GenomeNet

Database: UniProt
Entry: P22105
LinkDB: P22105
Original site: P22105 
ID   TENX_HUMAN              Reviewed;        4244 AA.
AC   P22105; P78530; P78531; Q08424; Q08AM0; Q08AM1; Q59GU7; Q5SQD3;
AC   Q5ST74; Q7L8Q4; Q8N4R1; Q9NPK9; Q9UC10; Q9UC11; Q9UC12; Q9UC13;
AC   Q9UMG7;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 5.
DT   13-FEB-2019, entry version 212.
DE   RecName: Full=Tenascin-X {ECO:0000305};
DE            Short=TN-X;
DE   AltName: Full=Hexabrachion-like protein;
DE   Flags: Precursor;
GN   Name=TNXB {ECO:0000312|HGNC:HGNC:11976};
GN   Synonyms=HXBL, TNX, TNXB1, TNXB2, XB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XB-SHORT).
RC   TISSUE=Adrenal gland;
RX   PubMed=8530023; DOI=10.1006/geno.1995.1128;
RA   Tee M.K., Thomson A.A., Bristow J., Miller W.L.;
RT   "Sequences promoting the transcription of the human XA gene
RT   overlapping P450c21A correctly predict the presence of a novel,
RT   adrenal-specific, truncated form of tenascin-X.";
RL   Genomics 28:171-178(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-2518.
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-302
RP   AND GLU-2518.
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XB-SHORT).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-747 (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1605-1862 (ISOFORMS 3/4/5).
RC   TISSUE=Leukocyte;
RX   PubMed=7686164; DOI=10.1083/jcb.122.1.265;
RA   Bristow J., Tee M.K., Gitelman S.E., Mellon S.H., Miller W.L.;
RT   "Tenascin-X: a novel extracellular matrix protein encoded by the human
RT   XB gene overlapping P450c21B.";
RL   J. Cell Biol. 122:265-278(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-23 (ISOFORMS 3/4/5).
RC   TISSUE=Fetal adrenal gland;
RX   PubMed=8923003; DOI=10.1093/hmg/5.11.1749;
RA   Speek M., Barry F., Miller W.L.;
RT   "Alternate promoters and alternate splicing of human tenascin-X, a
RT   gene with 5' and 3' ends buried in other genes.";
RL   Hum. Mol. Genet. 5:1749-1758(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1061-1148; 2521-2607; 2627-2714
RP   AND 2735-2821.
RC   TISSUE=B-cell;
RX   PubMed=1373119; DOI=10.1016/0888-7543(92)90438-X;
RA   Matsumoto K., Arai M., Ishihara N., Ando A., Inoko H., Ikemura T.;
RT   "Cluster of fibronectin type III repeats found in the human major
RT   histocompatibility complex class III region shows the highest homology
RT   with the repeats in an extracellular matrix protein, tenascin.";
RL   Genomics 12:485-491(1992).
RN   [9]
RP   PROTEIN SEQUENCE OF 1399-1407; 1438-1448; 2122-2130; 2438-2446;
RP   2549-2557; 2763-2771; 2782-2799; 2979-2987; 3018-3028; 3193-3201;
RP   3212-3229 AND 3232-3242 (ISOFORMS 3/4/5), PROTEIN SEQUENCE OF
RP   3609-3621 AND 3633-3665 (ISOFORMS XB-SHORT/3/4/5), INTERACTION WITH
RP   TROPOELASTIN, AND DEVELOPMENTAL STAGE.
RX   PubMed=17263730; DOI=10.1111/j.1742-4658.2007.05671.x;
RA   Egging D.F., Peeters A.C.T.M., Grebenchtchikov N., Geurts-Moespot A.,
RA   Sweep C.G.J., den Heijer M., Schalkwijk J.;
RT   "Identification and characterization of multiple species of tenascin-X
RT   in human serum.";
RL   FEBS J. 274:1280-1289(2007).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3360-4244 (ISOFORMS 3/4/5).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3425-4244 (ISOFORMS 3/4/5).
RX   PubMed=2475872; DOI=10.1073/pnas.86.17.6582;
RA   Morel Y., Bristow J., Gitelman S.E., Miller W.L.;
RT   "Transcript encoded on the opposite strand of the human steroid 21-
RT   hydroxylase/complement component C4 gene locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6582-6586(1989).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3920.
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.,
RA   Moore R.J., 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   [13]
RP   FUNCTION, AND INTERACTION WITH COLLAGEN AND TROPOELASTIN.
