ID CO7A1_HUMAN Reviewed; 2944 AA. AC Q02388; Q14054; Q16507; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 250. DE RecName: Full=Collagen alpha-1(VII) chain; DE AltName: Full=Long-chain collagen; DE Short=LC collagen; DE Flags: Precursor; GN Name=COL7A1; 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 [GENOMIC DNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=8088784; DOI=10.1006/geno.1994.1239; RA Christiano A.M., Hoffman G.G., Chung-Honet L.C., Lee S., Cheng W., RA Uitto J., Greenspan D.S.; RT "Structural organization of the human type VII collagen gene (COL7A1), RT composed of more exons than any previously characterized gene."; RL Genomics 21:169-179(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND HYDROXYLATION AT PRO-2167; RP PRO-2176; PRO-2185; PRO-2188; LYS-2625; LYS-2631; PRO-2664; PRO-2667 AND RP PRO-2673. RX PubMed=8051117; DOI=10.1016/s0021-9258(17)31984-1; RA Christiano A.M., Greenspan D.S., Lee S., Uitto J.; RT "Cloning of human type VII collagen. Complete primary sequence of the alpha RT 1(VII) chain and identification of intragenic polymorphisms."; RL J. Biol. Chem. 269:20256-20262(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-1493, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1307247; DOI=10.1093/hmg/1.7.475; RA Christiano A.M., Rosenbaum L.M., Chung-Honet L.C., Parente M.G., RA Woodley D.T., Pan T.C., Zhang R.Z., Chu M.-L., Burgeson R.E., Uitto J.; RT "The large non-collagenous domain (NC-1) of type VII collagen is amino- RT terminal and chimeric. Homology to cartilage matrix protein, the type III RT domains of fibronectin and the A domains of von Willebrand factor."; RL Hum. Mol. Genet. 1:475-481(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 195-1275. RC TISSUE=Keratinocyte; RX PubMed=1567409; DOI=10.1016/s0006-291x(05)80283-9; RA Tanaka T., Takahashi K., Furukawa F., Imamura S.; RT "Molecular cloning and characterization of type VII collagen cDNA."; RL Biochem. Biophys. Res. Commun. 183:958-963(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 369-1255. RX PubMed=1469284; DOI=10.1111/1523-1747.ep12614080; RA Gammon W.R., Abernethy M.L., Padilla K.M., Prisayanh P.S., Cook M.E., RA Wright J., Briggaman R.A., Hunt S.W. III; RT "Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion RT proteins involved in tissue-specific organization of extracellular RT matrix."; RL J. Invest. Dermatol. 99:691-696(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 815-1439. RX PubMed=1871109; DOI=10.1073/pnas.88.16.6931; RA Parente M.G., Chung L.C., Ryynaenen J., Woodley D.T., Wynn K.W., RA Bauer E.A., Mattei M.-G., Chu M.-L., Uitto J.; RT "Human type VII collagen: cDNA cloning and chromosomal mapping of the RT gene."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6931-6935(1991). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2395-2944. RX PubMed=8499916; DOI=10.1093/hmg/2.3.273; RA Greenspan D.S.; RT "The carboxyl-terminal half of type VII collagen, including the non- RT collagenous NC-2 domain and intron/exon organization of the corresponding RT region of the COL7A1 gene."; RL Hum. Mol. Genet. 2:273-278(1993). RN [8] RP PARTIAL PROTEIN SEQUENCE, AND HYDROXYLATION AT PRO-2036; PRO-2039; RP PRO-2084; PRO-2087 AND PRO-2090. RX PubMed=2537292; DOI=10.1016/s0021-9258(19)84924-4; RA Seltzer J.L., Eisen A.Z., Bauer E.A., Morris N.P., Glanville R.W., RA Burgeson R.E.; RT "Cleavage of type VII collagen by interstitial collagenase and type IV RT collagenase (gelatinase) derived from human skin."; RL J. Biol. Chem. 264:3822-3826(1989). RN [9] RP INTERACTION WITH MIA3. RX PubMed=19269366; DOI=10.1016/j.cell.2008.12.025; RA Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., RA Schekman R., Malhotra V.; RT "TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites."; RL Cell 136:891-902(2009). RN [10] RP REVIEW ON VARIANTS. RX PubMed=9375848; RX DOI=10.1002/(sici)1098-1004(1997)10:5<338::aid-humu2>3.0.co;2-b; RA Jaervikallio A., Pulkkinen L., Uitto J.; RT "Molecular basis of dystrophic epidermolysis bullosa: mutations in the type RT VII collagen gene (COL7A1)."; RL Hum. Mutat. 10:338-347(1997). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP VARIANT EBDSC ARG-2034. RX PubMed=2653224; DOI=10.1001/archderm.125.5.633; RA Fine J.-D., Johnson L., Wright T.; RT "Epidermolysis bullosa simplex superficialis. A new variant of RT epidermolysis bullosa characterized by subcorneal skin cleavage mimicking RT peeling skin syndrome."; RL Arch. Dermatol. 125:633-638(1989). RN [13] RP VARIANT RDEB LYS-2798. RX PubMed=8513326; DOI=10.1038/ng0593-62; RA Christiano A.M., Greenspan D.S., Hoffman G.G., Zhang X., Tamai Y., RA Lin A.N., Dietz H.C., Hovnanian A., Uitto J.; RT "A missense mutation in type VII collagen in two affected siblings with RT recessive dystrophic epidermolysis bullosa."; RL Nat. Genet. 4:62-66(1993). RN [14] RP VARIANT DDEB SER-2040. RX PubMed=8170945; DOI=10.1073/pnas.91.9.3549; RA Christiano A.M., Ryynaenen M., Uitto J.; RT "Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser RT substitution in the triple-helical domain of type VII collagen."; RL Proc. Natl. Acad. Sci. U.S.A. 91:3549-3553(1994). RN [15] RP VARIANT PR-DEB CYS-2623. RX PubMed=8541842; DOI=10.1093/hmg/4.9.1579; RA Christiano A.M., Lee J.Y.-Y., Chen W.J., Laforgia S., Uitto J.; RT "Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and RT identification of a glycine-to-cysteine substitution in the triple-helical RT domain of type VII collagen."; RL Hum. Mol. Genet. 4:1579-1583(1995). RN [16] RP VARIANT DDEB ARG-2043. RX PubMed=7861014; DOI=10.1111/1523-1747.ep12666033; RA Christiano A.M., Morricone A., Paradisi M., Angelo C., Mazzanti C., RA Cavalieri R., Uitto J.; RT "A glycine-to-arginine substitution in the triple-helical domain of type RT VII collagen in a family with dominant dystrophic epidermolysis bullosa."; RL J. Invest. Dermatol. 