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Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen)

 CO7A1_HUMAN             Reviewed;        2944 AA.
Q02388; Q14054; Q16507;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
27-SEP-2017, entry version 207.
RecName: Full=Collagen alpha-1(VII) chain;
AltName: Full=Long-chain collagen;
Short=LC collagen;
Flags: Precursor;
Name=COL7A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=8088784; DOI=10.1006/geno.1994.1239;
Christiano A.M., Hoffman G.G., Chung-Honet L.C., Lee S., Cheng W.,
Uitto J., Greenspan D.S.;
"Structural organization of the human type VII collagen gene (COL7A1),
composed of more exons than any previously characterized gene.";
Genomics 21:169-179(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8051117;
Christiano A.M., Greenspan D.S., Lee S., Uitto J.;
"Cloning of human type VII collagen. Complete primary sequence of the
alpha 1(VII) chain and identification of intragenic polymorphisms.";
J. Biol. Chem. 269:20256-20262(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 128-1493, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1307247; DOI=10.1093/hmg/1.7.475;
Christiano A.M., Rosenbaum L.M., Chung-Honet L.C., Parente M.G.,
Woodley D.T., Pan T.C., Zhang R.Z., Chu M.-L., Burgeson R.E.,
Uitto J.;
"The large non-collagenous domain (NC-1) of type VII collagen is
amino-terminal and chimeric. Homology to cartilage matrix protein, the
type III domains of fibronectin and the A domains of von Willebrand
factor.";
Hum. Mol. Genet. 1:475-481(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 195-1275.
TISSUE=Keratinocyte;
PubMed=1567409; DOI=10.1016/S0006-291X(05)80283-9;
Tanaka T., Takahashi K., Furukawa F., Imamura S.;
"Molecular cloning and characterization of type VII collagen cDNA.";
Biochem. Biophys. Res. Commun. 183:958-963(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 369-1255.
PubMed=1469284; DOI=10.1111/1523-1747.ep12614080;
Gammon W.R., Abernethy M.L., Padilla K.M., Prisayanh P.S., Cook M.E.,
Wright J., Briggaman R.A., Hunt S.W. III;
"Noncollagenous (NC1) domain of collagen VII resembles multidomain
adhesion proteins involved in tissue-specific organization of
extracellular matrix.";
J. Invest. Dermatol. 99:691-696(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 815-1439.
PubMed=1871109; DOI=10.1073/pnas.88.16.6931;
Parente M.G., Chung L.C., Ryynaenen J., Woodley D.T., Wynn K.W.,
Bauer E.A., Mattei M.-G., Chu M.-L., Uitto J.;
"Human type VII collagen: cDNA cloning and chromosomal mapping of the
gene.";
Proc. Natl. Acad. Sci. U.S.A. 88:6931-6935(1991).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2395-2944.
PubMed=8499916; DOI=10.1093/hmg/2.3.273;
Greenspan D.S.;
"The carboxyl-terminal half of type VII collagen, including the non-
collagenous NC-2 domain and intron/exon organization of the
corresponding region of the COL7A1 gene.";
Hum. Mol. Genet. 2:273-278(1993).
[8]
PARTIAL PROTEIN SEQUENCE, AND HYDROXYLATION.
PubMed=2537292;
Seltzer J.L., Eisen A.Z., Bauer E.A., Morris N.P., Glanville R.W.,
Burgeson R.E.;
"Cleavage of type VII collagen by interstitial collagenase and type IV
collagenase (gelatinase) derived from human skin.";
J. Biol. Chem. 264:3822-3826(1989).
[9]
INTERACTION WITH MIA3.
PubMed=19269366; DOI=10.1016/j.cell.2008.12.025;
Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D.,
Polischuk R., Schekman R., Malhotra V.;
"TANGO1 facilitates cargo loading at endoplasmic reticulum exit
sites.";
Cell 136:891-902(2009).
[10]
REVIEW ON VARIANTS.
PubMed=9375848;
DOI=10.1002/(SICI)1098-1004(1997)10:5<338::AID-HUMU2>3.3.CO;2-T;
Jaervikallio A., Pulkkinen L., Uitto J.;
"Molecular basis of dystrophic epidermolysis bullosa: mutations in the
type VII collagen gene (COL7A1).";
Hum. Mutat. 10:338-347(1997).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
VARIANT EBDSC ARG-2034.
PubMed=2653224; DOI=10.1001/archderm.1989.01670170047006;
Fine J.-D., Johnson L., Wright T.;
"Epidermolysis bullosa simplex superficialis. A new variant of
epidermolysis bullosa characterized by subcorneal skin cleavage
mimicking peeling skin syndrome.";
Arch. Dermatol. 125:633-638(1989).
[13]
VARIANT HS-DEB LYS-2798.
PubMed=8513326; DOI=10.1038/ng0593-62;
Christiano A.M., Greenspan D.S., Hoffman G.G., Zhang X., Tamai Y.,
Lin A.N., Dietz H.C., Hovnanian A., Uitto J.;
"A missense mutation in type VII collagen in two affected siblings
with recessive dystrophic epidermolysis bullosa.";
Nat. Genet. 4:62-66(1993).
[14]
VARIANT P-DEB SER-2040.
PubMed=8170945; DOI=10.1073/pnas.91.9.3549;
Christiano A.M., Ryynaenen M., Uitto J.;
"Dominant dystrophic epidermolysis bullosa: identification of a
Gly-->Ser substitution in the triple-helical domain of type VII
collagen.";
Proc. Natl. Acad. Sci. U.S.A. 91:3549-3553(1994).
[15]
VARIANT PR-DEB CYS-2623.
