TENX_HUMAN
ID TENX_HUMAN Reviewed; 4244 AA.
AC P22105; P78530; P78531; Q08424; Q08AM0; Q08AM1; Q59GU7; Q5SQD3; Q5ST74;
AC Q7L8Q4; Q8N4R1; Q9NPK9; Q9UC10; Q9UC11; Q9UC12; Q9UC13; Q9UMG7;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 5.
DT 03-AUG-2022, entry version 230.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 overlapping
RT P450c21A correctly predict the presence of a novel, adrenal-specific,
RT 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., Campbell R.D.,
RA 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 AND
RP 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 SEQUENCE
RP [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 XB
RT 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 gene
RT 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 AND
RP 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 with
RT 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; 2549-2557;
RP 2763-2771; 2782-2799; 2979-2987; 3018-3028; 3193-3201; 3212-3229 AND
RP 3232-3242 (ISOFORMS 3/4/5), PROTEIN SEQUENCE OF 3609-3621 AND 3633-3665
RP (ISOFORMS XB-SHORT/3/4/5), INTERACTION WITH TROPOELASTIN, AND DEVELOPMENTAL
RP 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 in
RT 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., 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 [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., Schalkwijk J.;
RT "Interactions of human tenascin-X domains with dermal extracellular matrix
RT 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., 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 STRUCTURE BY NMR OF 3654-4024.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 29th, 31st and 33rd fibronectin type-III domains
RT 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 syndrome
RT 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., Schalkwijk J.,
RA van Vlijmen-Willems I., Gartioux C., Malfait F., Syx D., Macchi L.,
RA Marcorelles P., Arbeille B., Croue A., De Paepe A., Dubas F.;
RT "Compound heterozygous mutations of the TNXB gene cause primary 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., Hains D.,
RA Bartkowiak B., Rabinovich C.E., Chandrasekharappa S., Homstad A.,
RA Westreich K., Wu G., Liu Y., Holanda D., Clarke J., Lavin P., Selim A.,
RA Miller S., Wiener J.S., Ross S.S., Foreman J., 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 play
CC 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 and
CC tropoelastin via its 29th fibronectin type-III domain.
CC {ECO:0000269|PubMed:17033827, ECO:0000269|PubMed:17263730}.
CC -!- INTERACTION:
CC P22105; Q8N9N5: BANP; NbExp=4; IntAct=EBI-2821024, EBI-744695;
CC P22105-1; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-20753895, EBI-11524452;
CC P22105-1; P40199: CEACAM6; NbExp=3; IntAct=EBI-20753895, EBI-4314501;
CC P22105-1; P42858: HTT; NbExp=3; IntAct=EBI-20753895, EBI-466029;
CC P22105-1; P78424: POU6F2; NbExp=3; IntAct=EBI-20753895, EBI-12029004;
CC P22105-1; Q96PF1: TGM7; NbExp=3; IntAct=EBI-20753895, EBI-12029034;
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 Name=3;
CC IsoId=P22105-1; Sequence=VSP_059794;
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 -!- TISSUE SPECIFICITY: Highly expressed in fetal adrenal, in fetal testis,
CC fetal smooth, striated and cardiac muscle. Isoform XB-short is only
CC 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) [MIM:606408]: A
CC form of Ehlers-Danlos syndrome, a group of connective tissue disorders
CC characterized by skin hyperextensibility, articular hypermobility, and
CC tissue fragility. EDSCLL patients lack atrophic scars, a major
CC diagnostic criteria for classic Ehlers-Danlos syndrome. Delayed wound
CC healing is only present in a subset of patients. EDSCLL inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:11642233,
CC ECO:0000269|PubMed:15733269, ECO:0000269|PubMed:23768946}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 risk
CC factor for urinary tract infections. Primary disease results from a
CC developmental defect of the ureterovesical junction. In combination
CC with intrarenal reflux, the resulting inflammatory reaction may result
CC in renal injury or scarring, also called reflux nephropathy. Extensive
CC renal scarring impairs renal function and may predispose patients to
CC hypertension, proteinuria, renal insufficiency and end-stage renal
CC disease. {ECO:0000269|PubMed:23620400}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to competing acceptor splice
CC site in exon 24.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to competing donor splice site
CC in exon 1. {ECO:0000305}.
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};
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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 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 SMR; P22105; -.
DR BioGRID; 113001; 45.
DR ComplexPortal; CPX-1014; Tenascin-X complex.
DR IntAct; P22105; 14.
DR MINT; P22105; -.
DR STRING; 9606.ENSP00000407685; -.
DR GlyConnect; 1794; 7 N-Linked glycans (3 sites).
DR GlyGen; P22105; 43 sites, 6 N-linked glycans (2 sites), 7 O-linked glycans (38 sites).