104:438-440(1995). RN [17] RP VARIANTS DDEB ARG-1557; ARG-1776 AND GLU-2055, AND VARIANTS RDEB ARG-2569; RP ARG-2653; ARG-2674 AND ARG-2749. RX PubMed=8644729; RA Christiano A.M., McGrath J.A., Tan K.C., Uitto J.; RT "Glycine substitutions in the triple-helical region of type VII collagen RT result in a spectrum of dystrophic epidermolysis bullosa phenotypes and RT patterns of inheritance."; RL Am. J. Hum. Genet. 58:671-681(1996). RN [18] RP VARIANT RDEB ARG-2575. RX PubMed=8592061; DOI=10.1111/1523-1747.ep12329600; RA Shimizu H., McGrath J.A., Christiano A.M., Nishikawa T., Uitto J.; RT "Molecular basis of recessive dystrophic epidermolysis bullosa: RT genotype/phenotype correlation in a case of moderate clinical severity."; RL J. Invest. Dermatol. 106:119-124(1996). RN [19] RP VARIANT RDEB ARG-1782. RX PubMed=8618018; DOI=10.1111/1523-1747.ep12345814; RA Christiano A.M., McGrath J.A., Uitto J.; RT "Influence of the second COL7A1 mutation in determining the phenotypic RT severity of recessive dystrophic epidermolysis bullosa."; RL J. Invest. Dermatol. 106:766-770(1996). RN [20] RP VARIANT RDEB ASP-2073. RX PubMed=8757758; DOI=10.1111/1523-1747.ep12329570; RA Dunnill M.G.S., McGrath J.A., Richards A.J., Christiano A.M., Uitto J., RA Pope F.M., Eady R.A.J.; RT "Clinicopathological correlations of compound heterozygous COL7A1 mutations RT in recessive dystrophic epidermolysis bullosa."; RL J. Invest. Dermatol. 107:171-177(1996). RN [21] RP VARIANTS RDEB TRP-1982; GLY-2008; ALA-2025; GLU-2049; TRP-2063 AND RP ARG-2575. RX PubMed=9326325; DOI=10.1086/515495; RA Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C., RA Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y., RA de Prost Y.; RT "Characterization of 18 new mutations in COL7A1 in recessive dystrophic RT epidermolysis bullosa provides evidence for distinct molecular mechanisms RT underlying defective anchoring fibril formation."; RL Am. J. Hum. Genet. 61:599-610(1997). RN [22] RP VARIANT RDEB ARG-1652. RX PubMed=9444387; DOI=10.1007/s004030050253; RA Cserhalmi-Friedman P.B., Karpati S., Horvath A., Christiano A.M.; RT "Identification of a glycine substitution and a splice site mutation in the RT type VII collagen gene in a proband with mitis recessive dystrophic RT epidermolysis bullosa."; RL Arch. Dermatol. Res. 289:640-645(1997). RN [23] RP VARIANT RDEB ARG-2009, AND VARIANT DDEB ARG-2043. RX PubMed=9215684; DOI=10.1093/hmg/6.7.1125; RA Winberg J.-O., Hammami-Hauasli N., Nilssen O., Anton-Lamprecht I., RA Naylor S.L., Kerbacher K., Zimmermann M., Krajci P., Gedde-Dahl T. Jr., RA Bruckner-Tuderman L.; RT "Modulation of disease severity of dystrophic epidermolysis bullosa by a RT splice site mutation in combination with a missense mutation in the COL7A1 RT gene."; RL Hum. Mol. Genet. 6:1125-1135(1997). RN [24] RP VARIANT RDEB VAL-2671. RX PubMed=9008239; DOI=10.1111/1523-1747.ep12335324; RA Kon A., McGrath J.A., Pulkkinen L., Nomura K., Nakamura T., Maekawa Y., RA Christiano A.M., Hashimoto I., Uitto J.; RT "Glycine substitution mutations in the type VII collagen gene (COL7A1) in RT dystrophic epidermolysis bullosa: implications for genetic counseling."; RL J. Invest. Dermatol. 108:224-228(1997). RN [25] RP VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034. RX PubMed=9668111; DOI=10.1074/jbc.273.30.19228; RA Hammami-Hauasli N., Schumann H., Raghunath M., Kilgus O., Luethi U., RA Luger T., Bruckner-Tuderman L.; RT "Some, but not all, glycine substitution mutations in COL7A1 result in RT intracellular accumulation of collagen VII, loss of anchoring fibrils, and RT skin blistering."; RL J. Biol. Chem. 273:19228-19234(1998). RN [26] RP VARIANT DDEB ARG-2207, AND VARIANTS RDEB CYS-2008 AND SER-2775. RX PubMed=9740253; DOI=10.1046/j.1523-1747.1998.00326.x; RA Kon A., Pulkkinen L., Ishida-Yamamoto A., Hashimoto I., Uitto J.; RT "Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa."; RL J. Invest. Dermatol. 111:534-537(1998). RN [27] RP VARIANT RDEB ARG-1347. RX PubMed=9804332; DOI=10.1046/j.1523-1747.1998.00397.x; RA Terracina M., Posteraro P., Schubert M., Sonego G., Atzori F., Zambruno G., RA Bruckner-Tuderman L., Castiglia D.; RT "Compound heterozygosity for a recessive glycine substitution and a splice RT site mutation in the COL7A1 gene causes an unusually mild form of localized RT recessive dystrophic epidermolysis bullosa."; RL J. Invest. Dermatol. 111:744-750(1998). RN [28] RP VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713. RX PubMed=9856843; DOI=10.1046/j.1523-1747.1998.00422.x; RA Rouan F., Pulkkinen L., Jonkman M.F., Bauer J.W., Cserhalmi-Friedman P.B., RA Christiano A.M., Uitto J.; RT "Novel and de novo glycine substitution mutations in the type VII collagen RT gene (COL7A1) in dystrophic epidermolysis bullosa: implications for genetic RT counseling."; RL J. Invest. Dermatol. 111:1210-1213(1998). RN [29] RP VARIANTS TBDN ASP-1519 AND GLU-2251. RX PubMed=9856844; DOI=10.1046/j.1523-1747.1998.00394.x; RA Hammami-Hauasli N., Raghunath M., Kuester W., Bruckner-Tuderman L.; RT "Transient bullous dermolysis of the newborn associated with compound RT heterozygosity for recessive and dominant COL7A1 mutations."; RL J. Invest. Dermatol. 111:1214-1219(1998). RN [30] RP VARIANTS DDEB/RDEB TRP-2063 AND SER-2366, AND VARIANT DDEB GLU-2079. RX PubMed=10232406; DOI=10.1111/j.1600-0625.1999.tb00362.x; RA Hashimoto I., Kon A., Tamai K., Uitto J.; RT "Diagnostic dilemma of 'sporadic' cases of dystrophic epidermolysis RT bullosa: a new dominant or mitis recessive mutation?"; RL Exp. Dermatol. 8:140-142(1999). RN [31] RP VARIANT DDEB/RDEB ARG-2348. RX PubMed=10232407; DOI=10.1111/j.1600-0625.1999.tb00363.x; RA Cserhalmi-Friedman P.B., Grossman J., Karpati S., Ahmad W., Horvath A., RA Christiano A.M.; RT "Identification of a de novo glycine substitution in the type VII collagen RT gene in a proband with mild dystrophic epidermolysis bullosa."; RL Exp. Dermatol. 8:143-145(1999). RN [32] RP VARIANT DDEB ARG-2079. RX PubMed=10232408; DOI=10.1111/j.1600-0625.1999.tb00364.x; RA Christiano A.M., Crollick J., Pincus S., Uitto J.; RT "Squamous cell carcinoma in a family with dominant dystrophic epidermolysis RT bullosa: a molecular genetic study."; RL Exp. Dermatol. 