PubMed=8541842; DOI=10.1093/hmg/4.9.1579;
Christiano A.M., Lee J.Y.-Y., Chen W.J., Laforgia S., Uitto J.;
"Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and
identification of a glycine-to-cysteine substitution in the triple-
helical domain of type VII collagen.";
Hum. Mol. Genet. 4:1579-1583(1995).
[16]
VARIANT DDEB ARG-2043.
PubMed=7861014; DOI=10.1111/1523-1747.ep12666033;
Christiano A.M., Morricone A., Paradisi M., Angelo C., Mazzanti C.,
Cavalieri R., Uitto J.;
"A glycine-to-arginine substitution in the triple-helical domain of
type VII collagen in a family with dominant dystrophic epidermolysis
bullosa.";
J. Invest. Dermatol. 104:438-440(1995).
[17]
VARIANTS DEB.
PubMed=8644729;
Christiano A.M., McGrath J.A., Tan K.C., Uitto J.;
"Glycine substitutions in the triple-helical region of type VII
collagen result in a spectrum of dystrophic epidermolysis bullosa
phenotypes and patterns of inheritance.";
Am. J. Hum. Genet. 58:671-681(1996).
[18]
VARIANT HS-DEB ARG-2575.
PubMed=8592061; DOI=10.1111/1523-1747.ep12329600;
Shimizu H., McGrath J.A., Christiano A.M., Nishikawa T., Uitto J.;
"Molecular basis of recessive dystrophic epidermolysis bullosa:
genotype/phenotype correlation in a case of moderate clinical
severity.";
J. Invest. Dermatol. 106:119-124(1996).
[19]
VARIANT RDEB ARG-1782.
PubMed=8618018; DOI=10.1111/1523-1747.ep12345814;
Christiano A.M., McGrath J.A., Uitto J.;
"Influence of the second COL7A1 mutation in determining the phenotypic
severity of recessive dystrophic epidermolysis bullosa.";
J. Invest. Dermatol. 106:766-770(1996).
[20]
VARIANT RDEB ASP-2073.
PubMed=8757758; DOI=10.1111/1523-1747.ep12329570;
Dunnill M.G.S., McGrath J.A., Richards A.J., Christiano A.M.,
Uitto J., Pope F.M., Eady R.A.J.;
"Clinicopathological correlations of compound heterozygous COL7A1
mutations in recessive dystrophic epidermolysis bullosa.";
J. Invest. Dermatol. 107:171-177(1996).
[21]
VARIANTS HS-DEB TRP-1982; GLY-2008; ALA-2025; GLU-2049; TRP-2063 AND
ARG-2575.
PubMed=9326325; DOI=10.1086/515495;
Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C.,
Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y.,
de Prost Y.;
"Characterization of 18 new mutations in COL7A1 in recessive
dystrophic epidermolysis bullosa provides evidence for distinct
molecular mechanisms underlying defective anchoring fibril
formation.";
Am. J. Hum. Genet. 61:599-610(1997).
[22]
VARIANT RDEB ARG-1652.
PubMed=9444387; DOI=10.1007/s004030050253;
Cserhalmi-Friedman P.B., Karpati S., Horvath A., Christiano A.M.;
"Identification of a glycine substitution and a splice site mutation
in the type VII collagen gene in a proband with mitis recessive
dystrophic epidermolysis bullosa.";
Arch. Dermatol. Res. 289:640-645(1997).
[23]
VARIANT RDEB ARG-2009, AND VARIANT DDEB ARG-2043.
PubMed=9215684; DOI=10.1093/hmg/6.7.1125;
Winberg J.-O., Hammami-Hauasli N., Nilssen O., Anton-Lamprecht I.,
Naylor S.L., Kerbacher K., Zimmermann M., Krajci P.,
Gedde-Dahl T. Jr., Bruckner-Tuderman L.;
"Modulation of disease severity of dystrophic epidermolysis bullosa by
a splice site mutation in combination with a missense mutation in the
COL7A1 gene.";
Hum. Mol. Genet. 6:1125-1135(1997).
[24]
VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034.
PubMed=9668111; DOI=10.1074/jbc.273.30.19228;
Hammami-Hauasli N., Schumann H., Raghunath M., Kilgus O., Luethi U.,
Luger T., Bruckner-Tuderman L.;
"Some, but not all, glycine substitution mutations in COL7A1 result in
intracellular accumulation of collagen VII, loss of anchoring fibrils,
and skin blistering.";
J. Biol. Chem. 273:19228-19234(1998).
[25]
VARIANT HS-DEB CYS-2008, VARIANT DDEB ARG-2207, AND VARIANT RDEB
SER-2775.
PubMed=9740253; DOI=10.1046/j.1523-1747.1998.00326.x;
Kon A., Pulkkinen L., Ishida-Yamamoto A., Hashimoto I., Uitto J.;
"Novel COL7A1 mutations in dystrophic forms of epidermolysis
bullosa.";
J. Invest. Dermatol. 111:534-537(1998).
[26]
VARIANT RDEB ARG-1347.
PubMed=9804332; DOI=10.1046/j.1523-1747.1998.00397.x;
Terracina M., Posteraro P., Schubert M., Sonego G., Atzori F.,
Zambruno G., Bruckner-Tuderman L., Castiglia D.;
"Compound heterozygosity for a recessive glycine substitution and a
splice site mutation in the COL7A1 gene causes an unusually mild form
of localized recessive dystrophic epidermolysis bullosa.";
J. Invest. Dermatol. 111:744-750(1998).
[27]
VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713.
PubMed=9856843; DOI=10.1046/j.1523-1747.1998.00422.x;
Rouan F., Pulkkinen L., Jonkman M.F., Bauer J.W.,
Cserhalmi-Friedman P.B., Christiano A.M., Uitto J.;
"Novel and de novo glycine substitution mutations in the type VII
collagen gene (COL7A1) in dystrophic epidermolysis bullosa:
implications for genetic counseling.";
J. Invest. Dermatol. 111:1210-1213(1998).
[28]
VARIANTS TBDN ASP-1519 AND GLU-2251.
