TENA_HUMAN
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 03-AUG-2022, entry version 235.
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 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 [15]
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 [16]
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 [17]
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.
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 -!- INDUCTION: By TGFB1.
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="http://atlasgeneticsoncology.org/Genes/TNCID42597ch9q33.html";
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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 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 AlphaFoldDB; P24821; -.
DR SMR; P24821; -.
DR BioGRID; 109602; 19.
DR ComplexPortal; CPX-466; Tenascin-C complex.
DR CORUM; P24821; -.
DR IntAct; P24821; 5.
DR MINT; P24821; -.
DR STRING; 9606.ENSP00000265131; -.
DR ChEMBL; CHEMBL3712856; -.
DR GlyConnect; 1792; 72 N-Linked glycans (14 sites).
DR GlyGen; P24821; 31 sites, 58 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; P24821; -.
DR PeptideAtlas; P24821; -.
DR PRIDE; 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 ABCD; P24821; 45 sequenced antibodies.
DR Antibodypedia; 1348; 997 antibodies from 44 providers.
DR DNASU; 3371; -.
DR Ensembl; ENST00000350763.9; ENSP00000265131.4; ENSG00000041982.16. [P24821-1]
DR Ensembl; ENST00000537320.5; ENSP00000443478.1; ENSG00000041982.16. [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 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; 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; DVEWDPL; -.
DR OrthoDB; 18592at2759; -.
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 1076 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 185 other tissues.
DR ExpressionAtlas; P24821; baseline and differential.
DR Genevisible; P24821; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0045545; F:syndecan binding; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0060739; P:mesenchymal-epithelial cell signaling involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
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; IC:ComplexPortal.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IDA:ComplexPortal.
DR CDD; cd00063; FN3; 15.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 15.
DR Gene3D; 3.90.215.10; -; 1.
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 InterPro; IPR033078; TNC.
DR PANTHER; PTHR46708:SF1; PTHR46708:SF1; 6.
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; SSF49265; SSF49265; 12.
DR SUPFAM; SSF56496; SSF56496; 1.
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.
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; Reference proteome; Repeat;
KW 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 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 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 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