8:146-152(1999). RN [33] RP VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND RP TRP-2043, AND VARIANTS RDEB CYS-2008; GLY-2008 AND ARG-2009. RX PubMed=10084325; DOI=10.1046/j.1523-1747.1999.00518.x; RA Mecklenbeck S., Hammami-Hauasli N., Hoepfner B., Schumann H., Kramer A., RA Kuester W., Bruckner-Tuderman L.; RT "Clustering of COL7A1 mutations in exon 73: implications for mutation RT analysis in dystrophic epidermolysis bullosa."; RL J. Invest. Dermatol. 112:398-400(1999). RN [34] RP VARIANT DDEB GLU-2037. RX PubMed=10233777; DOI=10.1046/j.1523-1747.1999.00568.x; RA Jonkman M.F., Moreno G., Rouan F., Oranje A.P., Pulkkinen L., Uitto J.; RT "Dominant dystrophic epidermolysis bullosa (Pasini) caused by a novel RT glycine substitution mutation in the type VII collagen gene (COL7A1)."; RL J. Invest. Dermatol. 112:815-817(1999). RN [35] RP VARIANTS EBP GLU-1791; ARG-2242; SER-2369 AND ARG-2713. RX PubMed=10383749; DOI=10.1046/j.1523-1747.1999.00614.x; RA Mellerio J.E., Ashton G.H.S., Mohammedi R., Lyon C.C., Kirby B., RA Harman K.E., Salas-Alanis J.C., Atherton D.J., Harrison P.V., RA Griffiths W.A.D., Black M.M., Eady R.A.J., McGrath J.A.; RT "Allelic heterogeneity of dominant and recessive COL7A1 mutations RT underlying epidermolysis bullosa pruriginosa."; RL J. Invest. Dermatol. 112:984-987(1999). RN [36] RP VARIANTS RDEB ARG-2287 AND ARG-2316. RX PubMed=10469344; DOI=10.1046/j.1523-1747.1999.00713.x; RA Shimizu H., Hammami-Hauasli N., Hatta N., Nishikawa T., RA Bruckner-Tuderman L.; RT "Compound heterozygosity for silent and dominant glycine substitution RT mutations in COL7A1 leads to a marked transient intracytoplasmic retention RT of procollagen VII and a moderately severe dystrophic epidermolysis bullosa RT phenotype."; RL J. Invest. Dermatol. 113:419-421(1999). RN [37] RP VARIANTS DDEB GLU-1522; ARG-1776 AND TRP-2791, VARIANTS RDEB ARG-1604; RP GLU-1703; TRP-1772; ASP-2132; SER-2192; VAL-2263; ASP-2674 AND ALA-2740, RP AND VARIANT ARG-2351. RX PubMed=10504458; DOI=10.1046/j.1523-1747.1999.00732.x; RA Whittock N.V., Ashton G.H.S., Mohammedi R., Mellerio J.E., Mathew C.G., RA Abbs S.J., Eady R.A.J., McGrath J.A.; RT "Comparative mutation detection screening of the type VII collagen gene RT (COL7A1) using the protein truncation test, fluorescent chemical cleavage RT of mismatch, and conformation sensitive gel electrophoresis."; RL J. Invest. Dermatol. 113:673-686(1999). RN [38] RP VARIANT DDEB ARG-2028. RX PubMed=10836608; DOI=10.1007/s004030050472; RA Lee J.Y.-Y., Li C., Chao S.-C., Pulkkinen L., Uitto J.; RT "A de novo glycine substitution mutation in the collagenous domain of RT COL7A1 in dominant dystrophic epidermolysis bullosa."; RL Arch. Dermatol. Res. 292:159-163(2000). RN [39] RP VARIANT DDEB ALA-2028, AND VARIANT EBP ARG-2028. RX PubMed=11142768; DOI=10.1007/s004030000162; RA Murata T., Masunaga T., Shimizu H., Takizawa Y., Ishiko A., Hatta N., RA Nishikawa T.; RT "Glycine substitution mutations by different amino acids in the same codon RT of COL7A1 lead to heterogeneous clinical phenotypes of dominant dystrophic RT epidermolysis bullosa."; RL Arch. Dermatol. Res. 292:477-481(2000). RN [40] RP VARIANT RDEB ARG-1812. RX PubMed=10620140; DOI=10.1046/j.1523-1747.2000.00848.x; RA Masunaga T., Shimizu H., Takizawa Y., Uitto J., Nishikawa T.; RT "Combination of novel premature termination codon and glycine substitution RT mutations in COL7A1 leads to moderately severe recessive dystrophic RT epidermolysis bullosa."; RL J. Invest. Dermatol. 114:204-205(2000). RN [41] RP VARIANT RDEB SER-2031. RX PubMed=11167698; DOI=10.1046/j.1365-2133.2001.03966.x; RA Nordal E.J., Mecklenbeck S., Hausser I., Skranes J., Bruckner-Tuderman L., RA Gedde-Dahl T. Jr.; RT "Generalized dystrophic epidermolysis bullosa: identification of a novel, RT homozygous glycine substitution, G2031S, in exon 73 of COL7A1 in monozygous RT triplets."; RL Br. J. Dermatol. 144:151-157(2001). RN [42] RP VARIANTS NDNC8 ARG-1595 AND ARG-1815. RX PubMed=11843659; DOI=10.1001/archderm.138.2.269; RA Sato-Matsumura K.C., Yasukawa K., Tomita Y., Shimizu H.; RT "Toenail dystrophy with COL7A1 glycine substitution mutations segregates as RT an autosomal dominant trait in 2 families with dystrophic epidermolysis RT bullosa."; RL Arch. Dermatol. 138:269-271(2002). RN [43] RP VARIANT EBDSC ARG-2034. RX PubMed=11874498; DOI=10.1046/j.0022-202x.2001.01702.x; RA Martinez-Mir A., Liu J., Gordon D., Weiner M.S., Ahmad W., Fine J.D., RA Ott J., Gilliam T.C., Christiano A.M.; RT "EB simplex superficialis resulting from a mutation in the type VII RT collagen gene."; RL J. Invest. Dermatol. 118:547-549(2002). RN [44] RP VARIANTS RDEB ARG-142 AND CYS-2069. RX PubMed=12787275; DOI=10.1046/j.1525-1470.2003.20312.x; RA Kahofer P., Bruckner-Tuderman L., Metze D., Lemmink H., Scheffer H., RA Smolle J.; RT "Dystrophic epidermolysis bullosa inversa with COL7A1 mutations and absence RT of GDA-J/F3 protein."; RL Pediatr. Dermatol. 20:243-248(2003). RN [45] RP VARIANTS [LARGE SCALE ANALYSIS] PRO-119; THR-1364 AND TRP-1366. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [46] RP VARIANT RDEB ALA-2221. RX PubMed=20108428; RA Garcia M., Escamez M.J., Cuadrado-Corrales N., Sanchez-Jimeno C., RA Illera N., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Ayuso C., Del Rio M.; RT "Novel human pathological mutations. Gene symbol: COL7A1. Disease: RT Epidermolysis bullosa dystrophica."; RL Hum. Genet. 127:116-117(2010). RN [47] RP VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069; GLU-2296; RP ARG-2557 AND TRP-2622, AND VARIANTS DDEB ARG-2003; ASP-2040; ARG-2043; RP ARG-2064; ARG-2070 AND ASP-2076. RX PubMed=20598510; DOI=10.1016/j.jdermsci.2010.05.007; RA Jerabkova B., Kopeckova L., Buckova H., Vesely K., Valickova J., RA Fajkusova L.; RT "Analysis of the COL7A1 gene in Czech patients with dystrophic RT epidermolysis bullosa reveals novel and recurrent mutations."; RL J. Dermatol. Sci. 59:136-140(2010). CC -!