COL17A1

COL17A1 (Collagen Type XVII Alpha 1 Chain) is a Protein Coding gene. Diseases associated with COL17A1 include Epithelial Recurrent Erosion Dystrophy and Epidermolysis Bullosa, Junctional, Non-Herlitz Type. Among its related pathways are Integrin Pathway and ERK Signaling. An important paralog of this gene is COL28A1.

Full Name

Collagen Type XVII Alpha 1 Chain

Function

May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.

The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies.

Biological Process

Cell-matrix adhesion Source: ProtInc
Collagen fibril organization Source: Reactome
Epidermis development Source: ProtInc
Extracellular matrix organization Source: GO_Central
Hemidesmosome assembly Source: UniProtKB
Regulation of immune response Source: Reactome

Cellular Location

Hemidesmosome; Membrane. Localized along the plasma membrane of the hemidesmosome.
120 kDa linear IgA disease antigen: Basement membrane. Exclusively localized to anchoring filaments. Localized to the epidermal side of split skin.
97 kDa linear IgA disease antigen: Basement membrane. Localized in the lamina lucida beneath the hemidesmosomes.

Involvement in disease

Generalized atrophic benign epidermolysis bullosa (GABEB):
A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.
Epithelial recurrent erosion dystrophy (ERED):
A corneal dystrophy characterized by recurrent episodes of epithelial erosions from childhood, with occasional impairment of vision. Most patients have attacks of redness, photophobia, epiphora, and ocular pain. Exposure to sunlight or draught, dust and smoke and lack of sleep can precipitate attacks.

Topology

Cytoplasmic: 1-467
Helical: 468-488
Extracellular: 489-1497

PTM

The intracellular/endo domain is disulfide-linked.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen. The shedding is mediated by membrane-bound metalloproteases. This cleavage is inhibited by phosphorylation at Ser-544.