DR iPTMnet; P22105; -.
DR PhosphoSitePlus; P22105; -.
DR BioMuta; TNXB; -.
DR DMDM; 290457668; -.
DR CPTAC; non-CPTAC-2701; -.
DR EPD; P22105; -.
DR jPOST; P22105; -.
DR MassIVE; P22105; -.
DR MaxQB; P22105; -.
DR PaxDb; P22105; -.
DR PeptideAtlas; P22105; -.
DR PRIDE; P22105; -.
DR ProteomicsDB; 53963; -. [P22105-1]
DR ProteomicsDB; 53964; -. [P22105-2]
DR ProteomicsDB; 53965; -. [P22105-3]
DR Antibodypedia; 3947; 230 antibodies from 31 providers.
DR DNASU; 7148; -.
DR Ensembl; ENST00000375244.7; ENSP00000364393.3; ENSG00000168477.19. [P22105-3]
DR Ensembl; ENST00000451343.4; ENSP00000407685.1; ENSG00000168477.19. [P22105-2]
DR Ensembl; ENST00000546684.2; ENSP00000447694.2; ENSG00000236236.9.
DR Ensembl; ENST00000550539.2; ENSP00000448326.2; ENSG00000229353.10.
DR Ensembl; ENST00000644971.2; ENSP00000496448.1; ENSG00000168477.19. [P22105-3]
DR GeneID; 7148; -.
DR KEGG; hsa:7148; -.
DR MANE-Select; ENST00000644971.2; ENSP00000496448.1; NM_001365276.2; NP_001352205.1.
DR UCSC; uc003nzg.1; human. [P22105-3]
DR CTD; 7148; -.
DR DisGeNET; 7148; -.
DR GeneCards; TNXB; -.
DR HGNC; HGNC:11976; TNXB.
DR HPA; ENSG00000168477; Tissue enriched (adrenal).
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; Classical-like Ehlers-Danlos syndrome type 1.
DR Orphanet; 289365; Familial vesicoureteral reflux.
DR PharmGKB; PA36662; -.
DR VEuPathDB; HostDB:ENSG00000168477; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000155565; -.
DR HOGENOM; CLU_026380_0_0_1; -.
DR InParanoid; P22105; -.
DR TreeFam; TF329915; -.
DR PathwayCommons; P22105; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; P22105; -.
DR BioGRID-ORCS; 7148; 16 hits in 1074 CRISPR screens.
DR ChiTaRS; TNXB; human.
DR EvolutionaryTrace; P22105; -.
DR GeneWiki; Tenascin_X; -.
DR GenomeRNAi; 7148; -.
DR Pharos; P22105; Tbio.
DR PRO; PR:P22105; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P22105; protein.
DR Bgee; ENSG00000168477; Expressed in apex of heart and 96 other tissues.
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:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0098633; F:collagen fibril binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS: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:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IMP:UniProtKB.
DR GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:1905935; P:positive regulation of cell fate determination; IC:ComplexPortal.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IDA:ComplexPortal.
DR GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0045595; P:regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0043506; P:regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR CDD; cd00063; FN3; 31.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 31.
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; 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; PTHR46708:SF3; PTHR46708:SF3; 12.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF18720; EGF_Tenascin; 10.
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 Direct protein sequencing; Disease variant; Disulfide bond;
KW EGF-like domain; Ehlers-Danlos syndrome; Extracellular matrix;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..4244
FT /note="Tenascin-X"
FT /id="PRO_0000007751"
FT DOMAIN 156..168
FT /note="EGF-like 1; incomplete"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 183..213
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..244
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 245..275
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 276..306
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 307..337
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 338..368
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 369..399
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 400..430
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 431..461
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 462..492
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 493..523
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 524..554
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 555..585
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 586..616
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 617..647
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 648..679
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 684..714
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 715..746
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 959..1051
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1064..1153
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1161..1249
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1263..1352
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1374..1468
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1476..1572
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1574..1669