- FUNCTION: Stratified squamous epithelial basement membrane protein that CC forms anchoring fibrils which may contribute to epithelial basement CC membrane organization and adherence by interacting with extracellular CC matrix (ECM) proteins such as type IV collagen. CC -!- SUBUNIT: Homotrimer. Interacts with MIA3/TANGO1; facilitating its CC loading into transport carriers and subsequent secretion. CC {ECO:0000269|PubMed:19269366}. CC -!- INTERACTION: CC Q02388; Q5JRA6: MIA3; NbExp=2; IntAct=EBI-724237, EBI-2291868; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q02388-1; Sequence=Displayed; CC Name=2; CC IsoId=Q02388-2; Sequence=VSP_024026; CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:2537292}. CC -!- DISEASE: Note=Epidermolysis bullosa acquisita (EBA) is an autoimmune CC acquired blistering skin disease resulting from autoantibodies to type CC VII collagen. CC -!- DISEASE: Epidermolysis bullosa dystrophica, autosomal dominant (DDEB) CC [MIM:131750]: A group of autosomal dominant blistering skin diseases CC characterized by tissue separation which occurs below the dermal- CC epidermal basement membrane at the level of the anchoring fibrils. CC Various clinical types with different severity are recognized, ranging CC from severe mutilating forms to mild forms with limited and localized CC scarring, and less frequent extracutaneous manifestations. CC {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10232406, CC ECO:0000269|PubMed:10232407, ECO:0000269|PubMed:10232408, CC ECO:0000269|PubMed:10233777, ECO:0000269|PubMed:10504458, CC ECO:0000269|PubMed:10836608, ECO:0000269|PubMed:11142768, CC ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:7861014, CC ECO:0000269|PubMed:8170945, ECO:0000269|PubMed:8644729, CC ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9668111, CC ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9856843}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Epidermolysis bullosa dystrophica, autosomal recessive (RDEB) CC [MIM:226600]: A group of autosomal recessive blistering skin diseases CC characterized by tissue separation which occurs below the dermal- CC epidermal basement membrane at the level of the anchoring fibrils. CC Various clinical types with different severity are recognized, ranging CC from severe mutilating forms, such as epidermolysis bullosa dystrophica CC Hallopeau-Siemens type, to mild forms with limited localized scarring CC and less frequent extracutaneous manifestations. Mild forms include CC epidermolysis bullosa mitis and epidermolysis bullosa localisata. CC {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10469344, CC ECO:0000269|PubMed:10504458, ECO:0000269|PubMed:10620140, CC ECO:0000269|PubMed:11167698, ECO:0000269|PubMed:12787275, CC ECO:0000269|PubMed:20108428, ECO:0000269|PubMed:20598510, CC ECO:0000269|PubMed:8513326, ECO:0000269|PubMed:8592061, CC ECO:0000269|PubMed:8618018, ECO:0000269|PubMed:8644729, CC ECO:0000269|PubMed:8757758, ECO:0000269|PubMed:9008239, CC ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9326325, CC ECO:0000269|PubMed:9444387, ECO:0000269|PubMed:9740253, CC ECO:0000269|PubMed:9804332}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Transient bullous dermolysis of the newborn (TBDN) CC [MIM:131705]: TBDN is a neonatal form of dystrophic epidermolysis CC bullosa characterized by sub-epidermal blisters, reduced or abnormal CC anchoring fibrils at the dermo-epidermal junction, and electron-dense CC inclusions in keratinocytes. TBDN heals spontaneously or strongly CC improves within the first months and years of life. CC {ECO:0000269|PubMed:9856844}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa dystrophica, pretibial type (PR-DEB) CC [MIM:131850]: A form of dystrophic epidermolysis bullosa characterized CC by pretibial blisters that develop into prurigo-like hyperkeratotic CC lesions. It predominantly affects the pretibial areas, sparing the CC knees and other parts of the skin. Other clinical features include nail CC dystrophy, albopapuloid skin lesions, and hypertrophic scars without CC pretibial predominance. The phenotype shows considerable CC interindividual variability. Inheritance is autosomal dominant. CC {ECO:0000269|PubMed:8541842}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa dystrophica, Bart type (B-DEB) CC [MIM:132000]: An autosomal dominant form of dystrophic epidermolysis CC bullosa characterized by congenital localized absence of skin, skin CC fragility and deformity of nails. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: A CC distinct clinical subtype of epidermolysis bullosa dystrophica. It is CC characterized by skin fragility, blistering, scar formation, intense CC pruritus and excoriated prurigo nodules. Onset is in early childhood, CC but in some cases is delayed until the second or third decade of life. CC Inheritance can be autosomal dominant or recessive. CC {ECO:0000269|PubMed:10383749, ECO:0000269|PubMed:11142768}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Nail disorder, non-syndromic congenital, 8 (NDNC8) CC [MIM:607523]: A nail disorder characterized by isolated toenail CC dystrophy. The nail changes are most severe in the great toes and CC consist of the nail plate being buried in the nail bed with a deformed CC and narrow free edge. {ECO:0000269|PubMed:11843659}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa dystrophica, with subcorneal cleavage CC (EBDSC) [MIM:131750]: A bullous skin disorder with variable sized CC clefts just beneath the level of the stratum corneum. Clinical features CC include blisters, milia, atrophic scarring, nail dystrophy, and oral CC and conjunctival involvement, as seen in dystrophic epidermolysis CC bullosa. {ECO:0000269|PubMed:11874498, ECO:0000269|PubMed:2653224}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA02853.1; Type=Frameshift; 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; L23982; AAA58965.1; -; Genomic_DNA. DR EMBL; L02870; AAA75438.1; -; mRNA. DR EMBL; D13694; BAA02853.1; ALT_FRAME; mRNA. DR EMBL; M96984; AAA36357.2; -; mRNA. DR EMBL; S51236; AAB24637.1; -; mRNA. DR