Description: Homo sapiens collagen, type I, alpha 1 (COL1A1), mRNA. RefSeq Summary (NM_000088): This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]. Sequence Note: The RefSeq transcript was derived from the reference genome assembly. The genomic coordinates were determined from alignments. Transcript (Including UTRs) Position: hg19 chr17:48,261,457-48,279,000 Size: 17,544 Total Exon Count: 51 Strand: - Coding Region Position: hg19 chr17:48,262,863-48,278,874 Size: 16,012 Coding Exon Count: 51
ID:CO1A1_HUMAN DESCRIPTION: RecName: Full=Collagen alpha-1(I) chain; AltName: Full=Alpha-1 type I collagen; Flags: Precursor; FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. DISEASE: Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:114000]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. DISEASE: Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. DISEASE: Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:130060]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:166200]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:166210]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:259420]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:166220]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. DISEASE: Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:166710]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture. DISEASE: Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. SIMILARITY: Belongs to the fibrillar collagen family. SIMILARITY: Contains 1 fibrillar collagen NC1 domain. SIMILARITY: Contains 1 VWFC domain. SEQUENCE CAUTION: Sequence=BAD92834.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=Collagen type I alpha 1 (COL1A1); URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A1"; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/COL1A1ID186.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/COL1A1"; WEB RESOURCE: Name=Wikipedia; Note=Type-I collagen entry; URL="http://en.wikipedia.org/wiki/Type-I_collagen";
achondroplasia Fathman CG et al. 1985, Nonrandom association of a type II procollagen genotype with achondroplasia., Proceedings of the National Academy of Sciences of the United States of America. 1985 Aug;82(16):5465-9.
[PubMed 2991928]
betaCL osteocalcin , Relations between VDR3 and COL1A1 genes and markers of bone tissue metabolism in patients with chronic obstructive pulmonary disease, Ter Arkh 2006 78(3) 17-20.
[PubMed 17019952]
Testing of VDR3 and COL1A1 genes gives grounds for detection of predisposition to development of pulmonogenic osteopenic syndrome.
bone characteristics van der Sluis IM et al. 2002, Collagen Ialpha1 polymorphism is associated with bone characteristics in Caucasian children and young adults., Calcified tissue international. 2002 Nov;71(5):393-9.
[PubMed 12232678]
In conclusion, the COLIA1 polymorphism in children and young adults is associated with several bone characteristics. However, at least a part of the COLIA1 effect on bone mass may be related to differences in frame size.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P02452
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.