ID TENA_HUMAN Reviewed; 2201 AA. AC P24821; C9IYT7; C9J575; C9J6D9; C9J848; Q14583; Q15567; Q5T7S3; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 3. DT 27-MAR-2024, entry version 244. DE RecName: Full=Tenascin; DE Short=TN; DE AltName: Full=Cytotactin; DE AltName: Full=GMEM; DE AltName: Full=GP 150-225; DE AltName: Full=Glioma-associated-extracellular matrix antigen; DE AltName: Full=Hexabrachion; DE AltName: Full=JI; DE AltName: Full=Myotendinous antigen; DE AltName: Full=Neuronectin; DE AltName: Full=Tenascin-C; DE Short=TN-C; DE Flags: Precursor; GN Name=TNC; Synonyms=HXB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-539; LEU-1677 AND RP GLN-2008. RX PubMed=1704365; DOI=10.1016/s0021-9258(18)49920-6; RA Nies D.E., Hemesath T.J., Kim J.H., Gulcher J.R., Stefansson K.; RT "The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain RT protein containing unique epidermal growth factor repeats."; RL J. Biol. Chem. 266:2818-2823(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), PROTEIN SEQUENCE OF RP 23-32, AND VARIANTS ARG-680 AND GLN-2008. RC TISSUE=Fetal brain, and Melanoma; RX PubMed=1707164; DOI=10.1093/nar/19.3.525; RA Siri A., Carnemolla B., Saginati M., Leprini A., Casari G., Baralle F., RA Zardi L.; RT "Human tenascin: primary structure, pre-mRNA splicing patterns and RT localization of the epitopes recognized by two monoclonal antibodies."; RL Nucleic Acids Res. 19:525-531(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-539; LEU-1677 AND RP GLN-2008. RX PubMed=1719530; DOI=10.1073/pnas.88.21.9438; RA Gulcher J.R., Nies D.E., Alexakos M.J., Ravikant N.A., Sturgill M.E., RA Marton L.S., Stefansson K.; RT "Structure of the human hexabrachion (tenascin) gene."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9438-9442(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LEU-1677 AND GLN-2008. RX PubMed=7531707; DOI=10.1074/jbc.270.7.3429; RA Gherzi R., Carnemolla B., Siri A., Ponassi M., Balza E., Zardi L.; RT "Human tenascin gene. Structure of the 5'-region, identification, and RT characterization of the transcription regulatory sequences."; RL J. Biol. Chem. 270:3429-3434(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-125 (ISOFORMS 1/2/3/4/5/6). RC TISSUE=Fetal cartilage; RX PubMed=7524681; DOI=10.1016/0167-4781(94)90220-8; RA Glumoff V., Savontaus M., Vehanen J., Vuorio E.; RT "Analysis of aggrecan and tenascin gene expression in mouse skeletal RT tissues by northern and in situ hybridization using species specific cDNA RT probes."; RL Biochim. Biophys. Acta 1219:613-622(1994). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 431-2055 (ISOFORMS 1 AND 6), AND VARIANTS RP ARG-539; LEU-1677 AND GLN-2008. RC TISSUE=Glioblastoma; RX PubMed=2466295; DOI=10.1073/pnas.86.5.1588; RA Gulcher J.R., Nies D.E., Marton L.S., Stefansson K.; RT "An alternatively spliced region of the human hexabrachion contains a RT repeat of potential N-glycosylation sites."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1588-1592(1989). RN [8] RP INTERACTION WITH CSPG4. RX PubMed=8824254; DOI=10.1074/jbc.271.42.26110; RA Burg M.A., Tillet E., Timpl R., Stallcup W.B.; RT "Binding of the NG2 proteoglycan to type VI collagen and other RT extracellular matrix molecules."; RL J. Biol. Chem. 271:26110-26116(1996). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1809. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-1079; ASN-1093; RP ASN-1261; ASN-1301; ASN-1485 AND ASN-2162. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1018; ASN-1034; ASN-1184; RP ASN-1275; ASN-1301; ASN-1366 AND ASN-1485. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [12] RP FUNCTION. RX PubMed=19884327; DOI=10.1096/fj.09-140491; RA Martina E., Degen M., Rueegg C., Merlo A., Lino M.M., Chiquet-Ehrismann R., RA Brellier F.; RT "Tenascin-W is a specific marker of glioma-associated blood vessels and RT stimulates angiogenesis in vitro."; RL FASEB J. 24:778-787(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP INTERACTION WITH ITGA9:ITGB1. RX PubMed=22654117; DOI=10.1074/jbc.m112.355016; RA Sato-Nishiuchi R., Nakano I., Ozawa A., Sato Y., Takeichi M., Kiyozumi D., RA Yamazaki K., Yasunaga T., Futaki S., Sekiguchi K.; RT "Polydom/SVEP1 is a ligand for integrin alpha9beta1."; RL J. Biol. Chem. 287:25615-25630(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-70; SER-72 AND RP THR-905, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP PHOSPHORYLATION AT SER-72. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [17] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-72. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF FIBRONECTIN TYPE-III 3. RX PubMed=1279805; DOI=10.1126/science.1279805; RA Leahy D.J., Hendrickson W.A., Aukhil I., Erickson H.P.; RT "Structure of a fibronectin type III domain from tenascin phased by MAD RT analysis of the selenomethionyl protein."; RL Science 258:987-991(1992). RN [19] RP VARIANTS DFNA56 MET-1773 AND SER-1796. RX PubMed=23936043; DOI=10.1371/journal.pone.0069549; RA Zhao Y., Zhao F., Zong L., Zhang P., Guan L., Zhang J., Wang D., Wang J., RA Chai W., Lan L., Li Q., Han B., Yang L., Jin X., Yang W., Hu X., Wang X., RA Li N., Li Y., Petit C., Wang J., Wang H.Y., Wang Q.; RT "Exome sequencing and linkage analysis identified tenascin-C (TNC) as a RT novel causative gene in nonsyndromic hearing loss."; RL PLoS ONE 8:E69549-E69549(2013). CC -!- FUNCTION: Extracellular matrix protein implicated in guidance of CC migrating neurons as well as axons during development, synaptic CC plasticity as well as neuronal regeneration. Promotes neurite outgrowth CC from cortical neurons grown on a monolayer of astrocytes. Ligand for CC integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha- CC V/beta-6. In tumors, stimulates angiogenesis by elongation, migration CC and sprouting of endothelial cells (PubMed:19884327). CC {ECO:0000269|PubMed:19884327}. CC -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in CC the triple coiled-coil region and may be stabilized by disulfide rings CC at both ends. Two of such half-hexabrachions may be disulfide linked CC within the central globule. Interacts with CSPG4 (PubMed:8824254). CC Interacts (via the 3rd fibronectin type-III domain) with integrin CC ITGA9:ITGB1 (PubMed:22654117). {ECO:0000269|PubMed:22654117, CC ECO:0000269|PubMed:8824254}. CC -!- INTERACTION: CC P24821; P20908: COL5A1; NbExp=2; IntAct=EBI-9979894, EBI-2464511; CC P24821; O00206: TLR4; NbExp=4; IntAct=EBI-9979894, EBI-528701; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Isoforms are produced in a tissue- and time-specific manner CC during development.; CC Name=1; CC IsoId=P24821-1; Sequence=Displayed; CC Name=2; Synonyms=HT-5; CC IsoId=P24821-2; Sequence=VSP_001412, VSP_001413; CC Name=3; CC IsoId=P24821-3; Sequence=VSP_001412; CC Name=4; Synonyms=HT-33; CC IsoId=P24821-4; Sequence=VSP_001413; CC Name=5; CC IsoId=P24821-5; Sequence=VSP_001414; CC Name=6; Synonyms=P31; CC IsoId=P24821-6; Sequence=VSP_001415; CC -!- TISSUE SPECIFICITY: Detected in fibroblasts (at protein level). CC {ECO:0000269|PubMed:36213313}. CC -!- DISEASE: Deafness, autosomal dominant, 56 (DFNA56) [MIM:615629]: A form CC of non-syndromic sensorineural hearing loss. Sensorineural deafness CC results from damage to the neural receptors of the inner ear, the nerve CC pathways to the brain, or the area of the brain that receives sound CC information. DFNA56 is characterized by progressive hearing impairment CC with postlingual onset. {ECO:0000269|PubMed:23936043}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42597/TNC"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M55618; AAA88083.1; -; mRNA. DR EMBL; X56160; CAA39628.1; -; mRNA. DR EMBL; X78565; CAA55309.1; -; mRNA. DR EMBL; AL162425; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X80280; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M24630; AAA52703.1; -; mRNA. DR