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Details on Person Type XIII is a non-fibril-forming type II transmembrane prot...

Class:IdSummation:2167967
_displayNameType XIII is a non-fibril-forming type II transmembrane prot...
_timestamp2012-09-27 09:18:17
created[InstanceEdit:2168010] Jupe, S, 2012-03-23
literatureReference[LiteratureReference:2143431] Type XIII collagen is identified as a plasma membrane protein
[LiteratureReference:2143429] Type XIII collagen forms homotrimers with three triple helical collagenous domains and its association into disulfide-bonded trimers is enhanced by prolyl 4-hydroxylase
[LiteratureReference:2168007] Type XIII collagen: a novel cell adhesion component present in a range of cell-matrix adhesions and in the intercalated discs between cardiac muscle cells
[LiteratureReference:2168026] Muscle-derived collagen XIII regulates maturation of the skeletal neuromuscular junction
[LiteratureReference:2167953] Distinct recognition of collagen subtypes by alpha(1)beta(1) and alpha(2)beta(1) integrins. Alpha(1)beta(1) mediates cell adhesion to type XIII collagen
[LiteratureReference:2471898] A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins
[LiteratureReference:2471920] The shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner
[LiteratureReference:2471894] The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin
[LiteratureReference:2471846] The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro
modified[InstanceEdit:2168943] Jupe, S, 2012-03-26
[InstanceEdit:2471915] Jupe, S, 2012-09-21
[InstanceEdit:2484928] Jupe, S, 2012-09-27
textType XIII is a non-fibril-forming type II transmembrane protein with a large amino terminal NC1 domain. This domain has a hydrophobic membrane-spanning segment that anchors the molecule to the plasma membrane and a large extracellular, mostly collagenous carboxyterminal domain (Hägg et al. 1998). Recombinant type XIII collagen can form homotrimers with triple-helical collagenous domains (Snellman et al. 2000a). It is detected at low levels in all connective tissue-producing cells; in cultured cells it is localized in focal adhesions (Hägg et al. 2001). The extracellular region has an adhesion-related function (Hägg et al. 2001) that is involved in formation of the neuromuscular junction (Latvanlehto et al. 2010). The purified protein has been shown to interact with Integrin alpha1beta1 (Nykvist et al. 2000). An N-terminal ectodomain portion of type XIII collagen is cleaved in culture medium by a furin-like protease (Snellman et al. 2000b, Väisänen et al. 2004). This ectodomain interacts with fibronectin, nidogen-2 and perlecan (Tu et al. 2002, Väisänen et al. 2006).
(summation)[BlackBoxEvent:2167942] Collagen type XIII ectodomain shedding [Homo sapiens]
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