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 27-MAR-2024, entry version 239. 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; P01137: TGFB1; NbExp=3; IntAct=EBI-2821024, EBI-779636; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 CCDS; CCDS93886.1; -. [P22105-3] 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; 16. DR MINT; P22105; -. DR STRING; 9606.ENSP00000407685; -. DR GlyConnect; 1794; 7 N-Linked glycans (3 sites). DR GlyCosmos; P22105; 43 sites, 13 glycans. DR GlyGen; P22105; 44 sites, 6 N-linked glycans (2 sites), 8 O-linked glycans (39 sites). DR iPTMnet; P22105; -. DR PhosphoSitePlus; P22105; -. DR SwissPalm; 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; 9606-ENSP00000407685; -. DR PeptideAtlas; P22105; -. DR ProteomicsDB; 53963; -. [P22105-1] DR ProteomicsDB; 53964; -. [P22105-2] DR ProteomicsDB; 53965; -. [P22105-3] DR Pumba; P22105; -. DR Antibodypedia; 3947; 265 antibodies from 31 providers. DR DNASU; 7148; -. DR Ensembl; ENST00000375244.7; ENSP00000364393.3; ENSG00000168477.21. [P22105-3] DR Ensembl; ENST00000451343.4; ENSP00000407685.1; ENSG00000168477.21. [P22105-2] DR Ensembl; ENST00000546684.2; ENSP00000447694.2; ENSG00000236236.9. DR Ensembl; ENST00000550539.2; ENSP00000448326.2; ENSG00000229353.10. DR Ensembl; ENST00000644971.2; ENSP00000496448.1; ENSG00000168477.21. [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 AGR; HGNC:11976; -. DR CTD; 7148; -. DR DisGeNET; 7148; -. DR GeneCards; TNXB; -. DR GeneReviews; TNXB; -. DR HGNC; HGNC:11976; TNXB. DR HPA; ENSG00000168477; Tissue enhanced (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 OrthoDB; 4251562at2759; -. DR TreeFam; TF329915; -. DR PathwayCommons; P22105; -. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR SignaLink; P22105; -. DR BioGRID-ORCS; 7148; 16 hits in 1152 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 98 other cell types or tissues. DR ExpressionAtlas; P22105; baseline and differential. 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0090733; C:tenascin complex; ISO:ComplexPortal. 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:0006631; P:fatty acid metabolic process; IEA:Ensembl. DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central. DR GO; GO:1905935; P:positive regulation of cell fate determination; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:ComplexPortal. DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IDA:ComplexPortal. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:ComplexPortal. DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:ComplexPortal. DR GO; GO:0030155; P:regulation of cell adhesion; ISO:ComplexPortal. DR GO; GO:0045595; P:regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0030334; P:regulation of cell migration; ISO:ComplexPortal. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR CDD; cd00054; EGF_CA; 5. DR CDD; cd00063; FN3; 31. DR CDD; cd00087; FReD; 1. DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 31. DR Gene3D; 2.10.25.10; Laminin; 17. 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 PANTHER; PTHR46708; TENASCIN; 1. DR PANTHER; PTHR46708:SF3; TENASCIN-X; 1. 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; SSF56496; Fibrinogen C-terminal domain-like; 1. DR SUPFAM; SSF49265; Fibronectin type III; 29. 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. DR Genevisible; P22105; HS. 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; 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 //