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1674..1764
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1778..1868
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1883..1971
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1989..2089
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2097..2185
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2196..2296
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2305..2398
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2408..2502
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2519..2617
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2625..2723
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2733..2840
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2841..2939
FT /note="Fibronectin type-III 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2949..3042
FT /note="Fibronectin type-III 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3062..3153
FT /note="Fibronectin type-III 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3168..3260
FT /note="Fibronectin type-III 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3264..3355
FT /note="Fibronectin type-III 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3357..3446
FT /note="Fibronectin type-III 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3451..3544
FT /note="Fibronectin type-III 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3553..3647
FT /note="Fibronectin type-III 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3657..3754
FT /note="Fibronectin type-III 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3758..3847
FT /note="Fibronectin type-III 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3848..3934
FT /note="Fibronectin type-III 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3935..4025
FT /note="Fibronectin type-III 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4021..4236
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 27..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2281..2304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2495..2542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2824..2847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2933..2969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3536..3559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3636..3662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1666..1668
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 940..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3643..3662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4095
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 187..197
FT /evidence="ECO:0000250"
FT DISULFID 191..202
FT /evidence="ECO:0000250"
FT DISULFID 204..213
FT /evidence="ECO:0000250"
FT DISULFID 218..228
FT /evidence="ECO:0000250"
FT DISULFID 222..233
FT /evidence="ECO:0000250"
FT DISULFID 235..244
FT /evidence="ECO:0000250"
FT DISULFID 249..259
FT /evidence="ECO:0000250"
FT DISULFID 253..264
FT /evidence="ECO:0000250"
FT DISULFID 266..275
FT /evidence="ECO:0000250"
FT DISULFID 280..290
FT /evidence="ECO:0000250"
FT DISULFID 284..295
FT /evidence="ECO:0000250"
FT DISULFID 297..306
FT /evidence="ECO:0000250"
FT DISULFID 311..321
FT /evidence="ECO:0000250"
FT DISULFID 315..326
FT /evidence="ECO:0000250"
FT DISULFID 328..337
FT /evidence="ECO:0000250"
FT DISULFID 342..352
FT /evidence="ECO:0000250"
FT DISULFID 346..357
FT /evidence="ECO:0000250"
FT DISULFID 359..368
FT /evidence="ECO:0000250"
FT DISULFID 373..383
FT /evidence="ECO:0000250"
FT DISULFID 377..388
FT /evidence="ECO:0000250"
FT DISULFID 390..399
FT /evidence="ECO:0000250"
FT DISULFID 404..414
FT /evidence="ECO:0000250"
FT DISULFID 408..419
FT /evidence="ECO:0000250"
FT DISULFID 421..430
FT /evidence="ECO:0000250"
FT DISULFID 435..445
FT /evidence="ECO:0000250"
FT DISULFID 439..450
FT /evidence="ECO:0000250"
FT DISULFID 452..461
FT /evidence="ECO:0000250"
FT DISULFID 466..476
FT /evidence="ECO:0000250"
FT DISULFID 470..481
FT /evidence="ECO:0000250"
FT DISULFID 483..492
FT /evidence="ECO:0000250"
FT DISULFID 497..507
FT /evidence="ECO:0000250"
FT DISULFID 501..512
FT /evidence="ECO:0000250"
FT DISULFID 514..523
FT /evidence="ECO:0000250"
FT DISULFID 528..538
FT /evidence="ECO:0000250"
FT DISULFID 532..543
FT /evidence="ECO:0000250"
FT DISULFID 545..554
FT /evidence="ECO:0000250"
FT DISULFID 559..569
FT /evidence="ECO:0000250"
FT DISULFID 563..574
FT /evidence="ECO:0000250"
FT DISULFID 576..585
FT /evidence="ECO:0000250"
FT DISULFID 590..600
FT /evidence="ECO:0000250"
FT DISULFID 594..605
FT /evidence="ECO:0000250"
FT DISULFID 607..616
FT /evidence="ECO:0000250"
FT DISULFID 621..631
FT /evidence="ECO:0000250"
FT DISULFID 625..636
FT /evidence="ECO:0000250"
FT DISULFID 638..647
FT /evidence="ECO:0000250"
FT DISULFID 652..662
FT /evidence="ECO:0000250"
FT DISULFID 656..667
