CO7A1_HUMAN
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 03-AUG-2022, entry version 241.
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.1989.01670170047006;
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 DEB.
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 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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
RP VARIANTS 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 [36]
RP VARIANTS DEB.
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
RP VARIANT 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 [46]
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:10836608,
CC ECO:0000269|PubMed:11142768, ECO:0000269|PubMed:20598510,
CC ECO:0000269|PubMed:7861014, ECO:0000269|PubMed:8170945,
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:10620140,
CC ECO:0000269|PubMed:11167698, ECO:0000269|PubMed:12787275,
CC ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:8513326,
CC ECO:0000269|PubMed:8592061, ECO:0000269|PubMed:8618018,
CC ECO:0000269|PubMed:8757758, ECO:0000269|PubMed:9215684,
CC ECO:0000269|PubMed:9326325, ECO:0000269|PubMed:9444387,
CC ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9804332}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 ---------------------------------------------------------------------------
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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; 19.
DR ComplexPortal; CPX-1737; Collagen type VII trimer.
DR IntAct; Q02388; 14.
DR MINT; Q02388; -.
DR STRING; 9606.ENSP00000332371; -.
DR MEROPS; I02.967; -.
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; Q02388; -.
DR PeptideAtlas; Q02388; -.
DR PRIDE; Q02388; -.
DR ProteomicsDB; 58086; -. [Q02388-1]
DR ProteomicsDB; 58087; -. [Q02388-2]
DR ABCD; Q02388; 1 sequenced antibody.
DR Antibodypedia; 4284; 193 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 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; PYMDPSG; -.
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 1072 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 185 other tissues.
DR ExpressionAtlas; Q02388; baseline and differential.
DR Genevisible; Q02388; HS.
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 CDD; cd00063; FN3; 9.
DR CDD; cd00109; KU; 1.
DR DisProt; DP02163; -.
DR Gene3D; 2.60.40.10; -; 9.
DR Gene3D; 3.40.50.410; -; 2.
DR Gene3D; 4.10.410.10; -; 1.
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 Pfam; PF01391; Collagen; 15.
DR Pfam; PF00041; fn3; 8.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50234; VWFA; 2.
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; unknown pathological significance;
FT may affect 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 /id="VAR_011162"
FT VARIANT 1557
FT /note="G -> R (in DDEB)"
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 /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 /id="VAR_011165"
FT VARIANT 1772
FT /note="R -> W (in RDEB; dbSNP:rs1032335328)"
FT /id="VAR_011166"
FT VARIANT 1776
FT /note="G -> R (in DDEB)"
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 /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; associated with squamous cell
FT carcinoma)"
FT /evidence="ECO:0000269|PubMed:10232408"
FT /id="VAR_011185"
FT VARIANT 2132
FT /note="G -> D (in RDEB; dbSNP:rs755669902)"
FT /id="VAR_011186"
FT VARIANT 2192
FT /note="G -> S (in RDEB)"
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 /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 /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 /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 /id="VAR_001833"
FT VARIANT 2671
FT /note="G -> V (in RDEB)"
FT /id="VAR_001834"
FT VARIANT 2674
FT /note="G -> D (in RDEB)"
FT /id="VAR_011196"
FT VARIANT 2674
FT /note="G -> R (in RDEB; mitis type)"
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 /id="VAR_011199"
FT VARIANT 2749
FT /note="G -> R (in RDEB; dbSNP:rs121912853)"
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 /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