EMBL; M65158; AAA96439.1; -; mRNA. DR EMBL; L06862; AAA89196.1; -; mRNA. DR CCDS; CCDS2773.1; -. [Q02388-1] DR PIR; A54849; A54849. DR RefSeq; NP_000085.1; NM_000094.3. [Q02388-1] DR RefSeq; XP_011531639.1; XM_011533337.1. DR SMR; Q02388; -. DR BioGRID; 107691; 20. DR ComplexPortal; CPX-1737; Collagen type VII trimer. DR IntAct; Q02388; 14. DR MINT; Q02388; -. DR STRING; 9606.ENSP00000332371; -. DR MEROPS; I02.967; -. DR GlyCosmos; Q02388; 6 sites, 1 glycan. DR GlyGen; Q02388; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q02388; -. DR PhosphoSitePlus; Q02388; -. DR BioMuta; COL7A1; -. DR DMDM; 1345650; -. DR EPD; Q02388; -. DR jPOST; Q02388; -. DR MassIVE; Q02388; -. DR MaxQB; Q02388; -. DR PaxDb; 9606-ENSP00000332371; -. DR PeptideAtlas; Q02388; -. DR ProteomicsDB; 58086; -. [Q02388-1] DR ProteomicsDB; 58087; -. [Q02388-2] DR Pumba; Q02388; -. DR ABCD; Q02388; 1 sequenced antibody. DR Antibodypedia; 4284; 242 antibodies from 34 providers. DR DNASU; 1294; -. DR Ensembl; ENST00000328333.12; ENSP00000332371.8; ENSG00000114270.18. [Q02388-1] DR Ensembl; ENST00000681320.1; ENSP00000506558.1; ENSG00000114270.18. [Q02388-1] DR GeneID; 1294; -. DR KEGG; hsa:1294; -. DR MANE-Select; ENST00000681320.1; ENSP00000506558.1; NM_000094.4; NP_000085.1. DR UCSC; uc003ctz.3; human. [Q02388-1] DR AGR; HGNC:2214; -. DR CTD; 1294; -. DR DisGeNET; 1294; -. DR GeneCards; COL7A1; -. DR GeneReviews; COL7A1; -. DR HGNC; HGNC:2214; COL7A1. DR HPA; ENSG00000114270; Tissue enhanced (skin). DR MalaCards; COL7A1; -. DR MIM; 120120; gene. DR MIM; 131705; phenotype. DR MIM; 131750; phenotype. DR MIM; 131850; phenotype. DR MIM; 132000; phenotype. DR MIM; 226600; phenotype. DR MIM; 604129; phenotype. DR MIM; 607523; phenotype. DR neXtProt; NX_Q02388; -. DR OpenTargets; ENSG00000114270; -. DR Orphanet; 231568; Autosomal dominant generalized dystrophic epidermolysis bullosa. DR Orphanet; 89842; Autosomal recessive generalized dystrophic epidermolysis bullosa, intermediate form. DR Orphanet; 79408; Autosomal recessive generalized dystrophic epidermolysis bullosa, severe form. DR Orphanet; 89843; Dystrophic epidermolysis bullosa pruriginosa. DR Orphanet; 158673; Localized dystrophic epidermolysis bullosa, acral form. DR Orphanet; 158676; Localized dystrophic epidermolysis bullosa, nails only. DR Orphanet; 79410; Localized dystrophic epidermolysis bullosa, pretibial form. DR Orphanet; 79409; Recessive dystrophic epidermolysis bullosa inversa. DR Orphanet; 79411; Self-improving dystrophic epidermolysis bullosa. DR PharmGKB; PA26730; -. DR VEuPathDB; HostDB:ENSG00000114270; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000154865; -. DR HOGENOM; CLU_000510_0_0_1; -. DR InParanoid; Q02388; -. DR OMA; QTFFAVD; -. DR OrthoDB; 5353225at2759; -. DR PhylomeDB; Q02388; -. DR TreeFam; TF351645; -. DR PathwayCommons; Q02388; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-5694530; Cargo concentration in the ER. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; Q02388; -. DR SIGNOR; Q02388; -. DR BioGRID-ORCS; 1294; 19 hits in 1154 CRISPR screens. DR ChiTaRS; COL7A1; human. DR GeneWiki; Collagen,_type_VII,_alpha_1; -. DR GenomeRNAi; 1294; -. DR Pharos; Q02388; Tbio. DR PRO; PR:Q02388; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q02388; Protein. DR Bgee; ENSG00000114270; Expressed in stromal cell of endometrium and 187 other cell types or tissues. DR ExpressionAtlas; Q02388; baseline and differential. DR GO; GO:0005604; C:basement membrane; TAS:ProtInc. DR GO; GO:0005590; C:collagen type VII trimer; TAS:ProtInc. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0008544; P:epidermis development; TAS:ProtInc. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR CDD; cd00063; FN3; 9. DR CDD; cd22627; Kunitz_collagen_alpha1_VII; 1. DR CDD; cd01482; vWA_collagen_alphaI-XII-like; 1. DR CDD; cd01450; vWFA_subfamily_ECM; 1. DR DisProt; DP02163; -. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 9. DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2. DR InterPro; IPR008160; Collagen. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR002223; Kunitz_BPTI. DR InterPro; IPR036880; Kunitz_BPTI_sf. DR InterPro; IPR020901; Prtase_inh_Kunz-CS. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01391; Collagen; 18. DR Pfam; PF00041; fn3; 8. DR Pfam; PF00014; Kunitz_BPTI; 1. DR Pfam; PF00092; VWA; 2. DR PRINTS; PR00759; BASICPTASE. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00060; FN3; 9. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57362; BPTI-like; 1. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR SUPFAM; SSF53300; vWA-like; 2. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. DR PROSITE; PS50853; FN3; 9. DR PROSITE; PS50234; VWFA; 2. DR Genevisible; Q02388; HS. PE 1: Evidence at protein level; KW Alternative splicing; Basement membrane; Cell adhesion; Collagen; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Epidermolysis bullosa; Extracellular matrix; Glycoprotein; Hydroxylation; KW Protease inhibitor; Reference proteome; Repeat; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..2944 FT /note="Collagen alpha-1(VII) chain" FT /id="PRO_0000005761" FT DOMAIN 38..211 FT /note="VWFA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 234..329 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 330..416 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 417..507 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 510..597 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 600..687 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 688..775 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 778..866 FT /note="Fibronectin type-III 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 869..957 FT /note="Fibronectin type-III 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 958..1051 FT /note="Fibronectin type-III 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1054..1229 FT /note="VWFA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 2872..2944 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT REGION 17..1253 FT /note="Nonhelical region (NC1)" FT REGION 632..651 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1239..1941 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1254..2784 FT /note="Triple-helical region" FT REGION 1254..1477 FT /note="Interrupted collagenous region" FT REGION 1963..2782 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2785..2944 FT /note="Nonhelical region (NC2)" FT REGION 2837..2872 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1170..1172 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1334..1336 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 2008..2010 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 2553..2555 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 1368..1392 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1425..1439 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1713..1730 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1848..1875 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1885..1901 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2056..2073 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2079..2096 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2169..2195 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2278..2292 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2334..2353 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2434..2449 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2537..2568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2632..2646 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2844..2869 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 2886..2887 FT /note="Reactive bond" FT /evidence="ECO:0000250" FT MOD_RES 2036 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2537292" FT MOD_RES 2039 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2537292" FT MOD_RES 2084 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2537292" FT MOD_RES 2087 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2537292" FT MOD_RES 2090 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2537292" FT MOD_RES 2167 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2176 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2188 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2625 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2631 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2664 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2667 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT MOD_RES 2673 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:8051117" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 786 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2625 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2631 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT DISULFID 2634 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 2802 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 2804 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 2876..2929 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 2885..2912 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 2904..2925 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT VAR_SEQ 1869..1900 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_024026" FT VARIANT 119 FT /note="T -> P (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035740" FT VARIANT 142 FT /note="K -> R (in RDEB; uncertain significance; may affect FT exon 3 splicing; dbSNP:rs121912856)" FT /evidence="ECO:0000269|PubMed:12787275" FT /id="VAR_001809" FT VARIANT 595 FT /note="P -> L (in dbSNP:rs2228561)" FT /id="VAR_001810" FT VARIANT 1120 FT /note="R -> K (in dbSNP:rs2228563)" FT /id="VAR_048766" FT VARIANT 1277 FT /note="P -> L (in dbSNP:rs35761247)" FT /id="VAR_001811" FT VARIANT 1347 FT /note="G -> R (in RDEB; localized type; mild; FT dbSNP:rs121912833)" FT /evidence="ECO:0000269|PubMed:9804332" FT /id="VAR_011160" FT VARIANT 1364 FT /note="P -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035741" FT VARIANT 1366 FT /note="R -> W (in a breast cancer sample; somatic mutation; FT dbSNP:rs147089666)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035742" FT VARIANT 1519 FT /note="G -> D (in TBDN; dbSNP:rs121912835)" FT /evidence="ECO:0000269|PubMed:9668111, FT ECO:0000269|PubMed:9856844" FT /id="VAR_011161" FT VARIANT 1522 FT /note="G -> E (in DDEB; dbSNP:rs387906605)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011162" FT VARIANT 1557 FT /note="G -> R (in DDEB)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001812" FT VARIANT 1595 FT /note="G -> R (in NDNC8; dbSNP:rs121912840)" FT /evidence="ECO:0000269|PubMed:11843659" FT /id="VAR_015519" FT VARIANT 1604 FT /note="G -> R (in RDEB; dbSNP:rs1560234201)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011163" FT VARIANT 1652 FT /note="G -> R (in RDEB; mitis type; dbSNP:rs1439299333)" FT /evidence="ECO:0000269|PubMed:9444387" FT /id="VAR_011164" FT VARIANT 1703 FT /note="G -> E (in RDEB; dbSNP:rs770304825)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011165" FT VARIANT 1772 FT /note="R -> W (in RDEB; dbSNP:rs1032335328)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011166" FT VARIANT 1776 FT /note="G -> R (in DDEB)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011167" FT VARIANT 1782 FT /note="G -> R (in RDEB; mitis type; dbSNP:rs374718902)" FT /evidence="ECO:0000269|PubMed:8618018" FT /id="VAR_001813" FT VARIANT 1791 FT /note="G -> E (in EBP; dbSNP:rs1575450640)" FT /evidence="ECO:0000269|PubMed:10383749" FT /id="VAR_011168" FT VARIANT 1812 FT /note="G -> R (in RDEB)" FT /evidence="ECO:0000269|PubMed:10620140" FT /id="VAR_011169" FT VARIANT 1815 FT /note="G -> R (in NDNC8; dbSNP:rs121912841)" FT /evidence="ECO:0000269|PubMed:11843659" FT /id="VAR_015520" FT VARIANT 1845 FT /note="G -> R (in RDEB)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_064994" FT VARIANT 1981 FT /note="K -> R (in RDEB; mild form)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_064995" FT VARIANT 1982 FT /note="G -> W (in