 ↔ 449 By similarity
Disulfide bond443 ↔ 454 By similarity
Disulfide bond456 ↔ 465 By similarity
Disulfide bond470 ↔ 480 By similarity
Disulfide bond474 ↔ 485 By similarity
Disulfide bond487 ↔ 496 By similarity
Disulfide bond501 ↔ 511 By similarity
Disulfide bond505 ↔ 516 By similarity
Disulfide bond518 ↔ 527 By similarity
Disulfide bond532 ↔ 542 By similarity
Disulfide bond536 ↔ 547 By similarity
Disulfide bond549 ↔ 558 By similarity
Disulfide bond563 ↔ 573 By similarity
Disulfide bond567 ↔ 578 By similarity
Disulfide bond580 ↔ 589 By similarity
Disulfide bond594 ↔ 604 By similarity
Disulfide bond598 ↔ 609 By similarity
Disulfide bond611 ↔ 620 By similarity

Natural variations

Alternative sequence1072 – 1616545Missing in isoform 5. Ref.1
VSP_052144
Alternative sequence1163 – 1616454Missing in isoform 4. Ref.1
VSP_052145
Alternative sequence1254 – 1616363Missing in isoform 3. Ref.1
VSP_052146
Alternative sequence1436 – 152691Missing in isoform 2. Ref.1
VSP_052147

Experimental info

Sequence conflict2021D → E in CAA39751. Ref.2
Sequence conflict3181D → S in CAA39751. Ref.2
Sequence conflict10191Y → S in CAA39751. Ref.2
Sequence conflict10251Q → H in CAA39751. Ref.2
Sequence conflict13061G → S in CAA39751. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A1FEA96F8BC2FE51

FASTA2,110231,807
        10         20         30         40         50         60 
MGAVTWLLPG IFLALFALTP EGGVLKKIIR HKRESGLNMT LPEENQPVVF NHIYNIKLPM 

        70         80         90        100        110        120 
GSQCSVDLES ASGEKDLTPT PESSGSFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK 

       130        140        150        160        170        180 
ELLSRLEELE LLVSSLREQC TMGTGCCLQP AEGRLDTRPF CSGRGNFSAE GCGCVCEPGW 

       190        200        210        220        230        240 
KGPNCSEPDC PGNCNLRGQC LDGQCICDEG FTGEDCSQLA CPNDCNDQGR CVNGVCVCFE 

       250        260        270        280        290        300 
GYAGPDCGLE VCPVPCSEEH GMCVDGRCVC KDGFAGEDCN EPLCLNNCYN RGRCVENECV 

       310        320        330        340        350        360 
CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGELTCPNDC QGRGQCEEGQ 

       370        380        390        400        410        420 
CVCNEGFAGA DCSEKRCPAD CHHRGRCLNG QCECDDGFTG ADCGDLQCPN GCSGHGRCVN 

       430        440        450        460        470        480 
GQCVCDEGYT GEDCSQRRCP NDCHNRGLCV QGKCICEQGF KGFDCSEMSC PNDCHQHGRC 

       490        500        510        520        530        540 
VNGMCICDDD YTGEDCRDRR CPRDCSQRGR CVDGQCICED GFTGPDCAEL SCPSDCHGHG 

       550        560        570        580        590        600 
RCVNGQCICH EGFTGKDCKE QRCPSDCHGQ GRCEDGQCIC HEGFTGLDCG QRSCPNDCSN 

       610        620        630        640        650        660 
QGQCVSGRCI CNEGYTGIDC SEVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLIMYTPTH 

       670        680        690        700        710        720 
ADGLEMQFRV PGDQTSTTIR ELEPGVEYFI RVFAILENKR SIPVSARVAT YLPAPEGLKF 

       730        740        750        760        770        780 
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE 

       790        800        810        820        830        840 
ISLHIVKNNT RGPGLKKVTT TRLDAPSHIE VKDVTDTTAL ITWFKPLAEI DSIELSYGIK 

       850        860        870        880        890        900 
DVPGDRTTID LTHEDNQYSI GNLRPDTEYE VSLISRRVDM ASNPAKETFI TGLDAPRNLR 

       910        920        930        940        950        960 
RVSQTDNSIT LEWRNVKADI DSYRIKYAPI SGGDHAEIDV PKSQQATTKT TLTGLRPGTE 

       970        980        990       1000       1010       1020 
YGIGVSAVKG DKESDPATIN AATEIDAPKD LRVSETTQDS LTFFWTTPLA KFDRYRLNYS 

      1030       1040       1050       1060       1070       1080 
LPTGQSMEVQ LPKDATSHVL TDLEPGQEYT VLLIAEKGRH KSKPARVKAS TEEVPSLENL 

      1090       1100       1110       1120       1130       1140 
TVTEAGWDGL RLNWTADDLA YEYFVIQVQE ANNVETAHNF TVPGNLRAAD IPGLKVATSY 

      1150       1160       1170       1180       1190       1200 
RVSIYGVARG YRTPVLSAET STGTTPNLGE VTVAEVGWDA LTLNWTAPEG AYKNFFIQVL 

      1210       1220       1230       1240       1250       1260 
EADTTQTVQN LTVPGGLRSV DLPGLKAATR YYITLRGVTQ DFGTAPLSVE VLTEDLPQLG 

      1270       1280       1290       1300       1310       1320 
GLSVTEVSWD GLTLNWTTDD LAYKHFVVQV QEANNVEAAQ NLTVPGSLRA VDIPGLKADT 