PubMed=9856844; DOI=10.1046/j.1523-1747.1998.00394.x;
Hammami-Hauasli N., Raghunath M., Kuester W., Bruckner-Tuderman L.;
"Transient bullous dermolysis of the newborn associated with compound
heterozygosity for recessive and dominant COL7A1 mutations.";
J. Invest. Dermatol. 111:1214-1219(1998).
[29]
VARIANTS DDEB/RDEB TRP-2063 AND SER-2366, AND VARIANT DDEB GLU-2079.
PubMed=10232406; DOI=10.1111/j.1600-0625.1999.tb00362.x;
Hashimoto I., Kon A., Tamai K., Uitto J.;
"Diagnostic dilemma of 'sporadic' cases of dystrophic epidermolysis
bullosa: a new dominant or mitis recessive mutation?";
Exp. Dermatol. 8:140-142(1999).
[30]
VARIANT DDEB/RDEB ARG-2348.
PubMed=10232407; DOI=10.1111/j.1600-0625.1999.tb00363.x;
Cserhalmi-Friedman P.B., Grossman J., Karpati S., Ahmad W.,
Horvath A., Christiano A.M.;
"Identification of a de novo glycine substitution in the type VII
collagen gene in a proband with mild dystrophic epidermolysis
bullosa.";
Exp. Dermatol. 8:143-145(1999).
[31]
VARIANT DDEB ARG-2079.
PubMed=10232408; DOI=10.1111/j.1600-0625.1999.tb00364.x;
Christiano A.M., Crollick J., Pincus S., Uitto J.;
"Squamous cell carcinoma in a family with dominant dystrophic
epidermolysis bullosa: a molecular genetic study.";
Exp. Dermatol. 8:146-152(1999).
[32]
VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND
TRP-2043, VARIANTS HS-DEB CYS-2008 AND GLY-2008, AND VARIANT RDEB
ARG-2009.
PubMed=10084325; DOI=10.1046/j.1523-1747.1999.00518.x;
Mecklenbeck S., Hammami-Hauasli N., Hoepfner B., Schumann H.,
Kramer A., Kuester W., Bruckner-Tuderman L.;
"Clustering of COL7A1 mutations in exon 73: implications for mutation
analysis in dystrophic epidermolysis bullosa.";
J. Invest. Dermatol. 112:398-400(1999).
[33]
VARIANT P-DEB GLU-2037.
PubMed=10233777; DOI=10.1046/j.1523-1747.1999.00568.x;
Jonkman M.F., Moreno G., Rouan F., Oranje A.P., Pulkkinen L.,
Uitto J.;
"Dominant dystrophic epidermolysis bullosa (Pasini) caused by a novel
glycine substitution mutation in the type VII collagen gene
(COL7A1).";
J. Invest. Dermatol. 112:815-817(1999).
[34]
VARIANTS EBP GLU-1791; ARG-2242; SER-2369 AND ARG-2713.
PubMed=10383749; DOI=10.1046/j.1523-1747.1999.00614.x;
Mellerio J.E., Ashton G.H.S., Mohammedi R., Lyon C.C., Kirby B.,
Harman K.E., Salas-Alanis J.C., Atherton D.J., Harrison P.V.,
Griffiths W.A.D., Black M.M., Eady R.A.J., McGrath J.A.;
"Allelic heterogeneity of dominant and recessive COL7A1 mutations
underlying epidermolysis bullosa pruriginosa.";
J. Invest. Dermatol. 112:984-987(1999).
[35]
VARIANTS ARG-2287 AND ARG-2316.
PubMed=10469344; DOI=10.1046/j.1523-1747.1999.00713.x;
Shimizu H., Hammami-Hauasli N., Hatta N., Nishikawa T.,
Bruckner-Tuderman L.;
"Compound heterozygosity for silent and dominant glycine substitution
mutations in COL7A1 leads to a marked transient intracytoplasmic
retention of procollagen VII and a moderately severe dystrophic
epidermolysis bullosa phenotype.";
J. Invest. Dermatol. 113:419-421(1999).
[36]
VARIANTS DEB.
PubMed=10504458; DOI=10.1046/j.1523-1747.1999.00732.x;
Whittock N.V., Ashton G.H.S., Mohammedi R., Mellerio J.E.,
Mathew C.G., Abbs S.J., Eady R.A.J., McGrath J.A.;
"Comparative mutation detection screening of the type VII collagen
gene (COL7A1) using the protein truncation test, fluorescent chemical
cleavage of mismatch, and conformation sensitive gel
electrophoresis.";
J. Invest. Dermatol. 113:673-686(1999).
[37]
VARIANT DDEB ARG-2028.
PubMed=10836608; DOI=10.1007/s004030050472;
Lee J.Y.-Y., Li C., Chao S.-C., Pulkkinen L., Uitto J.;
"A de novo glycine substitution mutation in the collagenous domain of
COL7A1 in dominant dystrophic epidermolysis bullosa.";
Arch. Dermatol. Res. 292:159-163(2000).
[38]
VARIANT DDEB ALA-2028, AND VARIANT EBP ARG-2028.
PubMed=11142768; DOI=10.1007/s004030000162;
Murata T., Masunaga T., Shimizu H., Takizawa Y., Ishiko A., Hatta N.,
Nishikawa T.;
"Glycine substitution mutations by different amino acids in the same
codon of COL7A1 lead to heterogeneous clinical phenotypes of dominant
dystrophic epidermolysis bullosa.";
Arch. Dermatol. Res. 292:477-481(2000).