CCDS; CCDS6811.1; -. [P24821-1] DR PIR; I38337; A32160. DR RefSeq; NP_002151.2; NM_002160.3. [P24821-1] DR RefSeq; XP_005252029.1; XM_005251972.3. [P24821-4] DR RefSeq; XP_005252031.1; XM_005251974.3. [P24821-5] DR RefSeq; XP_005252032.1; XM_005251975.3. [P24821-6] DR RefSeq; XP_011516931.1; XM_011518629.2. [P24821-2] DR PDB; 1TEN; X-ray; 1.80 A; A=802-891. DR PDB; 2RB8; X-ray; 1.45 A; A=802-893. DR PDB; 2RBL; X-ray; 2.10 A; A/B/M=802-893. DR PDB; 5R5T; X-ray; 1.55 A; A=1979-2196. DR PDB; 5R5U; X-ray; 1.52 A; A=1979-2196. DR PDB; 5R5V; X-ray; 1.70 A; A=1979-2196. DR PDB; 5R5W; X-ray; 1.60 A; A=1979-2196. DR PDB; 5R5X; X-ray; 1.56 A; A=1979-2196. DR PDB; 5R5Y; X-ray; 1.57 A; A=1979-2196. DR PDB; 5R5Z; X-ray; 1.67 A; A=1979-2196. DR PDB; 5R60; X-ray; 1.79 A; A=1979-2196. DR PDB; 5R61; X-ray; 1.38 A; A=1979-2196. DR PDB; 5R62; X-ray; 1.40 A; A=1979-2196. DR PDB; 5R63; X-ray; 1.59 A; A=1979-2196. DR PDB; 6BRB; X-ray; 2.82 A; D=809-893. DR PDB; 6QNV; X-ray; 1.40 A; A=1979-2196. DR PDB; 8FN8; X-ray; 1.89 A; A=1975-2201. DR PDB; 8FNB; X-ray; 1.80 A; A/B=1975-2201. DR PDBsum; 1TEN; -. DR PDBsum; 2RB8; -. DR PDBsum; 2RBL; -. DR PDBsum; 5R5T; -. DR PDBsum; 5R5U; -. DR PDBsum; 5R5V; -. DR PDBsum; 5R5W; -. DR PDBsum; 5R5X; -. DR PDBsum; 5R5Y; -. DR PDBsum; 5R5Z; -. DR PDBsum; 5R60; -. DR PDBsum; 5R61; -. DR PDBsum; 5R62; -. DR PDBsum; 5R63; -. DR PDBsum; 6BRB; -. DR PDBsum; 6QNV; -. DR PDBsum; 8FN8; -. DR PDBsum; 8FNB; -. DR AlphaFoldDB; P24821; -. DR SMR; P24821; -. DR BioGRID; 109602; 23. DR ComplexPortal; CPX-466; Tenascin-C complex. DR CORUM; P24821; -. DR IntAct; P24821; 6. DR MINT; P24821; -. DR STRING; 9606.ENSP00000265131; -. DR ChEMBL; CHEMBL3712856; -. DR UniLectin; P24821; -. DR GlyConnect; 1792; 72 N-Linked glycans (14 sites). DR GlyCosmos; P24821; 31 sites, 67 glycans. DR GlyGen; P24821; 32 sites, 65 N-linked glycans (14 sites), 2 O-linked glycans (8 sites). DR iPTMnet; P24821; -. DR PhosphoSitePlus; P24821; -. DR SwissPalm; P24821; -. DR BioMuta; TNC; -. DR DMDM; 281185495; -. DR CPTAC; non-CPTAC-2700; -. DR EPD; P24821; -. DR jPOST; P24821; -. DR MassIVE; P24821; -. DR MaxQB; P24821; -. DR PaxDb; 9606-ENSP00000265131; -. DR PeptideAtlas; P24821; -. DR ProteomicsDB; 54225; -. [P24821-1] DR ProteomicsDB; 54226; -. [P24821-2] DR ProteomicsDB; 54227; -. [P24821-3] DR ProteomicsDB; 54228; -. [P24821-4] DR ProteomicsDB; 54229; -. [P24821-5] DR ProteomicsDB; 54230; -. [P24821-6] DR Pumba; P24821; -. DR ABCD; P24821; 45 sequenced antibodies. DR Antibodypedia; 1348; 1133 antibodies from 44 providers. DR DNASU; 3371; -. DR Ensembl; ENST00000350763.9; ENSP00000265131.4; ENSG00000041982.17. [P24821-1] DR Ensembl; ENST00000537320.6; ENSP00000443478.1; ENSG00000041982.17. [P24821-6] DR GeneID; 3371; -. DR KEGG; hsa:3371; -. DR MANE-Select; ENST00000350763.9; ENSP00000265131.4; NM_002160.4; NP_002151.2. DR UCSC; uc004bjj.6; human. [P24821-1] DR AGR; HGNC:5318; -. DR CTD; 3371; -. DR DisGeNET; 3371; -. DR GeneCards; TNC; -. DR HGNC; HGNC:5318; TNC. DR HPA; ENSG00000041982; Tissue enhanced (lymphoid tissue, smooth muscle). DR MalaCards; TNC; -. DR MIM; 187380; gene. DR MIM; 615629; phenotype. DR neXtProt; NX_P24821; -. DR OpenTargets; ENSG00000041982; -. DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA. DR PharmGKB; PA35103; -. DR VEuPathDB; HostDB:ENSG00000041982; -. DR eggNOG; KOG1225; Eukaryota. DR eggNOG; KOG2579; Eukaryota. DR GeneTree; ENSGT00940000155188; -. DR HOGENOM; CLU_001162_1_1_1; -. DR InParanoid; P24821; -. DR OMA; PNACHGQ; -. DR OrthoDB; 5489847at2759; -. DR PhylomeDB; P24821; -. DR TreeFam; TF329915; -. DR PathwayCommons; P24821; -. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SignaLink; P24821; -. DR SIGNOR; P24821; -. DR BioGRID-ORCS; 3371; 10 hits in 1156 CRISPR screens. DR ChiTaRS; TNC; human. DR EvolutionaryTrace; P24821; -. DR GeneWiki; Tenascin_C; -. DR GenomeRNAi; 3371; -. DR Pharos; P24821; Tbio. DR PRO; PR:P24821; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P24821; Protein. DR Bgee; ENSG00000041982; Expressed in saphenous vein and 187 other cell types or tissues. DR ExpressionAtlas; P24821; baseline and differential. DR GO; GO:0005604; C:basement membrane; ISO:ComplexPortal. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005614; C:interstitial matrix; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0098966; C:perisynaptic extracellular matrix; IBA:GO_Central. DR GO; GO:0090733; C:tenascin complex; ISO:ComplexPortal. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL. DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB. DR GO; GO:0045545; F:syndecan binding; IDA:MGI. DR GO; GO:0060447; P:bud outgrowth involved in lung branching; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl. DR GO; GO:0060739; P:mesenchymal-epithelial cell signaling involved in prostate gland development; IEA:Ensembl. DR GO; GO:0002009; P:morphogenesis of an epithelium; ISO:ComplexPortal. DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0007528; P:neuromuscular junction development; ISO:ComplexPortal. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0014012; P:peripheral nervous system axon regeneration; ISO:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:ComplexPortal. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl. DR GO; GO:0030155; P:regulation of cell adhesion; IDA:ComplexPortal. DR GO; GO:0001558; P:regulation of cell growth; IDA:ComplexPortal. DR GO; GO:0030334; P:regulation of cell migration; NAS:ComplexPortal. DR GO; GO:0050727; P:regulation of inflammatory response; ISO:ComplexPortal. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IDA:ComplexPortal. DR CDD; cd00054; EGF_CA; 4. DR CDD; cd00063; FN3; 14. DR CDD; cd00087; FReD; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 15. DR Gene3D; 2.10.25.10; Laminin; 14. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR041161; EGF_Tenascin. DR InterPro; IPR036056; Fibrinogen-like_C. DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1. DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR NCBIfam; NF040941; GGGWT_bact; 1. DR PANTHER; PTHR46708; TENASCIN; 1. DR PANTHER; PTHR46708:SF1; TENASCIN; 1. DR Pfam; PF07974; EGF_2; 4. DR Pfam; PF18720; EGF_Tenascin; 9. DR Pfam; PF00147; Fibrinogen_C; 1. DR Pfam; PF00041; fn3; 15. DR SMART; SM00181; EGF; 14. DR SMART; SM00186; FBG; 1. DR SMART; SM00060; FN3; 15. DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1. DR SUPFAM; SSF49265; Fibronectin type III; 12. DR PROSITE; PS00022; EGF_1; 15. DR PROSITE; PS01186; EGF_2; 15. DR PROSITE; PS50026; EGF_3; 5. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. DR PROSITE; PS50853; FN3; 15. DR Genevisible; P24821; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Coiled coil; Deafness; KW Direct protein sequencing; Disease variant; Disulfide bond; KW EGF-like domain; Extracellular matrix; Glycoprotein; KW Non-syndromic deafness; Phosphoprotein; Proteoglycan; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:1707164" FT CHAIN 23..2201 FT /note="Tenascin" FT /id="PRO_0000007741" FT DOMAIN 174..186 FT /note="EGF-like 1; incomplete" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 186..217 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 217..248 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 248..280 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 280..311 FT /note="EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 311..342 FT /note="EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 342..373 FT /note="EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 373..404 FT /note="EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 404..435 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 435..466 FT /note="EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 466..497 