RDEB)" FT /evidence="ECO:0000269|PubMed:9326325" FT /id="VAR_001814" FT VARIANT 2003 FT /note="G -> R (in DDEB; dbSNP:rs121912832)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_001815" FT VARIANT 2006 FT /note="G -> A (in DDEB)" FT /id="VAR_011170" FT VARIANT 2006 FT /note="G -> D (in DDEB; interferes with collagen VII FT folding and secretion; dbSNP:rs121912842)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9668111" FT /id="VAR_011171" FT VARIANT 2008 FT /note="R -> C (in RDEB; dbSNP:rs1055680335)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9740253" FT /id="VAR_011172" FT VARIANT 2008 FT /note="R -> G (in RDEB; dbSNP:rs1055680335)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9326325" FT /id="VAR_001816" FT VARIANT 2009 FT /note="G -> R (in RDEB)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9215684" FT /id="VAR_011173" FT VARIANT 2015 FT /note="G -> E (in DDEB; interferes with collagen VII FT folding and secretion; dbSNP:rs121912843)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9668111" FT /id="VAR_011174" FT VARIANT 2025 FT /note="G -> A (in RDEB; mitis type; dbSNP:rs766931219)" FT /evidence="ECO:0000269|PubMed:9326325" FT /id="VAR_001817" FT VARIANT 2028 FT /note="G -> A (in DDEB)" FT /evidence="ECO:0000269|PubMed:11142768" FT /id="VAR_011175" FT VARIANT 2028 FT /note="G -> R (in DDEB and EBP; dbSNP:rs762162799)" FT /evidence="ECO:0000269|PubMed:10836608, FT ECO:0000269|PubMed:11142768" FT /id="VAR_011176" FT VARIANT 2031 FT /note="G -> S (in RDEB; severe phenotype; FT dbSNP:rs121912838)" FT /evidence="ECO:0000269|PubMed:11167698" FT /id="VAR_011177" FT VARIANT 2034 FT /note="G -> R (in DDEB and EBDSC; interferes with collagen FT VII folding and secretion; dbSNP:rs121912844)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:11874498, ECO:0000269|PubMed:2653224, FT ECO:0000269|PubMed:9668111" FT /id="VAR_001818" FT VARIANT 2034 FT /note="G -> W (in DDEB)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:9856843" FT /id="VAR_011178" FT VARIANT 2037 FT /note="G -> E (in DDEB; dbSNP:rs121912846)" FT /evidence="ECO:0000269|PubMed:10233777" FT /id="VAR_011179" FT VARIANT 2040 FT /note="G -> D (in DDEB)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_011180" FT VARIANT 2040 FT /note="G -> S (in DDEB; dbSNP:rs121912829)" FT /evidence="ECO:0000269|PubMed:8170945" FT /id="VAR_001819" FT VARIANT 2040 FT /note="G -> V (in DDEB)" FT /evidence="ECO:0000269|PubMed:9856843" FT /id="VAR_011181" FT VARIANT 2043 FT /note="G -> R (in DDEB; dbSNP:rs121912836)" FT /evidence="ECO:0000269|PubMed:10084325, FT ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:7861014, FT ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9856843" FT /id="VAR_001820" FT VARIANT 2043 FT /note="G -> W (in DDEB; localized type; dbSNP:rs121912836)" FT /evidence="ECO:0000269|PubMed:10084325" FT /id="VAR_011182" FT VARIANT 2046 FT /note="G -> V (in DDEB)" FT /id="VAR_011183" FT VARIANT 2049 FT /note="G -> E (in RDEB)" FT /evidence="ECO:0000269|PubMed:20598510, FT ECO:0000269|PubMed:9326325" FT /id="VAR_001821" FT VARIANT 2055 FT /note="G -> E (in DDEB; dbSNP:rs1553854678)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001822" FT VARIANT 2063 FT /note="R -> W (in RDEB; dbSNP:rs121912849)" FT /evidence="ECO:0000269|PubMed:10232406, FT ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:9326325" FT /id="VAR_001823" FT VARIANT 2064 FT /note="G -> R (in DDEB; dbSNP:rs866061439)" FT /evidence="ECO:0000269|PubMed:20598510, FT ECO:0000269|PubMed:9856843" FT /id="VAR_011184" FT VARIANT 2069 FT /note="R -> C (in RDEB; dbSNP:rs121912855)" FT /evidence="ECO:0000269|PubMed:12787275, FT ECO:0000269|PubMed:20598510" FT /id="VAR_064996" FT VARIANT 2070 FT /note="G -> R (in DDEB)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_064997" FT VARIANT 2073 FT /note="G -> D (in RDEB; mitis type)" FT /evidence="ECO:0000269|PubMed:8757758" FT /id="VAR_001825" FT VARIANT 2076 FT /note="G -> D (in DDEB; also in recessive forms; FT dbSNP:rs121912850)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_001826" FT VARIANT 2079 FT /note="G -> E (in DDEB)" FT /evidence="ECO:0000269|PubMed:10232406" FT /id="VAR_001827" FT VARIANT 2079 FT /note="G -> R (in DDEB)" FT /evidence="ECO:0000269|PubMed:10232408" FT /id="VAR_011185" FT VARIANT 2132 FT /note="G -> D (in RDEB; dbSNP:rs755669902)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011186" FT VARIANT 2192 FT /note="G -> S (in RDEB)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011187" FT VARIANT 2207 FT /note="G -> R (in DDEB)" FT /evidence="ECO:0000269|PubMed:9740253" FT /id="VAR_011188" FT VARIANT 2221 FT /note="G -> A (in RDEB)" FT /evidence="ECO:0000269|PubMed:20108428" FT /id="VAR_064998" FT VARIANT 2242 FT /note="G -> R (in EBP; dbSNP:rs121912837)" FT /evidence="ECO:0000269|PubMed:10383749" FT /id="VAR_001828" FT VARIANT 2251 FT /note="G -> E (in TBDN; also found in isolated toenail FT dystrophy; dbSNP:rs121912834)" FT /evidence="ECO:0000269|PubMed:9856844" FT /id="VAR_011189" FT VARIANT 2263 FT /note="G -> V (in RDEB)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011190" FT VARIANT 2287 FT /note="G -> R (in RDEB; also found in isolated toenail FT dystrophy; dbSNP:rs121912839)" FT /evidence="ECO:0000269|PubMed:10469344" FT /id="VAR_011191" FT VARIANT 2296 FT /note="G -> E (in RDEB)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_064999" FT VARIANT 2316 FT /note="G -> R (in RDEB)" FT /evidence="ECO:0000269|PubMed:10469344" FT /id="VAR_011192" FT VARIANT 2348 FT /note="G -> R (in DDEB/RDEB; mild form)" FT /evidence="ECO:0000269|PubMed:10232407" FT /id="VAR_011193" FT VARIANT 2351 FT /note="G -> R (in a patient with dystrophic epidermolysis FT bullosa; mitis type; dbSNP:rs1800013)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_001829" FT VARIANT 2366 FT /note="G -> S (in RDEB; mitis type; dbSNP:rs1560204600)" FT /evidence="ECO:0000269|PubMed:10232406" FT /id="VAR_011194" FT VARIANT 2369 FT /note="G -> S (in EBP)" FT /evidence="ECO:0000269|PubMed:10383749" FT /id="VAR_011195" FT VARIANT 2429 FT /note="P -> L (in dbSNP:rs2229822)" FT /id="VAR_033786" FT VARIANT 2557 FT /note="G -> R (in RDEB)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_065000" FT VARIANT 2569 FT /note="G -> R (in RDEB; severe and mitis type)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001830" FT VARIANT 2575 FT /note="G -> R (in RDEB; dbSNP:rs760891216)" FT /evidence="ECO:0000269|PubMed:8592061, FT ECO:0000269|PubMed:9326325" FT /id="VAR_001831" FT VARIANT 2622 FT /note="R -> W (in RDEB; dbSNP:rs139318843)" FT /evidence="ECO:0000269|PubMed:20598510" FT /id="VAR_065001" FT VARIANT 2623 FT /note="G -> C (in PR-DEB; dominant; dbSNP:rs121912831)" FT /evidence="ECO:0000269|PubMed:8541842" FT /id="VAR_001832" FT VARIANT 2653 FT /note="G -> R (in RDEB; mitis type; dbSNP:rs121912851)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001833" FT VARIANT 2671 FT /note="G -> V (in RDEB)" FT /evidence="ECO:0000269|PubMed:9008239" FT /id="VAR_001834" FT VARIANT 2674 FT /note="G -> D (in RDEB)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011196" FT VARIANT 2674 FT /note="G -> R (in RDEB; mitis type)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001835" FT VARIANT 2713 FT /note="G -> D (in DDEB; dbSNP:rs369591910)" FT /evidence="ECO:0000269|PubMed:9856843" FT /id="VAR_011197" FT VARIANT 2713 FT /note="G -> R (in EBP)" FT /evidence="ECO:0000269|PubMed:10383749" FT /id="VAR_011198" FT VARIANT 2740 FT /note="G -> A (in RDEB)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011199" FT VARIANT 2749 FT /note="G -> R (in RDEB; dbSNP:rs121912853)" FT /evidence="ECO:0000269|PubMed:8644729" FT /id="VAR_001836" FT VARIANT 2775 FT /note="G -> S (in RDEB; mitis type; dbSNP:rs1333259313)" FT /evidence="ECO:0000269|PubMed:9740253" FT /id="VAR_011200" FT VARIANT 2791 FT /note="R -> W (in DDEB; dbSNP:rs142566193)" FT /evidence="ECO:0000269|PubMed:10504458" FT /id="VAR_011201" FT VARIANT 2798 FT /note="M -> K (in RDEB; dbSNP:rs121912828)" FT /evidence="ECO:0000269|PubMed:8513326" FT /id="VAR_001837" FT CONFLICT 195..197 FT /note="FFF -> EFR (in Ref. 4; BAA02853)" FT /evidence="ECO:0000305" FT CONFLICT 369..371 FT /note="QQQ -> EFR (in Ref. 5; AAA36357/AAB24637)" FT /evidence="ECO:0000305" FT CONFLICT 518..519 FT /note="EL -> DV (in Ref. 5; AAA36357/AAB24637)" FT /evidence="ECO:0000305" FT CONFLICT 529 FT /note="S -> C (in Ref. 4; BAA02853)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="V -> W (in Ref. 5; AAA36357/AAB24637)" FT /evidence="ECO:0000305" FT CONFLICT 851 FT /note="R -> H (in Ref. 4; BAA02853)" FT /evidence="ECO:0000305" FT CONFLICT 893 FT /note="A -> E (in Ref. 1; AAA58965, 4; BAA02853 and 6; FT AAA96439)" FT /evidence="ECO:0000305" FT CONFLICT 1122 FT /note="R -> L (in Ref. 4; BAA02853)" FT /evidence="ECO:0000305" FT CONFLICT 1463..1464 FT /note="SP -> LR (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 2944 AA; 295220 MW; 96D8BF6D0FD387DB CRC64; MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG RSNFREVRSF LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG GDVIRAIREL SYKGGNTRTG AAILHVADHV FLPQLARPGV PKVCILITDG KSQDLVDTAA QRLKGQGVKL FAVGIKNADP EELKRVASQP TSDFFFFVND FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL SEPSSQSLRV QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV PGATGYRVTW RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG RSVGPATSLM ARTDASVEQT LRPVILGPTS ILLSWNLVPE ARGYRLEWRR ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY RLTLYTLLEG HEVATPATVV PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII VRSTQGVERT LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT DITGLQPGTT YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS SVTITWTRVP GATGYRVSWH SAHGPEKSQL VSGEATVAEL DGLEPDTEYT VHVRAHVAGV DGPPASVVVR TAPEPVGRVS RLQILNASSD VLRITWVGVT GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY SVRVTALVGD REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA RTESPRVPSI ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP GSPQTLPGIS SSQRVTGLEP GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR GLADVVFLPH ATQDNAHRAE ATRRVLERLV LALGPLGPQA VQVGLLSYSH RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT AHRYMLAPDA PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY CPKGQKGEPG EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF PGADGRPGSP GRAGNPGTPG APGLKGSPGL PGPRGDPGER GPRGPKGEPG APGQVIGGEG PGLPGRKGDP GPSGPPGPRG PLGDPGPRGP PGLPGTAMKG DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP PGKKGEKGDS EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA GPKGEKGDVG PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT GRAGPPGDSG PPGEKGDPGR PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL PGKAGERGLR GAPGVRGPVG EKGDQGDPGE DGRNGSPGSS GPKGDRGEPG PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG APGERGIEGF RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP GEDGRKGEKG DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ GFPGVPGGTG PKGDRGETGS KGEQGLPGER GLRGEPGSVP NVDRLLETAG IKASALREIV ETWDESSGSF LPVPERRRGP KGDSGEQGPP GKEGPIGFPG ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG IPGLPGRAGG VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG NPGLPGERGM AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ GPSGLKGEPG ETGPPGRGLT GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV GETGKPGAPG RDGASGKDGD RGSPGVPGSP GLPGPVGPKG EPGPTGAPGQ AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE KGEAGRAGEP GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP PGASGLKGDK GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS RGERGEKGDV GSAGLKGDKG DSAVILGPPG PRGAKGDMGE RGPRGLDGDK GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR GLLGPQGQPG AAGIPGDPGS PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK GDKGEAGPPG RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE RVVGAPGVPG APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ HCACQGQFIA SGSRPLPSYA ADTAGSQLHA VPVLRVSHAE EEERVPPEDD EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL DEGSCTAYTL RWYHRAVTGS TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD //