Collagen alpha-1(VII) chain
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.
Involvement in disease
Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen.
Epidermolysis bullosa dystrophica, autosomal dominant
DDEB
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Epidermolysis bullosa dystrophica, autosomal recessive
RDEB
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, such as epidermolysis bullosa dystrophica Hallopeau-Siemens type, to mild forms with limited localized scarring and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.
None
The disease is caused by variants affecting the gene represented in this entry.
Transient bullous dermolysis of the newborn
TBDN
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Epidermolysis bullosa dystrophica, pretibial type
PR-DEB
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Epidermolysis bullosa dystrophica, Bart type
B-DEB
An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
None
The disease is caused by variants affecting the gene represented in this entry.
Epidermolysis bullosa pruriginosa
EBP
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Nail disorder, non-syndromic congenital, 8
NDNC8
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Epidermolysis bullosa dystrophica, with subcorneal cleavage
EBDSC
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
- Basement membrane
Alternative names
Collagen alpha-1(VII) chain, Long-chain collagen, LC collagen, COL7A1