FT /note="EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 497..528 FT /note="EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 528..559 FT /note="EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 559..590 FT /note="EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 590..621 FT /note="EGF-like 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 625..715 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 716..804 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 805..894 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 895..990 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 991..1075 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1076..1165 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1167..1256 FT /note="Fibronectin type-III 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1258..1350 FT /note="Fibronectin type-III 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1351..1439 FT /note="Fibronectin type-III 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1440..1531 FT /note="Fibronectin type-III 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1533..1621 FT /note="Fibronectin type-III 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1622..1711 FT /note="Fibronectin type-III 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1712..1801 FT /note="Fibronectin type-III 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1802..1888 FT /note="Fibronectin type-III 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1889..1977 FT /note="Fibronectin type-III 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1975..2190 FT /note="Fibrinogen C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739" FT COILED 118..145 FT /evidence="ECO:0000255" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 72 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:24275569" FT MOD_RES 905 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 72 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 327 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 788 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1018 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1034 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1079 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 1093 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 1119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1210 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1261 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 1275 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 1366 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1392 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1455 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1485 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 1534 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1809 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 2162 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT DISULFID 190..200 FT /evidence="ECO:0000250" FT DISULFID 194..205 FT /evidence="ECO:0000250" FT DISULFID 207..216 FT /evidence="ECO:0000250" FT DISULFID 221..231 FT /evidence="ECO:0000250" FT DISULFID 225..236 FT /evidence="ECO:0000250" FT DISULFID 238..247 FT /evidence="ECO:0000250" FT DISULFID 252..263 FT /evidence="ECO:0000250" FT DISULFID 256..268 FT /evidence="ECO:0000250" FT DISULFID 270..279 FT /evidence="ECO:0000250" FT DISULFID 284..294 FT /evidence="ECO:0000250" FT DISULFID 288..299 FT /evidence="ECO:0000250" FT DISULFID 301..310 FT /evidence="ECO:0000250" FT DISULFID 315..325 FT /evidence="ECO:0000250" FT DISULFID 319..330 FT /evidence="ECO:0000250" FT DISULFID 332..341 FT /evidence="ECO:0000250" FT DISULFID 346..356 FT /evidence="ECO:0000250" FT DISULFID 350..361 FT /evidence="ECO:0000250" FT DISULFID 363..372 FT /evidence="ECO:0000250" FT DISULFID 377..387 FT /evidence="ECO:0000250" FT DISULFID 381..392 FT /evidence="ECO:0000250" FT DISULFID 394..403 FT /evidence="ECO:0000250" FT DISULFID 408..418 FT /evidence="ECO:0000250" FT DISULFID 412..423 FT /evidence="ECO:0000250" FT DISULFID 425..434 FT /evidence="ECO:0000250" FT DISULFID 439..449 FT /evidence="ECO:0000250" FT DISULFID 443..454 FT /evidence="ECO:0000250" FT DISULFID 456..465 FT /evidence="ECO:0000250" FT DISULFID 470..480 FT /evidence="ECO:0000250" FT DISULFID 474..485 FT /evidence="ECO:0000250" FT DISULFID 487..496 FT /evidence="ECO:0000250" FT DISULFID 501..511 FT /evidence="ECO:0000250" FT DISULFID 505..516 FT /evidence="ECO:0000250" FT DISULFID 518..527 FT /evidence="ECO:0000250" FT DISULFID 532..542 FT /evidence="ECO:0000250" FT DISULFID 536..547 FT /evidence="ECO:0000250" FT DISULFID 549..558 FT /evidence="ECO:0000250" FT DISULFID 563..573 FT /evidence="ECO:0000250" FT DISULFID 567..578 FT /evidence="ECO:0000250" FT DISULFID 580..589 FT /evidence="ECO:0000250" FT DISULFID 594..604 FT /evidence="ECO:0000250" FT DISULFID 598..609 FT /evidence="ECO:0000250" FT DISULFID 611..620 FT /evidence="ECO:0000250" FT VAR_SEQ 1072..1708 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:2466295" FT /id="VSP_001415" FT VAR_SEQ 1072..1617 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:1707164" FT /id="VSP_001414" FT VAR_SEQ 1072..1435 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:1707164" FT /id="VSP_001412" FT VAR_SEQ 1527..1617 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:1707164" FT /id="VSP_001413" FT VARIANT 213 FT /note="G -> S (in dbSNP:rs7020958)" FT /id="VAR_055778" FT VARIANT 539 FT /note="Q -> R (in dbSNP:rs1757095)" FT /evidence="ECO:0000269|PubMed:1704365, FT ECO:0000269|PubMed:1719530, ECO:0000269|PubMed:2466295" FT /id="VAR_024266" FT VARIANT 605 FT /note="V -> I (in dbSNP:rs3827816)" FT /id="VAR_024267" FT VARIANT 680 FT /note="Q -> R (in dbSNP:rs1061494)" FT /evidence="ECO:0000269|PubMed:1707164" FT /id="VAR_024268" FT VARIANT 850 FT /note="D -> H (in dbSNP:rs3748169)" FT /id="VAR_055779" FT VARIANT 1677 FT /note="I -> L (in dbSNP:rs2104772)" FT /evidence="ECO:0000269|PubMed:1704365, FT ECO:0000269|PubMed:1719530, ECO:0000269|PubMed:2466295, FT ECO:0000269|PubMed:7531707" FT /id="VAR_060738" FT VARIANT 1773 FT /note="V -> M (in DFNA56; dbSNP:rs137933052)" FT /evidence="ECO:0000269|PubMed:23936043" FT /id="VAR_070984" FT VARIANT 1781 FT /note="A -> T (in dbSNP:rs2274750)" FT /id="VAR_020169" FT VARIANT 1796 FT /note="T -> S (in DFNA56; dbSNP:rs431905513)" FT /evidence="ECO:0000269|PubMed:23936043" FT /id="VAR_070985" FT VARIANT 2008 FT /note="E -> Q (in dbSNP:rs13321)" FT /evidence="ECO:0000269|PubMed:1704365, FT ECO:0000269|PubMed:1707164, ECO:0000269|PubMed:1719530, FT ECO:0000269|PubMed:2466295, ECO:0000269|PubMed:7531707" FT /id="VAR_014665" FT CONFLICT 244 FT /note="Missing (in Ref. 2; CAA39628)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="V -> L (in Ref. 1; no nucleotide entry, 3; AAA88083 FT and 4; CAA55309)" FT /evidence="ECO:0000305" FT CONFLICT 1066 FT /note="R -> H (in Ref. 1; no nucleotide entry, 3; AAA88083 FT and 7; AAA52703)" FT /evidence="ECO:0000305" FT CONFLICT 1600..1608 FT /note="SGFTQGHQT -> LWLHPRASN (in Ref. 1; no nucleotide FT entry, 3; AAA88083 and 7; AAA52703)" FT /evidence="ECO:0000305" FT CONFLICT 2054 FT /note="F -> FLH (in Ref. 1; no nucleotide entry and 3; FT AAA88083)" FT /evidence="ECO:0000305" FT CONFLICT 2055 FT /note="W -> L (in Ref. 7; AAA52703)" FT /evidence="ECO:0000305" FT CONFLICT 2140..2143 FT /note="YKGA -> TRG (in Ref. 2; CAA39628)" FT /evidence="ECO:0000305" FT STRAND 807..813 FT /evidence="ECO:0007829|PDB:2RB8" FT STRAND 819..824 FT /evidence="ECO:0007829|PDB:2RB8" FT HELIX 827..829 FT /evidence="ECO:0007829|PDB:2RBL" FT STRAND 831..839 FT /evidence="ECO:0007829|PDB:2RB8" FT STRAND 842..844 FT /evidence="ECO:0007829|PDB:2RBL" FT STRAND 847..852 FT /evidence="ECO:0007829|PDB:2RB8" FT HELIX 853..855 FT /evidence="ECO:0007829|PDB:6BRB" FT STRAND 857..860 FT /evidence="ECO:0007829|PDB:2RB8" FT STRAND 868..877 FT /evidence="ECO:0007829|PDB:2RB8" FT STRAND 885..890 FT /evidence="ECO:0007829|PDB:2RB8" FT STRAND 1977..1980 FT /evidence="ECO:0007829|PDB:8FN8" FT HELIX 1984..1989 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 1996..2001 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2002..2004 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2008..2015 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2018..2020 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2023..2032 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2040..2045 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2052..2055 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2058..2065 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2070..2078 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2081..2092 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2095..2097 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2101..2110 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2115..2117 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2130..2134 FT /evidence="ECO:0007829|PDB:8FNB" FT HELIX 2136..2140 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2147..2149 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2151..2153 FT /evidence="ECO:0007829|PDB:5R61" FT TURN 2163..2165 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2166..2169 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2170..2173 FT /evidence="ECO:0007829|PDB:5R61" FT STRAND 2180..2188 FT /evidence="ECO:0007829|PDB:5R61" FT HELIX 2189..2193 FT /evidence="ECO:0007829|PDB:5R61" SQ SEQUENCE 2201 AA; 240853 MW; B2BEF378AA6F1D85 CRC64; MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF NHVYNIKLPV GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK ELLSRLEELE NLVSSLREQC TAGAGCCLQP ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW KGPNCSEPEC PGNCHLRGRC IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE GYAGADCSRE ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC HTQGRCEEGQ CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG ADCGELKCPN GCSGHGRCVN GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC VNGMCVCDDG YTGEDCRDRQ CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG RCVNGQCVCH EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT EYLVVYTPTH EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK DVPGDRTTID LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT TLTGLRPGTE YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS LTLLWKTPLA KFDRYRLNYS LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN VLLTAEKGRH KSKPARVKAS TEQAPELENL TVTEVGWDGL RLNWTAADQA YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY TVSIYGVIQG YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE VLTEEVPDMG NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH NLTVPGSLRS MEIPGLRAGT PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ VQEVNKVEAA QNLTLPGSLR AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAKEPE IGNLNVSDIT PESFNLSWMA TDGIFETFTI EIIDSNRLLE TVEYNISGAE RTAHISGLPP STDFIVYLSG LAPSIRTKTI SATATTEALP LLENLTISDI NPYGFTVSWM ASENAFDSFL VTVVDSGKLL DPQEFTLSGT QRKLELRGLI TGIGYEVMVS GFTQGHQTKP LRAEIVTEAE PEVDNLLVSD ATPDGFRLSW TADEGVFDNF VLKIRDTKKQ SEPLEITLLA PERTRDITGL REATEYEIEL YGISKGRRSQ TVSAIATTAM GSPKEVIFSD ITENSATVSW RAPTAQVESF RITYVPITGG TPSMVTVDGT KTQTRLVKLI PGVEYLVSII AMKGFEESEP VSGSFTTALD GPSGLVTANI TDSEALARWQ PAIATVDSYV ISYTGEKVPE ITRTVSGNTV EYALTDLEPA TEYTLRIFAE KGPQKSSTIT AKFTTDLDSP RDLTATEVQS ETALLTWRPP RASVTGYLLV YESVDGTVKE VIVGPDTTSY SLADLSPSTH YTAKIQALNG PLRSNMIQTI FTTIGLLYPF PKDCSQAMLN GDTTSGLYTI YLNGDKAEAL EVFCDMTSDG GGWIVFLRRK NGRENFYQNW KAYAAGFGDR REEFWLGLDN LNKITAQGQY ELRVDLRDHG ETAFAVYDKF SVGDAKTRYK LKVEGYSGTA GDSMAYHNGR SFSTFDKDTD SAITNCALSY KGAFWYRNCH RVNLMGRYGD NNHSQGVNWF HWKGHEHSIQ FAEMKLRPSN FRNLEGRRKR A //