      1330       1340       1350       1360       1370       1380 
PYRVSIYGVI QGYRTPMLST DVSTAREPEI GNLNVSDVTP KSFNLSWTAT DGIFDMFTIE 

      1390       1400       1410       1420       1430       1440 
IIDSNRLLQT AEHNISGAER TAHISGLPPS TDFIVYLSGI APSIRTKTIS TTATTEALPL 

      1450       1460       1470       1480       1490       1500 
LENLTISDTN PYGFTVSWTA SENAFDSFLV TVVDSGKLLD PQEFTLSGTQ RKLELRGLIT 

      1510       1520       1530       1540       1550       1560 
GIGYEVLVSG FTQGHQTKPL RAETITEAEP EVDNLLVSDA TPDGFRLSWT ADEGIFDSFV 

      1570       1580       1590       1600       1610       1620 
IRIRDTKKQS EPQEISLPSP ERTRDITGLR EATEYEIELY GISRGRRSQP VSAIATTAMG 

      1630       1640       1650       1660       1670       1680 
SPKEIMFSDI TENAATVSWR APTAQVESFR ITYVPMTGGA PSMVTVDGTD TETRLVKLTP 

      1690       1700       1710       1720       1730       1740 
GVEYRVSVIA MKGFEESDPV SGTLITALDG PSGLLIANIT DSEALAMWQP AIATVDSYVI 

      1750       1760       1770       1780       1790       1800 
SYTGERVPEV TRTVSGNTVE YELHDLEPAT EYILSIFAEK GQQKSSTIAT KFTTDLDSPR 

      1810       1820       1830       1840       1850       1860 
EFTATEVQSE TALLTWRPPR ASVTGYLLVY ESVDGTVKEV IVGPDTTSYS LADLSPSTHY 

      1870       1880       1890       1900       1910       1920 
SARIQALSGS LRSKLIQTIF TTIGLLYPFP RDCSQAMLNG DTTSGLYTIY INGDKTQALE 

      1930       1940       1950       1960       1970       1980 
VYCDMTSDGG GWIVFLRRKN GREDFYRNWK AYAAGFGDRR EEFWLGLDNL SKITAQGQYE 

      1990       2000       2010       2020       2030       2040 
LRVDLQDHGE SAYAVYDRFS VGDAKSRYKL KVEGYSGTAG DSMNYHNGRS FSTYDKDTDS 

      2050       2060       2070       2080       2090       2100 
AITNCALSYK GAFWYKNCHR VNLMGRYGDN NHSQGVNWFH WKGHEYSIQF AEMKLRPSNF 

      2110 
RNLEGRRKRA 

« Hide

Isoform 2 [UniParc].

Checksum: 27C4BFFA2024304C
Show »

FASTA2,019221,879
Isoform 3 [UniParc].

Checksum: 18733FA4332BC36B
Show »

FASTA1,747192,063
Isoform 4 [UniParc].

Checksum: 1DC087F9641641AE
Show »

FASTA1,656182,340
Isoform 5 [UniParc].

Checksum: A8BA58FE720C4BBD
Show »

FASTA1,565172,354

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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., 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.
Strain: C57BL/6.
Tissue: Plasma.
+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.
CCDSCCDS18265.1. [Q80YX1-2]
PIRJQ1322.
RefSeqNP_035737.2. NM_011607.3. [Q80YX1-2]
XP_006537837.1. XM_006537774.1. [Q80YX1-1]
UniGeneMm.454219.
Mm.980.

3D structure databases

ProteinModelPortalQ80YX1.
SMRQ80YX1. Positions 158-2098.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80YX1. 1 interaction.
MINTMINT-4110071.

PTM databases

PhosphoSiteQ80YX1.

Proteomic databases

MaxQBQ80YX1.
PaxDbQ80YX1.
PRIDEQ80YX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030056; ENSMUSP00000030056; ENSMUSG00000028364. [Q80YX1-2]
ENSMUST00000107372; ENSMUSP00000102995; ENSMUSG00000028364. [Q80YX1-1]
ENSMUST00000107377; ENSMUSP00000103000; ENSMUSG00000028364. [Q80YX1-2]
GeneID21923.
KEGGmmu:21923.
UCSCuc008thg.2. mouse. [Q80YX1-2]

Organism-specific databases

CTD3371.
MGIMGI:101922. Tnc.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117522.
HOGENOMHOG000234355.
HOVERGENHBG008949.
InParanoidQ80YX1.
KOK06252.
OMAGCCLQPA.
OrthoDBEOG7X9G60.
PhylomeDBQ80YX1.
TreeFamTF329915.

Enzyme and pathway databases

ReactomeREACT_206066. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ80YX1.
BgeeQ80YX1.
CleanExMM_TNC.
GenevestigatorQ80YX1.

Family and domain databases

Gene3D2.60.40.10. 14 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR000742. 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]
PfamPF07974. EGF_2. 7 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 14 hits.
PF12661. hEGF. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 12 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 14 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 11 hits.
SSF56496. SSF56496. 1 hit.
PROSITEPS00022. EGF_1. 15 hits.
PS01186. EGF_2. 14 hits.
PS50026. EGF_3. 5 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 14 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301496.
PROQ80YX1.
SOURCESearch...

Entry information

Entry nameTENA_MOUSE
AccessionPrimary (citable) accession number: Q80YX1
Secondary accession number(s): Q64706, Q80YX2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot