COL13A1

Collagen, type XIII, alpha 1, also known as COL13A1, is a human gene.

PBB_Summary
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summary_text = This gene encodes 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.cite web | title = Entrez Gene: COL13A1 collagen, type XIII, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1305| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Juvonen M, Pihlajaniemi T |title=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. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24693–9 |year= 1992 |pmid= 1447209 |doi=
*cite journal | author=Juvonen M, Sandberg M, Pihlajaniemi T |title=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. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24700–7 |year= 1992 |pmid= 1447210 |doi=
*cite journal | author=Pihlajaniemi T, Tamminen M |title=The alpha 1 chain of type XIII collagen consists of three collagenous and four noncollagenous domains, and its primary transcript undergoes complex alternative splicing. |journal=J. Biol. Chem. |volume=265 |issue= 28 |pages= 16922–8 |year= 1990 |pmid= 1698771 |doi=
*cite journal | author=Tikka L, Elomaa O, Pihlajaniemi T, Tryggvason K |title=Human alpha 1 (XIII) collagen gene. Multiple forms of the gene transcripts are generated through complex alternative splicing of several short exons. |journal=J. Biol. Chem. |volume=266 |issue= 26 |pages= 17713–9 |year= 1991 |pmid= 1894651 |doi=
*cite journal | author=Tikka L, Pihlajaniemi T, Henttu P, "et al." |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 20 |pages= 7491–5 |year= 1988 |pmid= 2459707 |doi=10.1073/pnas.85.20.7491
*cite journal | author=Shows TB, Tikka L, Byers MG, "et al." |title=Assignment of the human collagen alpha 1 (XIII) chain gene (COL13A1) to the q22 region of chromosome 10. |journal=Genomics |volume=5 |issue= 1 |pages= 128–33 |year= 1989 |pmid= 2767682 |doi=10.1016/0888-7543(89)90096-7
*cite journal | author=Pihlajaniemi T, Myllylä R, Seyer J, "et al." |title=Partial characterization of a low molecular weight human collagen that undergoes alternative splicing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 4 |pages= 940–4 |year= 1987 |pmid= 3547403 |doi=10.1073/pnas.84.4.940
*cite journal | author=Juvonen M, Pihlajaniemi T, Autio-Harmainen H |title=Location and alternative splicing of type XIII collagen RNA in the early human placenta. |journal=Lab. Invest. |volume=69 |issue= 5 |pages= 541–51 |year= 1994 |pmid= 8246446 |doi=
*cite journal | author=Hägg P, Rehn M, Huhtala P, "et al." |title=Type XIII collagen is identified as a plasma membrane protein. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15590–7 |year= 1998 |pmid= 9624150 |doi=10.1074/jbc.273.25.15590
*cite journal | author=Kvist AP, Latvanlehto A, Sund M, "et al." |title=Complete exon-intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue. |journal=Matrix Biol. |volume=18 |issue= 3 |pages= 261–74 |year= 1999 |pmid= 10429945 |doi=10.1016/S0945-053X(99)00018-9
*cite journal | author=Nykvist P, Tu H, Ivaska J, "et al." |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 8255–61 |year= 2000 |pmid= 10713152 |doi=10.1074/jbc.275.11.8255
*cite journal | author=Sandberg-Lall M, Hägg PO, Wahlström I, Pihlajaniemi T |title=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. |journal=Exp. Eye Res. |volume=70 |issue= 4 |pages= 401–10 |year= 2000 |pmid= 10865988 |doi= 10.1006/exer.1998.0826
*cite journal | author=Tu H, Sasaki T, Snellman A, "et al." |title=The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 23092–9 |year= 2002 |pmid= 11956183 |doi= 10.1074/jbc.M107583200
*cite journal | author=Latvanlehto A, Snellman A, Tu H, Pihlajaniemi T |title=Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains. |journal=J. Biol. Chem. |volume=278 |issue= 39 |pages= 37590–9 |year= 2003 |pmid= 12832406 |doi= 10.1074/jbc.M305974200

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