Collagen Type XIII (COL13)

COL13A1; COL13-A1; Collagen Alpha-1(XIII)chain

SPN	U706
HGNC	2190
MGI	1277201
PubMed	9417920
RGD	1595704
UniProt	Q5TAT6
Wiki	COL13A1

Collagen alpha-1(XIII) chain is the alpha chain of one of the nonfibrillar collagens. The function of this gene product is not known, however, it has been detected at low levels in all connective tissue-producing cells so it may serve a general function in connective tissues. Unlike most of the collagens, which are secreted into the extracellular matrix, collagen XIII contains a transmembrane domain and the protein has been localized to the plasma membrane. The transcripts for this gene undergo complex and extensive splicing involving at least eight exons. Like other collagens, collagen XIII is a trimer; it is not known whether this trimer is composed of one or more than one alpha chain isomer. A number of alternatively spliced transcript variants have been described, but the full length nature of some of them has not been determined.

Reference

"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."
EMBO J. 19:5051-5059(2000) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and comparative analysis of human chromosome 10."
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"The alpha 1 chain of type XIII collagen consists of three collagenous and four noncollagenous domains, and its primary transcript undergoes complex alternative splicing."
J. Biol. Chem. 265:16922-16928(1990) [PubMed] [Europe PMC] [Abstract].

"Partial characterization of a low molecular weight human collagen that undergoes alternative splicing."
Proc. Natl. Acad. Sci. U.S.A. 84:940-944(1987) [PubMed] [Europe PMC] [Abstract].

"Gene structure for the alpha 1 chain of a human short-chain collagen (type XIII) with alternatively spliced transcripts and translation termination codon at the 5' end of the last exon."
Proc. Natl. Acad. Sci. U.S.A. 85:7491-7495(1988) [PubMed] [Europe PMC] [Abstract]

"Characterization of the spectrum of alternative splicing of alpha 1 (XIII) collagen transcripts in HT-1080 cells and calvarial tissue resulted in identification of two previously unidentified alternatively spliced sequences, one previously unidentified exon, and nine new mRNA variants."
J. Biol. Chem. 267:24693-24699(1992) [PubMed] [Europe PMC] [Abstract]

"Patterns of expression of the six alternatively spliced exons affecting the structures of the COL1 and NC2 domains of the alpha 1(XIII) collagen chain in human tissues and cell lines."
J. Biol. Chem. 267:24700-24707(1992) [PubMed] [Europe PMC] [Abstract]

"Location and alternative splicing of type XIII collagen RNA in the early human placenta."
Lab. Invest. 69:541-551(1993) [PubMed] [Europe PMC] [Abstract]

"Type XIII collagen is widely expressed in the adult and developing human eye and accentuated in the ciliary muscle, the optic nerve and the neural retina."
Exp. Eye Res. 70:401-410(2000) [PubMed] [Europe PMC] [Abstract]

"The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin."
J. Biol. Chem. 277:23092-23099(2002) [PubMed] [Europe PMC] [Abstract]