Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. (updated: March 4, 2015)
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No sequence conservation computed yet.
Total structural coverage: 92%
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The reference OMIM entry for this protein is 600943
Serpin peptidase inhibitor, clade h, member 1; serpinh1
Collagen-binding protein 2; cbp2
Colligin 2
Serpinh2
Heat-shock protein 47; hsp47
Rheumatoid arthritis antigen-a47; ra-a47 cbp1, included
DESCRIPTION
Collagen-binding proteins, or colligins, are glycoproteins that bind specifically to collagen type I (e.g.,
120150,
120160), collagen type IV (e.g.,
120130), and gelatin. Colligins are characterized by an amino acid structure that includes an N-terminal hydrophobic signal sequence and 2 putative N-linked oligosaccharide attachment sites (Clarke et al., 1991). Colligins also have a C-terminal RDEL sequence that acts as an endoplasmic reticulum (ER) retention sequence. Other features permit the colligin-binding protein of ER to be classified as a serpin (serine-arginine protease inhibitor).
CLONING
Ikegawa et al. (1995) isolated and characterized a full-length human cDNA clone that encodes a 418-amino acid peptide highly homologous (97% identity) to the human colligin-1 gene (CBP1) reported by Clarke and Sanwal (1992). Nagai et al. (1999) later found that CBP1 is not transcribed and represents a pseudogene located on chromosome 9. Ikegawa et al. (1995) called the novel gene colligin-2 and identified a genomic clone that contained the entire coding sequence of the cDNA. The authors found that the colligin-2 gene is expressed ubiquitously among all normal human tissues except brain and circulating leukocytes. Nagai et al. (1999) cloned CBP2 from a human skin fibroblast cDNA library using mouse Hsp47 cDNA as probe. By sequence analysis, they determined that CBP2 and Hsp47 are identical.
GENE STRUCTURE
Ikegawa and Nakamura (1997) found that the CBP2 gene spans approximately 11 kb of genomic DNA and contains 5 exons.
MAPPING
By fluorescence in situ hybridization Ikegawa et al. (1995) determined that the CBP2 gene maps to chromosome 11q13.5.
GENE FUNCTION
Ikegawa and Nakamura (1997) noted that the promoter sequence of the human CBP2 gene shows significant homology to that of its murine counterpart, which contains several regulatory sequences including heat-shock and retinoic acid-responsive elements. The findings suggested that colligin may function as a collagen-specific molecular chaperone and play a role in the process of retinoic acid-induced differentiation. Hattori et al. (1998) found that CBP2, synthesized by a chondrocytic cell line, is recognized as an antigen by sera from rheumatoid arthritis (RA;
180300) patients. They designated the protein RA-A47 due to its apparent molecular mass of 47 kD by SDS/PAGE. They also found that heat-shock treatment or exposure of cells to TGF-beta (see
190180) enhanced the expression of a 2-kb CBP2 transcript. Tasab et al. (2000) presented evidence that mammalian CBP2, which they called Hsp47, preferentially interacted with triple-helical procollagen molecules in vitro. The association of CBP2 with procollagen coincided with the formation of a collagen triple helix. Yasuda et al. (2002) found that, in mice, Kruppel-like factor Zf9 (
602053) regulated the transcription of Cbp2 by binding the BS5-B promoter element in cooperation with Sp2 (
601801) and/or Sp3 (
601804). In an individual with a severe deforming form of OI (OI10;
613848), Christiansen et al. (2010) identified a homozygous mutation in the SERPINH1 gene (
600943.0002) that resulted in degradation of the endoplasmic reticulum resident HSP47 via proteasome. Type I procollagen accumulated in the Golgi of fibroblasts from the affected individual and a population of the secreted type I procollagen was protease sensitive. Christiansen et al. (2010) suggested that HSP47 monitors the inte ...
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Subscribe to this protein entry history
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600943 was added.