RX   PubMed=17033827; DOI=10.1007/s00403-006-0706-9;
RA   Egging D.F., van den Berkmortel F., Taylor G., Bristow J.,
RA   Schalkwijk J.;
RT   "Interactions of human tenascin-X domains with dermal extracellular
RT   matrix molecules.";
RL   Arch. Dermatol. Res. 298:389-396(2007).
RN   [14]
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   STRUCTURE BY NMR OF 3654-4024.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the 29th, 31st and 33rd fibronectin type-III
RT   domains of the human tenascin-X.";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [16]
RP   INVOLVEMENT IN EDSCLL.
RX   PubMed=11642233; DOI=10.1056/NEJMoa002939;
RA   Schalkwijk J., Zweers M.C., Steijlen P.M., Dean W.B., Taylor G.,
RA   van Vlijmen I.M., van Haren B., Miller W.L., Bristow J.;
RT   "A recessive form of the Ehlers-Danlos syndrome caused by tenascin-X
RT   deficiency.";
RL   N. Engl. J. Med. 345:1167-1175(2001).
RN   [17]
RP   VARIANTS EDSCLL TRP-29 AND MET-1108, AND VARIANT ILE-3988.
RX   PubMed=15733269; DOI=10.1111/j.1399-0004.2005.00401.x;
RA   Zweers M.C., Dean W.B., van Kuppevelt T.H., Bristow J., Schalkwijk J.;
RT   "Elastic fiber abnormalities in hypermobility type Ehlers-Danlos
RT   syndrome patients with tenascin-X mutations.";
RL   Clin. Genet. 67:330-334(2005).
RN   [18]
RP   VARIANT EDSCLL CYS-4074.
RX   PubMed=23768946; DOI=10.1016/j.nmd.2013.04.009;
RA   Penisson-Besnier I., Allamand V., Beurrier P., Martin L.,
RA   Schalkwijk J., van Vlijmen-Willems I., Gartioux C., Malfait F.,
RA   Syx D., Macchi L., Marcorelles P., Arbeille B., Croue A., De Paepe A.,
RA   Dubas F.;
RT   "Compound heterozygous mutations of the TNXB gene cause primary
RT   myopathy.";
RL   Neuromuscul. Disord. 23:664-669(2013).
RN   [19]
RP   VARIANTS VUR8 ARG-1244 AND ILE-3212.
RX   PubMed=23620400; DOI=10.1681/ASN.2012121148;
RA   Gbadegesin R.A., Brophy P.D., Adeyemo A., Hall G., Gupta I.R.,
RA   Hains D., Bartkowiak B., Rabinovich C.E., Chandrasekharappa S.,
RA   Homstad A., Westreich K., Wu G., Liu Y., Holanda D., Clarke J.,
RA   Lavin P., Selim A., Miller S., Wiener J.S., Ross S.S., Foreman J.,
RA   Rotimi C., Winn M.P.;
RT   "TNXB mutations can cause vesicoureteral reflux.";
RL   J. Am. Soc. Nephrol. 24:1313-1322(2013).
CC   -!- FUNCTION: Appears to mediate interactions between cells and the
CC       extracellular matrix. Substrate-adhesion molecule that appears to
CC       inhibit cell migration. Accelerates collagen fibril formation. May
CC       play a role in supporting the growth of epithelial tumors.
CC       {ECO:0000269|PubMed:17033827}.
CC   -!- SUBUNIT: Homotrimer. Interacts with type I, III and V collagens
CC       and tropoelastin via its 29th fibronectin type-III domain.
CC       {ECO:0000269|PubMed:17033827, ECO:0000269|PubMed:17263730}.
CC   -!- INTERACTION:
CC       Q8N9N5:BANP; NbExp=4; IntAct=EBI-2821024, EBI-744695;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=4;
CC         IsoId=P22105-3; Sequence=Displayed;
CC         Note=No experimental confirmation available. May be due to
CC         competing acceptor splice site in exon 24.;
CC       Name=3;
CC         IsoId=P22105-1; Sequence=VSP_059794;
CC         Note=No experimental confirmation available.;
CC       Name=XB-short; Synonyms=2;
CC         IsoId=P22105-2; Sequence=VSP_059792;
CC       Name=5;
CC         IsoId=P22105-4; Sequence=VSP_059793, VSP_059794;
CC         Note=No experimental confirmation available. May be due to
CC         competing donor splice site in exon 1.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in fetal adrenal, in fetal
CC       testis, fetal smooth, striated and cardiac muscle. Isoform XB-
CC       short is only expressed in the adrenal gland.
CC   -!- DEVELOPMENTAL STAGE: Expression levels are lower in adults than in
CC       children. {ECO:0000269|PubMed:17263730}.
CC   -!- DISEASE: Ehlers-Danlos syndrome, classic-like (EDSCLL)
CC       [MIM:606408]: A form of Ehlers-Danlos syndrome, a group of
CC       connective tissue disorders characterized by skin
CC       hyperextensibility, articular hypermobility, and tissue fragility.
CC       EDSCLL patients lack atrophic scars, a major diagnostic criteria
CC       for classic Ehlers-Danlos syndrome. Delayed wound healing is only
CC       present in a subset of patients. EDSCLL inheritance is autosomal
CC       recessive. {ECO:0000269|PubMed:11642233,
CC       ECO:0000269|PubMed:15733269, ECO:0000269|PubMed:23768946}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Vesicoureteral reflux 8 (VUR8) [MIM:615963]: A disease
CC       belonging to the group of congenital anomalies of the kidney and
CC       urinary tract. It is characterized by the reflux of urine from the
CC       bladder into the ureters and sometimes into the kidneys, and is a
CC       risk factor for urinary tract infections. Primary disease results
CC       from a developmental defect of the ureterovesical junction. In
CC       combination with intrarenal reflux, the resulting inflammatory
CC       reaction may result in renal injury or scarring, also called
CC       reflux nephropathy. Extensive renal scarring impairs renal
CC       function and may predispose patients to hypertension, proteinuria,
CC       renal insufficiency and end-stage renal disease.
CC       {ECO:0000269|PubMed:23620400}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
CC   -!- CAUTION: There are two genes for TN-X: TNXA and TNXB. TNXA can
CC       sometimes recombine with TNXB. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB47488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAB67981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB89296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; U24488; AAB41287.1; -; mRNA.
DR   EMBL; AF019413; AAB67981.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U89337; AAB47488.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL049547; CAB89296.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL049547; CAB89300.1; -; Genomic_DNA.
DR   EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL772248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03574.1; -; Genomic_DNA.
DR   EMBL; BC033740; AAH33740.1; -; mRNA.
DR   EMBL; BC125114; AAI25115.1; -; mRNA.
DR   EMBL; BC125115; AAI25116.1; -; mRNA.
DR   EMBL; BC130037; AAI30038.1; -; mRNA.
DR   EMBL; X71923; CAA50739.1; -; mRNA.
DR   EMBL; Y13782; CAA74109.1; -; mRNA.
DR   EMBL; Y13783; CAA74110.1; -; Genomic_DNA.
DR   EMBL; U52696; AAC50889.1; -; mRNA.
DR   EMBL; AB209012; BAD92249.1; -; mRNA.
DR   EMBL; M25813; AAA35884.1; -; mRNA.
DR   CCDS; CCDS4736.1; -. [P22105-2]
DR   PIR; A40701; A40701.
DR   PIR; A42175; A42175.
DR   PIR; B42175; B42175.
DR   PIR; D42175; D42175.
DR   RefSeq; NP_061978.6; NM_019105.6. [P22105-1]
DR   RefSeq; NP_115859.2; NM_032470.3. [P22105-2]
DR   UniGene; Hs.485104; -.
DR   PDB; 2CUH; NMR; -; A=3845-3946.
DR   PDB; 2CUI; NMR; -; A=3654-3752.
DR   PDB; 2CUM; NMR; -; A=3933-4024.
DR   PDBsum; 2CUH; -.
DR   PDBsum; 2CUI; -.
DR   PDBsum; 2CUM; -.
DR   ProteinModelPortal; P22105; -.
DR   SMR; P22105; -.
DR   BioGrid; 113001; 3.
DR   ComplexPortal; CPX-1014; Tenascin-X complex.
DR   IntAct; P22105; 13.
DR   MINT; P22105; -.
DR   STRING; 9606.ENSP00000407685; -.
DR   GlyConnect; 1794; -.
DR   iPTMnet; P22105; -.
DR   PhosphoSitePlus; P22105; -.
DR   BioMuta; TNXB; -.
DR   DMDM; 290457668; -.
DR   EPD; P22105; -.
DR   jPOST; P22105; -.
DR   PaxDb; P22105; -.
DR   PeptideAtlas; P22105; -.
DR   PRIDE; P22105; -.
DR   ProteomicsDB; 53963; -.
DR   ProteomicsDB; 53964; -. [P22105-2]
DR   ProteomicsDB; 53965; -. [P22105-3]
DR   DNASU; 7148; -.
DR   Ensembl; ENST00000375244; ENSP00000364393; ENSG00000168477. [P22105-3]
DR   Ensembl; ENST00000451343; ENSP00000407685; ENSG00000168477. [P22105-2]
DR   Ensembl; ENST00000546684; ENSP00000447694; ENSG00000236236.
DR   Ensembl; ENST00000550539; ENSP00000448326; ENSG00000229353.
DR   Ensembl; ENST00000644971; ENSP00000496448; ENSG00000168477. [P22105-3]
DR   GeneID; 7148; -.
DR   KEGG; hsa:7148; -.
DR   UCSC; uc003nzg.1; human. [P22105-3]
DR   CTD; 7148; -.
DR   DisGeNET; 7148; -.
DR   EuPathDB; HostDB:ENSG00000168477.17; -.
DR   GeneCards; TNXB; -.
DR   H-InvDB; HIX0165968; -.
DR   H-InvDB; HIX0207682; -.
DR   HGNC; HGNC:11976; TNXB.
DR   MalaCards; TNXB; -.
DR   MIM; 600985; gene.
DR   MIM; 606408; phenotype.
DR   MIM; 615963; phenotype.
DR   neXtProt; NX_P22105; -.
DR   OpenTargets; ENSG00000168477; -.
DR   Orphanet; 230839; Ehlers-Danlos syndrome due to tenascin-X deficiency.
DR   Orphanet; 285; Ehlers-Danlos syndrome, hypermobility type.
DR   Orphanet; 289365; Familial vesicoureteral reflux.
DR   PharmGKB; PA36662; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   eggNOG; ENOG410ZYS4; LUCA.
DR   GeneTree; ENSGT00940000155565; -.
DR   HOVERGEN; HBG006855; -.
DR   InParanoid; P22105; -.
DR   KO; K06252; -.
DR   OMA; PEGHFDH; -.
DR   OrthoDB; 357340at2759; -.
DR   TreeFam; TF329915; -.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   ChiTaRS; TNXB; human.
DR   EvolutionaryTrace; P22105; -.
DR   GeneWiki; Tenascin_X; -.
DR   GenomeRNAi; 7148; -.
DR   PRO; PR:P22105; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000168477; Expressed in 112 organ(s), highest expression level in left adrenal gland.
DR   ExpressionAtlas; P22105; baseline and differential.
DR   Genevisible; P22105; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR   GO; GO:0098633; F:collagen fibril binding; IDA:UniProtKB.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:UniProtKB.
DR   GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB.
DR   CDD; cd00063; FN3; 31.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 2.60.40.10; -; 31.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR020837; Fibrinogen_CS.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR033081; TNX.
DR   PANTHER; PTHR19143:SF244; PTHR19143:SF244; 21.
DR   Pfam; PF07974; EGF_2; 2.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 31.
DR   SMART; SM00181; EGF; 18.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 32.
DR   SUPFAM; SSF49265; SSF49265; 29.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00022; EGF_1; 18.
DR   PROSITE; PS01186; EGF_2; 19.
DR   PROSITE; PS50026; EGF_3; 8.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 32.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Coiled coil;
KW   Complete proteome; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; EGF-like domain; Ehlers-Danlos syndrome;
KW   Extracellular matrix; Glycoprotein; Polymorphism; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   4244       Tenascin-X.
FT                                /FTId=PRO_0000007751.
FT   DOMAIN      156    168       EGF-like 1; incomplete.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      183    213       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      214    244       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      245    275       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      276    306       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      307    337       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      338    368       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      369    399       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      400    430       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      431    461       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      462    492       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      493    523       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      524    554       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      555    585       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      586    616       EGF-like 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      617    647       EGF-like 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      648    679       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      684    714       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      715    746       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      959   1051       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1064   1153       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1161   1249       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1263   1352       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1374   1468       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1476   1572       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1574   1669       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1674   1764       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1778   1868       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1883   1971       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1989   2089       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2097   2185       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2196   2296       Fibronectin type-III 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2305   2398       Fibronectin type-III 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2408   2502       Fibronectin type-III 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2519   2617       Fibronectin type-III 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2625   2723       Fibronectin type-III 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2733   2840       Fibronectin type-III 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2841   2939       Fibronectin type-III 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2949   3042       Fibronectin type-III 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3062   3153       Fibronectin type-III 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3168   3260       Fibronectin type-III 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3264   3355       Fibronectin type-III 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3357   3446       Fibronectin type-III 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3451   3544       Fibronectin type-III 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3553   3647       Fibronectin type-III 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3657   3754       Fibronectin type-III 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3758   3847       Fibronectin type-III 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3848   3934       Fibronectin type-III 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3935   4025       Fibronectin type-III 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4021   4236       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   MOTIF      1666   1668       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3855   3855       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3908   3908       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3920   3920       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4095   4095       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    187    197       {ECO:0000250}.
FT   DISULFID    191    202       {ECO:0000250}.
FT   DISULFID    204    213       {ECO:0000250}.
FT   DISULFID    218    228       {ECO:0000250}.
FT   DISULFID    222    233       {ECO:0000250}.
FT   DISULFID    235    244       {ECO:0000250}.
FT   DISULFID    249    259       {ECO:0000250}.
FT   DISULFID    253    264       {ECO:0000250}.
FT   DISULFID    266    275       {ECO:0000250}.
FT   DISULFID    280    290       {ECO:0000250}.
FT   DISULFID    284    295       {ECO:0000250}.
FT   DISULFID    297    306       {ECO:0000250}.
FT   DISULFID    311    321       {ECO:0000250}.
FT   DISULFID    315    326       {ECO:0000250}.
FT   DISULFID    328    337       {ECO:0000250}.
FT   DISULFID    342    352       {ECO:0000250}.
FT   DISULFID    346    357       {ECO:0000250}.
FT   DISULFID    359    368       {ECO:0000250}.
FT   DISULFID    373    383       {ECO:0000250}.
FT   DISULFID    377    388       {ECO:0000250}.
FT   DISULFID    390    399       {ECO:0000250}.
FT   DISULFID    404    414       {ECO:0000250}.
FT   DISULFID    408    419       {ECO:0000250}.
FT   DISULFID    421    430       {ECO:0000250}.
FT   DISULFID    435    445       {ECO:0000250}.
FT   DISULFID    439    450       {ECO:0000250}.
FT   DISULFID    452    461       {ECO:0000250}.
FT   DISULFID    466    476       {ECO:0000250}.
FT   DISULFID    470    481       {ECO:0000250}.
FT   DISULFID    483    492       {ECO:0000250}.
FT   DISULFID    497    507       {ECO:0000250}.
FT   DISULFID    501    512       {ECO:0000250}.
FT   DISULFID    514    523       {ECO:0000250}.
FT   DISULFID    528    538       {ECO:0000250}.
FT   DISULFID    532    543       {ECO:0000250}.
FT   DISULFID    545    554       {ECO:0000250}.
FT   DISULFID    559    569       {ECO:0000250}.
FT   DISULFID    563    574       {ECO:0000250}.
FT   DISULFID    576    585       {ECO:0000250}.
FT   DISULFID    590    600       {ECO:0000250}.
FT   DISULFID    594    605       {ECO:0000250}.
FT   DISULFID    607    616       {ECO:0000250}.
FT   DISULFID    621    631       {ECO:0000250}.
FT   DISULFID    625    636       {ECO:0000250}.
FT   DISULFID    638    647       {ECO:0000250}.
FT   DISULFID    652    662       {ECO:0000250}.
FT   DISULFID    656    667       {ECO:0000250}.
FT   DISULFID    669    678       {ECO:0000250}.
FT   DISULFID    688    698       {ECO:0000250}.
FT   DISULFID    692    703       {ECO:0000250}.
FT   DISULFID    705    714       {ECO:0000250}.
FT   DISULFID    719    729       {ECO:0000250}.
FT   DISULFID    723    734       {ECO:0000250}.
FT   DISULFID    736    745       {ECO:0000250}.
FT   DISULFID   4030   4060       {ECO:0000250}.
FT   DISULFID   4182   4195       {ECO:0000250}.
FT   VAR_SEQ       1   3571       Missing (in isoform XB-short).
FT                                /FTId=VSP_059792.
FT   VAR_SEQ     135    135       G -> GEQG (in isoform 5).
FT                                /FTId=VSP_059793.
FT   VAR_SEQ    2823   2825       APE -> E (in isoform 3 and isoform 5).
FT                                /FTId=VSP_059794.
FT   VARIANT      29     29       R -> W (in EDSCLL; dbSNP:rs368512272).
FT                                {ECO:0000269|PubMed:15733269}.
FT                                /FTId=VAR_046499.
FT   VARIANT     302    302       T -> A (in dbSNP:rs1150752).
FT                                {ECO:0000269|PubMed:14574404}.
FT                                /FTId=VAR_044347.
FT   VARIANT     511    511       R -> H (in dbSNP:rs204896).
FT                                /FTId=VAR_021908.
FT   VARIANT     641    641       G -> C (in dbSNP:rs17201609).
FT                                /FTId=VAR_055781.
FT   VARIANT     650    650       R -> H (in dbSNP:rs17201602).
FT                                /FTId=VAR_055782.
FT   VARIANT     873    873       S -> A (in dbSNP:rs204900).
FT                                /FTId=VAR_055783.
FT   VARIANT    1108   1108       V -> M (in EDSCLL; dbSNP:rs121912575).
FT                                {ECO:0000269|PubMed:15733269}.
FT                                /FTId=VAR_046500.
FT   VARIANT    1161   1161       H -> R (in dbSNP:rs185819).
FT                                /FTId=VAR_024270.
FT   VARIANT    1244   1244       T -> R (in VUR8).
FT                                {ECO:0000269|PubMed:23620400}.
FT                                /FTId=VAR_072580.
FT   VARIANT    1905   1905       E -> K (in dbSNP:rs17207923).
FT                                /FTId=VAR_059276.
FT   VARIANT    2301   2301       P -> H (in dbSNP:rs2269428).
FT                                /FTId=VAR_020170.
FT   VARIANT    2363   2363       P -> H (in dbSNP:rs2269428).
FT                                /FTId=VAR_055784.
FT   VARIANT    2412   2412       P -> L (in dbSNP:rs12524664).
FT                                /FTId=VAR_059277.
FT   VARIANT    2495   2495       G -> S (in dbSNP:rs2269429).
FT                                /FTId=VAR_020171.
FT   VARIANT    2518   2518       G -> E (in dbSNP:rs1009382).
FT                                {ECO:0000269|PubMed:14574404,
FT                                ECO:0000269|PubMed:14656967}.
FT                                /FTId=VAR_020172.
FT   VARIANT    3212   3212       V -> I (in VUR8; shows significantly
FT                                impaired migration in a wound-healing
FT                                assay; associated with decreased
FT                                expression of phosphorylated PTK2
FT                                protein; dbSNP:rs1473257039).
FT                                {ECO:0000269|PubMed:23620400}.
FT                                /FTId=VAR_072581.
FT   VARIANT    3988   3988       L -> I (in dbSNP:rs7742632).
FT                                {ECO:0000269|PubMed:15733269}.
FT                                /FTId=VAR_046501.
FT   VARIANT    4074   4074       R -> C (in EDSCLL; dbSNP:rs587777682).
FT                                {ECO:0000269|PubMed:23768946}.
FT                                /FTId=VAR_072582.
FT   CONFLICT   3791   3791       Q -> L (in Ref. 5; AAH33740).
FT                                {ECO:0000305}.
FT   CONFLICT   3877   3877       V -> I (in Ref. 5; AAI25115/AAI25116 and
FT                                10; BAD92249). {ECO:0000305}.
FT   CONFLICT   3974   3974       N -> T (in Ref. 5; AAI25115/AAI25116 and
FT                                10; BAD92249). {ECO:0000305}.
FT   CONFLICT   3993   3993       P -> G (in Ref. 1; AAB41287 and 11;
FT                                AAA35884). {ECO:0000305}.
FT   CONFLICT   4004   4004       M -> T (in Ref. 5; AAI25116 and 10;
FT                                BAD92249). {ECO:0000305}.
FT   CONFLICT   4057   4057       N -> I (in Ref. 5; AAI25115).
FT                                {ECO:0000305}.
FT   CONFLICT   4118   4118       M -> I (in Ref. 1; AAB41287 and 11;
FT                                AAA35884). {ECO:0000305}.
FT   STRAND     3662   3665       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3671   3674       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3683   3690       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3695   3697       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3707   3712       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3717   3720       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3728   3736       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3738   3750       {ECO:0000244|PDB:2CUI}.
FT   STRAND     3849   3852       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3857   3859       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3861   3866       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3873   3880       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3882   3884       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3887   3892       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3896   3900       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3905   3917       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3925   3931       {ECO:0000244|PDB:2CUH}.
FT   TURN       3936   3938       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3939   3941       {ECO:0000244|PDB:2CUH}.
FT   STRAND     3949   3954       {ECO:0000244|PDB:2CUM}.
FT   STRAND     3961   3968       {ECO:0000244|PDB:2CUM}.
FT   STRAND     3974   3979       {ECO:0000244|PDB:2CUM}.
FT   STRAND     3984   3988       {ECO:0000244|PDB:2CUM}.
FT   STRAND     3996   4005       {ECO:0000244|PDB:2CUM}.
FT   STRAND     4013   4018       {ECO:0000244|PDB:2CUM}.
SQ   SEQUENCE   4244 AA;  458388 MW;  45A3D29FDF133DBA CRC64;
     MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA GVGSPSSQLY
     EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV QALRVRLEIL EELVKGLKEQ
     CTGGCCPASA QAGTGQTDVR TLCSLHGVFD LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP
     PSASGSCPDD CNDQGRCVRG RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS
     GPDCSQRSCP RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG
     YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG RCVDGRCVCW
     PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG VRSCPGDCNQ RGRCEDGRCV
     CWPGYTGTDC GSRACPRDCR GRGRCENGVC VCNAGYSGED CGVRSCPGDC RGRGRCESGR
     CMCWPGYTGR DCGTRACPGD CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED
     GVCVCDAGYS GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC
     QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR MCPADCRGRG
     RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA GQCVCVEGFR GPDCAIQTCP
     GDCRGRGECH DGSCVCKDGY AGEDCGEEVP TIEGMRMHLL EETTVRTEWT PAPGPVDAYE
     IQFIPTTEGA SPPFTARVPS SASAYDQRGL APGQEYQVTV RALRGTSWGL PASKTITTMI
     DGPQDLRVVA VTPTTLELGW LRPQAEVDRF VVSYVSAGNQ RVRLEVPPEA DGTLLTDLMP
     GVEYVVTVTA ERGRAVSYPA SVRANTGSSP LGLLGTTDEP PPSGPSTTQG AQAPLLQQRP
     QELGELRVLG RDETGRLRVV WTAQPDTFAY FQLRMRVPEG PGAHEEVLPG DVRQALVPPP
     PPGTPYELSL HGVPPGGKPS DPIIYQGIMD KDEEKPGKSS GPPRLGELTV TDRTSDSLLL
     RWTVPEGEFD SFVIQYKDRD GQPQVVPVEG PQRSAVITSL DPGRKYKFVL YGFVGKKRHG
     PLVAEAKILP QSDPSPGTPP HLGNLWVTDP TPDSLHLSWT VPEGQFDTFM VQYRDRDGRP
     QVVPVEGPER SFVVSSLDPD HKYRFTLFGI ANKKRYGPLT ADGTTAPERK EEPPRPEFLE
     QPLLGELTVT GVTPDSLRLS WTVAQGPFDS FMVQYKDAQG QPQAVPVAGD ENEVTVPGLD
     PDRKYKMNLY GLRGRQRVGP ESVVAKTAPQ EDVDETPSPT ELGTEAPESP EEPLLGELTV
     TGSSPDSLSL FWTVPQGSFD SFTVQYKDRD GRPRAVRVGG KESEVTVGGL EPGHKYKMHL
     YGLHEGQRVG PVSAVGVTAP QQEETPPATE SPLEPRLGEL TVTDVTPNSV GLSWTVPEGQ
     FDSFIVQYKD KDGQPQVVPV AADQREVTVY NLEPERKYKM NMYGLHDGQR MGPLSVVIVT
     APLPPAPATE ASKPPLEPRL GELTVTDITP DSVGLSWTVP EGEFDSFVVQ YKDRDGQPQV
     VPVAADQREV TIPDLEPSRK YKFLLFGIQD GKRRSPVSVE AKTVARGDAS PGAPPRLGEL
     WVTDPTPDSL RLSWTVPEGQ FDSFVVQFKD KDGPQVVPVE GHERSVTVTP LDAGRKYRFL
     LYGLLGKKRH GPLTADGTTE ARSAMDDTGT KRPPKPRLGE ELQVTTVTQN SVGLSWTVPE
     GQFDSFVVQY KDRDGQPQVV PVEGSLREVS VPGLDPAHRY KLLLYGLHHG KRVGPISAVA
     ITAGREETET ETTAPTPPAP EPHLGELTVE EATSHTLHLS WMVTEGEFDS FEIQYTDRDG
     QLQMVRIGGD RNDITLSGLE SDHRYLVTLY GFSDGKHVGP VHVEALTVPE EEKPSEPPTA
     TPEPPIKPRL GELTVTDATP DSLSLSWTVP EGQFDHFLVQ YRNGDGQPKA VRVPGHEEGV
     TISGLEPDHK YKMNLYGFHG GQRMGPVSVV GVTAAEEETP SPTEPSMEAP EPAEEPLLGE
     LTVTGSSPDS LSLSWTVPQG RFDSFTVQYK DRDGRPQVVR VGGEESEVTV GGLEPGRKYK
     MHLYGLHEGR RVGPVSAVGV TAPEEESPDA PLAKLRLGQM TVRDITSDSL SLSWTVPEGQ
     FDHFLVQFKN GDGQPKAVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPVSAVGLT
     APGKDEEMAP ASTEPPTPEP PIKPRLEELT VTDATPDSLS LSWTVPEGQF DHFLVQYKNG
     DGQPKATRVP GHEDRVTISG LEPDNKYKMN LYGFHGGQRV GPVSAIGVTA AEEETPSPTE
     PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG RPQVVRVGGE
     ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP
     EEPLLGELTV TGSSPDSLSL SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL
     EPGRKYKMHL YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT
     PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH
     GGQRVGPISV IGVTAAEEET PSPTELSTEA PEPPEEPLLG ELTVTGSSPD SLSLSWTIPQ
     GHFDSFTVQY KDRDGRPQVM RVRGEESEVT VGGLEPGRKY KMHLYGLHEG RRVGPVSTVG
     VTAPEDEAET TQAVPTTTPE PPNKPRLGEL TVTDATPDSL SLSWMVPEGQ FDHFLVQYRN
     GDGQPKVVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPISVIGVT AAEEETPAPT
     EPSTEAPEPP EEPLLGELTV TGSSPDSLSL SWTIPQGRFD SFTVQYKDRD GRPQVVRVRG
     EESEVTVGGL EPGCKYKMHL YGLHEGQRVG PVSAVGVTAP KDEAETTQAV PTMTPEPPIK
     PRLGELTVTD ATPDSLSLSW MVPEGQFDHF LVQYRNGDGQ PKAVRVPGHE DGVTISGLEP
     DHKYKMNLYG FHGGQRVGPV SAIGVTEEET PSPTEPSTEA PEAPEEPLLG ELTVTGSSPD
     SLSLSWTVPQ GRFDSFTVQY KDRDGQPQVV RVRGEESEVT VGGLEPGRKY KMHLYGLHEG
     QRVGPVSTVG ITAPLPTPLP VEPRLGELAV AAVTSDSVGL SWTVAQGPFD SFLVQYRDAQ
     GQPQAVPVSG DLRAVAVSGL DPARKYKFLL FGLQNGKRHG PVPVEARTAP DTKPSPRLGE
     LTVTDATPDS VGLSWTVPEG EFDSFVVQYK DKDGRLQVVP VAANQREVTV QGLEPSRKYR
     FLLYGLSGRK RLGPISADST TAPLEKELPP HLGELTVAEE TSSSLRLSWT VAQGPFDSFV
     VQYRDTDGQP RAVPVAADQR TVTVEDLEPG KKYKFLLYGL LGGKRLGPVS ALGMTAPEED
     TPAPELAPEA PEPPEEPRLG VLTVTDTTPD SMRLSWSVAQ GPFDSFVVQY EDTNGQPQAL
     LVDGDQSKIL ISGLEPSTPY RFLLYGLHEG KRLGPLSAEG TTGLAPAGQT SEESRPRLSQ
     LSVTDVTTSS LRLNWEAPPG AFDSFLLRFG VPSPSTLEPH PRPLLQRELM VPGTRHSAVL
     RDLRSGTLYS LTLYGLRGPH KADSIQGTAR TLSPVLESPR DLQFSEIRET SAKVNWMPPP
     SRADSFKVSY QLADGGEPQS VQVDGQARTQ KLQGLIPGAR YEVTVVSVRG FEESEPLTGF
     LTTVPDGPTQ LRALNLTEGF AVLHWKPPQN PVDTYDVQVT APGAPPLQAE TPGSAVDYPL
     HDLVLHTNYT ATVRGLRGPN LTSPASITFT TGLEAPRDLE AKEVTPRTAL LTWTEPPVRP
     AGYLLSFHTP GGQNQEILLP GGITSHQLLG LFPSTSYNAR LQAMWGQSLL PPVSTSFTTG
     GLRIPFPRDC GEEMQNGAGA SRTSTIFLNG NRERPLNVFC DMETDGGGWL VFQRRMDGQT
     DFWRDWEDYA HGFGNISGEF WLGNEALHSL TQAGDYSMRV DLRAGDEAVF AQYDSFHVDS
     AAEYYRLHLE GYHGTAGDSM SYHSGSVFSA RDRDPNSLLI SCAVSYRGAW WYRNCHYANL
     NGLYGSTVDH QGVSWYHWKG FEFSVPFTEM KLRPRNFRSP AGGG
//
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