Complete primary structure and genomic organization of the mouse Col14a1 gene

被引:8
作者
Gerecke, DR
Meng, XM
Liu, B
Birk, DE
机构
[1] Thomas Jefferson Univ, Dept Pathol Anat & Cell Biol, Philadelphia, PA 19107 USA
[2] Rutgers State Univ, Ernest Mario Sch Pharm, Dept Pharmacol & Toxicol, Environm & Occupat Hlth Sci Inst, Piscataway, NJ 08854 USA
关键词
type XIV collagen; mouse; cDNA sequence; genomic organization;
D O I
10.1016/S0945-053X(03)00021-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The entire mouse cDNA sequence for type XIV collagen was determined using overlapping PCR products. The 6456 nucleotide (nt) cDNA sequence contains a 5391-nt open reading frame encoding 1797 amino acid residues. The amino terminus has a 28-residue signal peptide that is followed by the mature polypeptide of 1769 amino acid residues with a calculated molecular mass of 193.2 kDa. The mouse alpha1(XIV) collagen chain is predicted to contain all the structural domains described for the polypeptide in chicken and human. These include fibronectin type III repeats, von Willebrand factor A domains, thrombospondin-N-terminal-like domains and two triple-helical domains similar to those of other collagen family members. The amino acid residue sequence of human alpha1(XIV) collagen showed an overall identity of 74% to the chicken sequence and 88% to the human sequence. The entire mouse genomic structure has been determined and is made up of 48 exons. Alternatively spliced forms of mouse type XIV, collagen were not identified corresponding to the findings for the human form. (C) 2003 Elsevier Science B.V and International Society of Matrix Biology. All rights reserved.
引用
收藏
页码:209 / 216
页数:8
相关论文
共 25 条
[1]
Complete primary structure of human collagen type XIV (undulin) [J].
Bauer, M ;
Dieterich, W ;
Ehnis, T ;
Schuppan, D .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1997, 1354 (03) :183-188
[2]
Differential expression of collagens XII and XIV in human skin and in reconstructed skin [J].
Berthod, F ;
Germain, L ;
Guignard, R ;
Lethias, C ;
Garrone, R ;
Damour, O ;
vanderRest, M ;
Auger, FA .
JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1997, 108 (05) :737-742
[3]
STRUCTURE AND BINDING-PROPERTIES OF COLLAGEN TYPE-XIV ISOLATED FROM HUMAN PLACENTA [J].
BROWN, JC ;
MANN, K ;
WIEDEMANN, H ;
TIMPL, R .
JOURNAL OF CELL BIOLOGY, 1993, 120 (02) :557-567
[4]
CASTAGNOLA P, 1992, EUR J CELL BIOL, V59, P340
[5]
DUBLET B, 1991, J BIOL CHEM, V266, P6853
[6]
GERECKE DR, 1993, J BIOL CHEM, V268, P12177
[7]
Gordon MK, 1996, DEV DYNAM, V206, P49, DOI 10.1002/(SICI)1097-0177(199605)206:1<49::AID-AJA5>3.0.CO
[8]
2-0
[9]
GORDON MK, 1989, J BIOL CHEM, V264, P19772
[10]
Alternative splicing of the first F3 domain from chicken collagen XIV affects cell adhesion and heparin binding [J].
Imhof, M ;
Trueb, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (12) :9141-9148