[39]
VARIANT RDEB ARG-1812.
PubMed=10620140; DOI=10.1046/j.1523-1747.2000.00848.x;
Masunaga T., Shimizu H., Takizawa Y., Uitto J., Nishikawa T.;
"Combination of novel premature termination codon and glycine
substitution mutations in COL7A1 leads to moderately severe recessive
dystrophic epidermolysis bullosa.";
J. Invest. Dermatol. 114:204-205(2000).
[40]
VARIANT RDEB SER-2031.
PubMed=11167698; DOI=10.1046/j.1365-2133.2001.03966.x;
Nordal E.J., Mecklenbeck S., Hausser I., Skranes J.,
Bruckner-Tuderman L., Gedde-Dahl T. Jr.;
"Generalized dystrophic epidermolysis bullosa: identification of a
novel, homozygous glycine substitution, G2031S, in exon 73 of COL7A1
in monozygous triplets.";
Br. J. Dermatol. 144:151-157(2001).
[41]
VARIANTS NDNC8 ARG-1595 AND ARG-1815.
PubMed=11843659; DOI=10.1001/archderm.138.2.269;
Sato-Matsumura K.C., Yasukawa K., Tomita Y., Shimizu H.;
"Toenail dystrophy with COL7A1 glycine substitution mutations
segregates as an autosomal dominant trait in 2 families with
dystrophic epidermolysis bullosa.";
Arch. Dermatol. 138:269-271(2002).
[42]
VARIANT EBDSC ARG-2034.
PubMed=11874498; DOI=10.1046/j.0022-202x.2001.01702.x;
Martinez-Mir A., Liu J., Gordon D., Weiner M.S., Ahmad W., Fine J.D.,
Ott J., Gilliam T.C., Christiano A.M.;
"EB simplex superficialis resulting from a mutation in the type VII
collagen gene.";
J. Invest. Dermatol. 118:547-549(2002).
[43]
VARIANTS [LARGE SCALE ANALYSIS] PRO-119; THR-1364 AND TRP-1366.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[44]
VARIANT ALA-2221.
PubMed=20108428;
Garcia M., Escamez M.J., Cuadrado-Corrales N., Sanchez-Jimeno C.,
Illera N., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Ayuso C.,
Del Rio M.;
"Novel human pathological mutations. Gene symbol: COL7A1. Disease:
Epidermolysis bullosa dystrophica.";
Hum. Genet. 127:116-117(2010).
[45]
VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069;
GLU-2296; ARG-2557 AND TRP-2622, AND VARIANTS DDEB ARG-2003; ASP-2040;
ARG-2043; ARG-2064; ARG-2070 AND ASP-2076.
PubMed=20598510; DOI=10.1016/j.jdermsci.2010.05.007;
Jerabkova B., Kopeckova L., Buckova H., Vesely K., Valickova J.,
Fajkusova L.;
"Analysis of the COL7A1 gene in Czech patients with dystrophic
epidermolysis bullosa reveals novel and recurrent mutations.";
J. Dermatol. Sci. 59:136-140(2010).
-!- FUNCTION: Stratified squamous epithelial basement membrane protein
that forms anchoring fibrils which may contribute to epithelial
basement membrane organization and adherence by interacting with
extracellular matrix (ECM) proteins such as type IV collagen.
-!- SUBUNIT: Homotrimer. Interacts with MIA3/TANGO1; facilitating its
loading into transport carriers and subsequent secretion.
{ECO:0000269|PubMed:19269366}.
-!- INTERACTION:
Q5JRA6:MIA3; NbExp=2; IntAct=EBI-724237, EBI-2291868;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q02388-1; Sequence=Displayed;
Name=2;
IsoId=Q02388-2; Sequence=VSP_024026;
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:2537292}.
-!- DISEASE: Note=Epidermolysis bullosa acquisita (EBA) is an
autoimmune acquired blistering skin disease resulting from
autoantibodies to type VII collagen.
-!- DISEASE: Epidermolysis bullosa dystrophica, autosomal dominant
(DDEB) [MIM:131750]: A group of autosomal dominant blistering skin
diseases characterized by tissue separation which occurs below the
dermal-epidermal basement membrane at the level of the anchoring
fibrils. Various clinical types with different severity are
recognized, ranging from severe mutilating forms to mild forms
with limited and localized scarring, and less frequent
extracutaneous manifestations. {ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:10232406, ECO:0000269|PubMed:10232407,
ECO:0000269|PubMed:10232408, ECO:0000269|PubMed:10836608,
ECO:0000269|PubMed:11142768, ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:7861014, ECO:0000269|PubMed:9215684,
ECO:0000269|PubMed:9668111, ECO:0000269|PubMed:9740253,
ECO:0000269|PubMed:9856843}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, autosomal recessive
(RDEB) [MIM:226600]: A group of autosomal recessive blistering
skin diseases characterized by tissue separation which occurs
below the dermal-epidermal basement membrane at the level of the
anchoring fibrils. Various clinical types with different severity
are recognized, ranging from severe mutilating forms to mild forms
with limited and localized scarring, and less frequent
extracutaneous manifestations. Mild forms include epidermolysis
bullosa mitis and epidermolysis bullosa localisata.
{ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10620140,
ECO:0000269|PubMed:11167698, ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:8618018, ECO:0000269|PubMed:8757758,
ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9444387,
ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9804332}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, Pasini type (P-DEB)
[MIM:131750]: A severe, dominantly inherited form of dystrophic
epidermolysis bullosa characterized by albopapuloid Pasini papule,
dorsal extremity blistering, milia formation and red atrophic
scarring after recurrent blisters. {ECO:0000269|PubMed:10233777,
ECO:0000269|PubMed:8170945}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, Hallopeau-Siemens type
(HS-DEB) [MIM:226600]: The most severe recessive form of
dystrophic epidermolysis bullosa. It manifests with mutilating
scarring, joint contractures, corneal erosions, esophagus
structures, and propensity to formation of cutaneous squamous cell
carcinomas leading to premature demise of the affected
individuals. {ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:8513326, ECO:0000269|PubMed:8592061,
ECO:0000269|PubMed:9326325, ECO:0000269|PubMed:9740253}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Transient bullous dermolysis of the newborn (TBDN)
[MIM:131705]: TBDN is a neonatal form of dystrophic epidermolysis
bullosa characterized by sub-epidermal blisters, reduced or
abnormal anchoring fibrils at the dermo-epidermal junction, and
electron-dense inclusions in keratinocytes. TBDN heals
spontaneously or strongly improves within the first months and
years of life. {ECO:0000269|PubMed:9856844}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, pretibial type (PR-
DEB) [MIM:131850]: A form of dystrophic epidermolysis bullosa
characterized by pretibial blisters that develop into prurigo-like
hyperkeratotic lesions. It predominantly affects the pretibial
areas, sparing the knees and other parts of the skin. Other
clinical features include nail dystrophy, albopapuloid skin
lesions, and hypertrophic scars without pretibial predominance.
The phenotype shows considerable interindividual variability.
Inheritance is autosomal dominant. {ECO:0000269|PubMed:8541842}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, Bart type (B-DEB)
[MIM:132000]: An autosomal dominant form of dystrophic
epidermolysis bullosa characterized by congenital localized
absence of skin, skin fragility and deformity of nails. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: A
distinct clinical subtype of epidermolysis bullosa dystrophica. It
is characterized by skin fragility, blistering, scar formation,
intense pruritus and excoriated prurigo nodules. Onset is in early
childhood, but in some cases is delayed until the second or third
decade of life. Inheritance can be autosomal dominant or
recessive. {ECO:0000269|PubMed:10383749,
ECO:0000269|PubMed:11142768}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Nail disorder, non-syndromic congenital, 8 (NDNC8)
[MIM:607523]: A nail disorder characterized by isolated toenail
dystrophy. The nail changes are most severe in the great toes and
consist of the nail plate being buried in the nail bed with a
deformed and narrow free edge. {ECO:0000269|PubMed:11843659}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epidermolysis bullosa dystrophica, with subcorneal
cleavage (EBDSC) [MIM:131750]: A bullous skin disorder with
variable sized clefts just beneath the level of the stratum
corneum. Clinical features include blisters, milia, atrophic
scarring, nail dystrophy, and oral and conjunctival involvement,
as seen in dystrophic epidermolysis bullosa.
{ECO:0000269|PubMed:11874498, ECO:0000269|PubMed:2653224}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA02853.1; Type=Frameshift; Positions=275, 282, 476, 494, 523, 541, 543; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L23982; AAA58965.1; -; Genomic_DNA.
EMBL; L02870; AAA75438.1; -; mRNA.
EMBL; D13694; BAA02853.1; ALT_FRAME; mRNA.
EMBL; M96984; AAA36357.2; -; mRNA.
EMBL; S51236; AAB24637.1; -; mRNA.
EMBL; M65158; AAA96439.1; -; mRNA.
EMBL; L06862; AAA89196.1; -; mRNA.
CCDS; CCDS2773.1; -. [Q02388-1]
PIR; A54849; A54849.
RefSeq; NP_000085.1; NM_000094.3. [Q02388-1]
RefSeq; XP_011531639.1; XM_011533337.1. [Q02388-1]
UniGene; Hs.476218; -.
ProteinModelPortal; Q02388; -.
SMR; Q02388; -.
BioGrid; 107691; 17.
IntAct; Q02388; 14.
MINT; MINT-1390694; -.
STRING; 9606.ENSP00000332371; -.
MEROPS; I02.967; -.
iPTMnet; Q02388; -.
PhosphoSitePlus; Q02388; -.
BioMuta; COL7A1; -.
DMDM; 1345650; -.
EPD; Q02388; -.
MaxQB; Q02388; -.
PaxDb; Q02388; -.
PeptideAtlas; Q02388; -.
PRIDE; Q02388; -.
Ensembl; ENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
GeneID; 1294; -.
KEGG; hsa:1294; -.
UCSC; uc003ctz.3; human. [Q02388-1]
CTD; 1294; -.
DisGeNET; 1294; -.
EuPathDB; HostDB:ENSG00000114270.15; -.
GeneCards; COL7A1; -.
GeneCards; MIR711; -.
GeneReviews; COL7A1; -.
HGNC; HGNC:2214; COL7A1.
HPA; CAB016357; -.
HPA; HPA042420; -.
MalaCards; COL7A1; -.
MIM; 120120; gene.
MIM; 131705; phenotype.
MIM; 131750; phenotype.
MIM; 131850; phenotype.
MIM; 132000; phenotype.
MIM; 226600; phenotype.
MIM; 604129; phenotype.
MIM; 607523; phenotype.
neXtProt; NX_Q02388; -.
OpenTargets; ENSG00000114270; -.
Orphanet; 158673; Acral dystrophic epidermolysis bullosa.
Orphanet; 89841; Centripetalis recessive dystrophic epidermolysis bullosa.
Orphanet; 89843; Dystrophic epidermolysis bullosa pruriginosa.
Orphanet; 158676; Dystrophic epidermolysis bullosa, nails only.
Orphanet; 89839; Epidermolysis bullosa simplex superficialis.
Orphanet; 231568; Generalized dominant dystrophic epidermolysis bullosa.
Orphanet; 79410; Pretibial dystrophic epidermolysis bullosa.
Orphanet; 79409; Recessive dystrophic epidermolysis bullosa inversa.
Orphanet; 89842; Recessive dystrophic epidermolysis bullosa-generalized other.
Orphanet; 79408; Severe generalized recessive dystrophic epidermolysis bullosa.
Orphanet; 79411; Transient bullous dermolysis of the newborn.
PharmGKB; PA26730; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00760000119000; -.
HOGENOM; HOG000111866; -.
HOVERGEN; HBG051053; -.
InParanoid; Q02388; -.
KO; K16628; -.
OMA; EYRLTLY; -.
OrthoDB; EOG091G008X; -.
PhylomeDB; Q02388; -.
TreeFam; TF351645; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474244; Extracellular matrix organization.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-2214320; Anchoring fibril formation.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; Q02388; -.
ChiTaRS; COL7A1; human.
GeneWiki; Collagen,_type_VII,_alpha_1; -.
GenomeRNAi; 1294; -.
PRO; PR:Q02388; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114270; -.
CleanEx; HS_COL7A1; -.
ExpressionAtlas; Q02388; baseline and differential.
Genevisible; Q02388; HS.
GO; GO:0005604; C:basement membrane; TAS:ProtInc.
GO; GO:0005590; C:collagen type VII trimer; TAS:ProtInc.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
CDD; cd00063; FN3; 9.
CDD; cd00109; KU; 1.
Gene3D; 2.60.40.10; -; 9.
Gene3D; 3.40.50.410; -; 2.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
InterPro; IPR002035; VWF_A.
Pfam; PF01391; Collagen; 15.
Pfam; PF00041; fn3; 8.
Pfam; PF00014; Kunitz_BPTI; 1.
Pfam; PF00092; VWA; 2.
PRINTS; PR00759; BASICPTASE.
SMART; SM00060; FN3; 9.
SMART; SM00327; VWA; 1.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF53300; SSF53300; 2.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PROSITE; PS50853; FN3; 9.
PROSITE; PS50234; VWFA; 2.
1: Evidence at protein level;
Alternative splicing; Basement membrane; Cell adhesion; Collagen;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Epidermolysis bullosa; Extracellular matrix;
Glycoprotein; Hydroxylation; Polymorphism; Protease inhibitor;
Reference proteome; Repeat; Secreted; Serine protease inhibitor;
Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 2944 Collagen alpha-1(VII) chain.
/FTId=PRO_0000005761.
DOMAIN 38 211 VWFA 1. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 234 329 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 330 416 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 417 507 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 510 597 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 600 687 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 688 775 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 778 866 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 869 957 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 958 1051 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1054 1229 VWFA 2. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 2872 2944 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 17 1253 Nonhelical region (NC1).
REGION 1254 2784 Triple-helical region.
REGION 1254 1477 Interrupted collagenous region.
REGION 2785 2944 Nonhelical region (NC2).
MOTIF 1170 1172 Cell attachment site. {ECO:0000255}.
MOTIF 1334 1336 Cell attachment site. {ECO:0000255}.
MOTIF 2008 2010 Cell attachment site. {ECO:0000255}.
MOTIF 2553 2555 Cell attachment site. {ECO:0000255}.
SITE 2886 2887 Reactive bond. {ECO:0000250}.
MOD_RES 2167 2167 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2176 2176 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2185 2185 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2188 2188 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2625 2625 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2631 2631 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2664 2664 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2667 2667 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
MOD_RES 2673 2673 4-hydroxyproline.
{ECO:0000269|PubMed:2537292}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 786 786 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1109 1109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2625 2625 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2631 2631 O-linked (Gal...) hydroxylysine;
alternate.
DISULFID 2634 2634 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00031}.
DISULFID 2802 2802 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00031}.
DISULFID 2804 2804 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00031}.
DISULFID 2876 2929 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 2885 2912 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 2904 2925 {ECO:0000255|PROSITE-ProRule:PRU00031}.
VAR_SEQ 1869 1900 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_024026.
VARIANT 119 119 T -> P (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035740.
VARIANT 142 142 K -> R (in RDEB; dbSNP:rs121912856).
/FTId=VAR_001809.
VARIANT 595 595 P -> L (in RDEB; dbSNP:rs2228561).
/FTId=VAR_001810.
VARIANT 1120 1120 R -> K (in dbSNP:rs2228563).
/FTId=VAR_048766.
VARIANT 1277 1277 P -> L (in RDEB; dbSNP:rs35761247).
/FTId=VAR_001811.
VARIANT 1347 1347 G -> R (in RDEB; localized type; mild;
dbSNP:rs121912833).
{ECO:0000269|PubMed:9804332}.
/FTId=VAR_011160.
VARIANT 1364 1364 P -> T (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035741.
VARIANT 1366 1366 R -> W (in a breast cancer sample;
somatic mutation; dbSNP:rs147089666).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035742.
VARIANT 1519 1519 G -> D (in TBDN; compound heterozygous
with E-2251; clinically silent when
heterozygous with a normal allele;
dbSNP:rs121912835).
{ECO:0000269|PubMed:9668111,
ECO:0000269|PubMed:9856844}.
/FTId=VAR_011161.
VARIANT 1522 1522 G -> E (in DDEB; dbSNP:rs387906605).
/FTId=VAR_011162.
VARIANT 1557 1557 G -> R (in DDEB).
/FTId=VAR_001812.
VARIANT 1595 1595 G -> R (in NDNC8; dbSNP:rs121912840).
{ECO:0000269|PubMed:11843659}.
/FTId=VAR_015519.
VARIANT 1604 1604 G -> R (in RDEB).
/FTId=VAR_011163.
VARIANT 1652 1652 G -> R (in RDEB; mitis type).
{ECO:0000269|PubMed:9444387}.
/FTId=VAR_011164.
VARIANT 1703 1703 G -> E (in RDEB; dbSNP:rs770304825).
/FTId=VAR_011165.
VARIANT 1772 1772 R -> W (in RDEB).
/FTId=VAR_011166.
VARIANT 1776 1776 G -> R (in DDEB).
/FTId=VAR_011167.
VARIANT 1782 1782 G -> R (in RDEB; mitis type;
dbSNP:rs374718902).
{ECO:0000269|PubMed:8618018}.
/FTId=VAR_001813.
VARIANT 1791 1791 G -> E (in EBP).
{ECO:0000269|PubMed:10383749}.
/FTId=VAR_011168.
VARIANT 1812 1812 G -> R (in RDEB).
{ECO:0000269|PubMed:10620140}.
/FTId=VAR_011169.
VARIANT 1815 1815 G -> R (in NDNC8; dbSNP:rs121912841).
{ECO:0000269|PubMed:11843659}.
/FTId=VAR_015520.
VARIANT 1845 1845 G -> R (in RDEB).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_064994.
VARIANT 1981 1981 K -> R (in RDEB; mild form).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_064995.
VARIANT 1982 1982 G -> W (in HS-DEB).
{ECO:0000269|PubMed:9326325}.
/FTId=VAR_001814.
VARIANT 2003 2003 G -> R (in DDEB; dbSNP:rs121912832).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_001815.
VARIANT 2006 2006 G -> A (in DDEB).
/FTId=VAR_011170.
VARIANT 2006 2006 G -> D (in DDEB; interferes with collagen
VII folding and secretion;
dbSNP:rs121912842).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9668111}.
/FTId=VAR_011171.
VARIANT 2008 2008 R -> C (in HS-DEB; also in a milder
localized type).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9740253}.
/FTId=VAR_011172.
VARIANT 2008 2008 R -> G (in HS-DEB).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9326325}.
/FTId=VAR_001816.
VARIANT 2009 2009 G -> R (in RDEB).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9215684}.
/FTId=VAR_011173.
VARIANT 2015 2015 G -> E (in DDEB; interferes with collagen
VII folding and secretion;
dbSNP:rs121912843).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9668111}.
/FTId=VAR_011174.
VARIANT 2025 2025 G -> A (in RDEB; mitis type;
dbSNP:rs766931219).
{ECO:0000269|PubMed:9326325}.
/FTId=VAR_001817.
VARIANT 2028 2028 G -> A (in DDEB).
{ECO:0000269|PubMed:11142768}.
/FTId=VAR_011175.
VARIANT 2028 2028 G -> R (in DDEB and EBP;
dbSNP:rs762162799).
{ECO:0000269|PubMed:10836608,
ECO:0000269|PubMed:11142768}.
/FTId=VAR_011176.
VARIANT 2031 2031 G -> S (in RDEB; severe phenotype;
dbSNP:rs121912838).
{ECO:0000269|PubMed:11167698}.
/FTId=VAR_011177.
VARIANT 2034 2034 G -> R (in DDEB and EBDSC; interferes
with collagen VII folding and secretion;
dbSNP:rs121912844).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:11874498,
ECO:0000269|PubMed:2653224,
ECO:0000269|PubMed:9668111}.
/FTId=VAR_001818.
VARIANT 2034 2034 G -> W (in DDEB).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:9856843}.
/FTId=VAR_011178.
VARIANT 2037 2037 G -> E (in P-DEB; dbSNP:rs121912846).
{ECO:0000269|PubMed:10233777}.
/FTId=VAR_011179.
VARIANT 2040 2040 G -> D (in DDEB).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_011180.
VARIANT 2040 2040 G -> S (in P-DEB; dbSNP:rs121912829).
{ECO:0000269|PubMed:8170945}.
/FTId=VAR_001819.
VARIANT 2040 2040 G -> V (in DDEB).
{ECO:0000269|PubMed:9856843}.
/FTId=VAR_011181.
VARIANT 2043 2043 G -> R (in DDEB; dbSNP:rs121912836).
{ECO:0000269|PubMed:10084325,
ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:7861014,
ECO:0000269|PubMed:9215684,
ECO:0000269|PubMed:9856843}.
/FTId=VAR_001820.
VARIANT 2043 2043 G -> W (in DDEB; localized type).
{ECO:0000269|PubMed:10084325}.
/FTId=VAR_011182.
VARIANT 2046 2046 G -> V (in DDEB).
/FTId=VAR_011183.
VARIANT 2049 2049 G -> E (in HS-DEB).
{ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:9326325}.
/FTId=VAR_001821.
VARIANT 2055 2055 G -> E (in DDEB).
/FTId=VAR_001822.
VARIANT 2063 2063 R -> W (in HS-DEB; also in a mild form;
dbSNP:rs121912849).
{ECO:0000269|PubMed:10232406,
ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:9326325}.
/FTId=VAR_001823.
VARIANT 2064 2064 G -> R (in DDEB; dbSNP:rs866061439).
{ECO:0000269|PubMed:20598510,
ECO:0000269|PubMed:9856843}.
/FTId=VAR_011184.
VARIANT 2069 2069 R -> C (in RDEB; dbSNP:rs121912855).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_064996.
VARIANT 2070 2070 G -> R (in DDEB).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_064997.
VARIANT 2073 2073 G -> D (in RDEB; mitis type).
{ECO:0000269|PubMed:8757758}.
/FTId=VAR_001825.
VARIANT 2076 2076 G -> D (in DDEB; also in recessive forms;
dbSNP:rs121912850).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_001826.
VARIANT 2079 2079 G -> E (in DDEB).
{ECO:0000269|PubMed:10232406}.
/FTId=VAR_001827.
VARIANT 2079 2079 G -> R (in DDEB; associated with squamous
cell carcinoma).
{ECO:0000269|PubMed:10232408}.
/FTId=VAR_011185.
VARIANT 2132 2132 G -> D (in RDEB; dbSNP:rs755669902).
/FTId=VAR_011186.
VARIANT 2192 2192 G -> S (in RDEB).
/FTId=VAR_011187.
VARIANT 2207 2207 G -> R (in DDEB).
{ECO:0000269|PubMed:9740253}.
/FTId=VAR_011188.
VARIANT 2221 2221 G -> A (in RDEB).
{ECO:0000269|PubMed:20108428}.
/FTId=VAR_064998.
VARIANT 2242 2242 G -> R (in EBP; dbSNP:rs121912837).
{ECO:0000269|PubMed:10383749}.
/FTId=VAR_001828.
VARIANT 2251 2251 G -> E (in TBDN; compound heterozygous
with D-1519; leads to isolated toenail
dystrophy when heterozygous with a normal
allele; dbSNP:rs121912834).
{ECO:0000269|PubMed:9856844}.
/FTId=VAR_011189.
VARIANT 2263 2263 G -> V (in RDEB).
/FTId=VAR_011190.
VARIANT 2287 2287 G -> R (in RDEB; moderately severe
phenotype when compound heterozygous with
R-2316; leads to isolated toenail
dystrophy when heterozygous with a normal
allele; dbSNP:rs121912839).
{ECO:0000269|PubMed:10469344}.
/FTId=VAR_011191.
VARIANT 2296 2296 G -> E (in RDEB).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_064999.
VARIANT 2316 2316 G -> R (in RDEB; moderately severe
phenotype when compound heterozygous with
R-2287). {ECO:0000269|PubMed:10469344}.
/FTId=VAR_011192.
VARIANT 2348 2348 G -> R (in DDEB/RDEB; mild form).
{ECO:0000269|PubMed:10232407}.
/FTId=VAR_011193.
VARIANT 2351 2351 G -> R (in a patient with dystrophic
epidermolysis bullosa; mitis type;
dbSNP:rs1800013).
/FTId=VAR_001829.
VARIANT 2366 2366 G -> S (in RDEB; mitis type).
{ECO:0000269|PubMed:10232406}.
/FTId=VAR_011194.
VARIANT 2369 2369 G -> S (in EBP).
{ECO:0000269|PubMed:10383749}.
/FTId=VAR_011195.
VARIANT 2429 2429 P -> L (in dbSNP:rs2229822).
/FTId=VAR_033786.
VARIANT 2557 2557 G -> R (in RDEB).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_065000.
VARIANT 2569 2569 G -> R (in RDEB; severe and mitis type).
/FTId=VAR_001830.
VARIANT 2575 2575 G -> R (in HS-DEB; also in a mild form;
dbSNP:rs760891216).
{ECO:0000269|PubMed:8592061,
ECO:0000269|PubMed:9326325}.
/FTId=VAR_001831.
VARIANT 2622 2622 R -> W (in RDEB; dbSNP:rs139318843).
{ECO:0000269|PubMed:20598510}.
/FTId=VAR_065001.
VARIANT 2623 2623 G -> C (in PR-DEB; dominant;
dbSNP:rs121912831).
{ECO:0000269|PubMed:8541842}.
/FTId=VAR_001832.
VARIANT 2653 2653 G -> R (in RDEB; mitis type;
dbSNP:rs121912851).
/FTId=VAR_001833.
VARIANT 2671 2671 G -> V (in RDEB).
/FTId=VAR_001834.
VARIANT 2674 2674 G -> D (in RDEB).
/FTId=VAR_011196.
VARIANT 2674 2674 G -> R (in RDEB; mitis type).
/FTId=VAR_001835.
VARIANT 2713 2713 G -> D (in DDEB; dbSNP:rs369591910).
{ECO:0000269|PubMed:9856843}.
/FTId=VAR_011197.
VARIANT 2713 2713 G -> R (in EBP).
{ECO:0000269|PubMed:10383749}.
/FTId=VAR_011198.
VARIANT 2740 2740 G -> A (in RDEB).
/FTId=VAR_011199.
VARIANT 2749 2749 G -> R (in HS-DEB; also in a mild form;
dbSNP:rs121912853).
/FTId=VAR_001836.
VARIANT 2775 2775 G -> S (in RDEB; mitis type).
{ECO:0000269|PubMed:9740253}.
/FTId=VAR_011200.
VARIANT 2791 2791 R -> W (in DDEB; dbSNP:rs142566193).
/FTId=VAR_011201.
VARIANT 2798 2798 M -> K (in HS-DEB; also in a mild form;
dbSNP:rs121912828).
{ECO:0000269|PubMed:8513326}.
/FTId=VAR_001837.
CONFLICT 195 197 FFF -> EFR (in Ref. 4; BAA02853).
{ECO:0000305}.
CONFLICT 369 371 QQQ -> EFR (in Ref. 5; AAA36357/
AAB24637). {ECO:0000305}.
CONFLICT 518 519 EL -> DV (in Ref. 5; AAA36357/AAB24637).
{ECO:0000305}.
CONFLICT 529 529 S -> C (in Ref. 4; BAA02853).
{ECO:0000305}.
CONFLICT 541 541 V -> W (in Ref. 5; AAA36357/AAB24637).
{ECO:0000305}.
CONFLICT 851 851 R -> H (in Ref. 4; BAA02853).
{ECO:0000305}.
CONFLICT 893 893 A -> E (in Ref. 1; AAA58965, 4; BAA02853
and 6; AAA96439). {ECO:0000305}.
CONFLICT 1122 1122 R -> L (in Ref. 4; BAA02853).
{ECO:0000305}.
CONFLICT 1463 1464 SP -> LR (in Ref. 3; AA sequence).
{ECO:0000305}.
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


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