FT /evidence="ECO:0000250"
FT DISULFID 669..678
FT /evidence="ECO:0000250"
FT DISULFID 688..698
FT /evidence="ECO:0000250"
FT DISULFID 692..703
FT /evidence="ECO:0000250"
FT DISULFID 705..714
FT /evidence="ECO:0000250"
FT DISULFID 719..729
FT /evidence="ECO:0000250"
FT DISULFID 723..734
FT /evidence="ECO:0000250"
FT DISULFID 736..745
FT /evidence="ECO:0000250"
FT DISULFID 4030..4060
FT /evidence="ECO:0000250"
FT DISULFID 4182..4195
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..3571
FT /note="Missing (in isoform XB-short)"
FT /id="VSP_059792"
FT VAR_SEQ 135
FT /note="G -> GEQG (in isoform 5)"
FT /id="VSP_059793"
FT VAR_SEQ 2823..2825
FT /note="APE -> E (in isoform 3 and isoform 5)"
FT /id="VSP_059794"
FT VARIANT 29
FT /note="R -> W (in EDSCLL; dbSNP:rs368512272)"
FT /evidence="ECO:0000269|PubMed:15733269"
FT /id="VAR_046499"
FT VARIANT 302
FT /note="T -> A (in dbSNP:rs1150752)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_044347"
FT VARIANT 511
FT /note="R -> H (in dbSNP:rs204896)"
FT /id="VAR_021908"
FT VARIANT 641
FT /note="G -> C (in dbSNP:rs17201609)"
FT /id="VAR_055781"
FT VARIANT 650
FT /note="R -> H (in dbSNP:rs17201602)"
FT /id="VAR_055782"
FT VARIANT 873
FT /note="S -> A (in dbSNP:rs204900)"
FT /id="VAR_055783"
FT VARIANT 1108
FT /note="V -> M (in EDSCLL; dbSNP:rs121912575)"
FT /evidence="ECO:0000269|PubMed:15733269"
FT /id="VAR_046500"
FT VARIANT 1161
FT /note="H -> R (in dbSNP:rs185819)"
FT /id="VAR_024270"
FT VARIANT 1244
FT /note="T -> R (in VUR8)"
FT /evidence="ECO:0000269|PubMed:23620400"
FT /id="VAR_072580"
FT VARIANT 1905
FT /note="E -> K (in dbSNP:rs17207923)"
FT /id="VAR_059276"
FT VARIANT 2301
FT /note="P -> H (in dbSNP:rs2269428)"
FT /id="VAR_020170"
FT VARIANT 2363
FT /note="P -> H (in dbSNP:rs2269428)"
FT /id="VAR_055784"
FT VARIANT 2412
FT /note="P -> L (in dbSNP:rs12524664)"
FT /id="VAR_059277"
FT VARIANT 2495
FT /note="G -> S (in dbSNP:rs2269429)"
FT /id="VAR_020171"
FT VARIANT 2518
FT /note="G -> E (in dbSNP:rs1009382)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14656967"
FT /id="VAR_020172"
FT VARIANT 3212
FT /note="V -> I (in VUR8; shows significantly impaired
FT migration in a wound-healing assay; associated with
FT decreased expression of phosphorylated PTK2 protein;
FT dbSNP:rs1473257039)"
FT /evidence="ECO:0000269|PubMed:23620400"
FT /id="VAR_072581"
FT VARIANT 3988
FT /note="L -> I (in dbSNP:rs7742632)"
FT /evidence="ECO:0000269|PubMed:15733269"
FT /id="VAR_046501"
FT VARIANT 4074
FT /note="R -> C (in EDSCLL; dbSNP:rs587777682)"
FT /evidence="ECO:0000269|PubMed:23768946"
FT /id="VAR_072582"
FT CONFLICT 3791
FT /note="Q -> L (in Ref. 5; AAH33740)"
FT /evidence="ECO:0000305"
FT CONFLICT 3877
FT /note="V -> I (in Ref. 5; AAI25115/AAI25116 and 10;
FT BAD92249)"
FT /evidence="ECO:0000305"
FT CONFLICT 3974
FT /note="N -> T (in Ref. 5; AAI25115/AAI25116 and 10;
FT BAD92249)"
FT /evidence="ECO:0000305"
FT CONFLICT 3993
FT /note="P -> G (in Ref. 1; AAB41287 and 11; AAA35884)"
FT /evidence="ECO:0000305"
FT CONFLICT 4004
FT /note="M -> T (in Ref. 5; AAI25116 and 10; BAD92249)"
FT /evidence="ECO:0000305"
FT CONFLICT 4057
FT /note="N -> I (in Ref. 5; AAI25115)"
FT /evidence="ECO:0000305"
FT CONFLICT 4118
FT /note="M -> I (in Ref. 1; AAB41287 and 11; AAA35884)"
FT /evidence="ECO:0000305"
FT STRAND 3662..3665
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3671..3674
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3683..3690
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3695..3697
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3707..3712
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3717..3720
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3728..3736
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3738..3750
FT /evidence="ECO:0007829|PDB:2CUI"
FT STRAND 3849..3852
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3857..3859
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3861..3866
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3873..3880
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3882..3884
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3887..3892
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3896..3900
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3905..3917
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3925..3931
FT /evidence="ECO:0007829|PDB:2CUH"
FT TURN 3936..3938
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3939..3941
FT /evidence="ECO:0007829|PDB:2CUH"
FT STRAND 3949..3954
FT /evidence="ECO:0007829|PDB:2CUM"
FT STRAND 3961..3968
FT /evidence="ECO:0007829|PDB:2CUM"
FT STRAND 3974..3979
FT /evidence="ECO:0007829|PDB:2CUM"
FT STRAND 3984..3988
FT /evidence="ECO:0007829|PDB:2CUM"
FT STRAND 3996..4005
FT /evidence="ECO:0007829|PDB:2CUM"
FT STRAND 4013..4018
FT /evidence="ECO:0007829|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
