COL11A1
| Collagen type XI, alpha1 | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 181,065 Daltons / 1,806 amino acids (Isoform1)
182,422 Daltons / 1,818 amino acids (Isoform2) 176,619 Daltons / 1,767 amino acids (Isoform3) 167,752 Daltons / 1,690 amino acids (Isoform4) |
|
| Isoforms | 4th | |
| Identifier | ||
| Gene names | COL11A1 COLL6 | |
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 1301 | 12814 |
| Ensemble | ENSG00000060718 | ENSMUSG00000027966 |
| UniProt | P12107 | Q61245 |
| Refseq (mRNA) | NM_001190709 | NM_007729 |
| Refseq (protein) | NP_001177638 | NP_031755 |
| Gene locus | Chr 1: 102.88 - 103.11 Mb | Chr 3: 114.03 - 114.22 Mb |
| PubMed search | 1301 |
12814
|
Type XI, alpha1 collagen is a protein encoded by the COL11A1 gene . It represents the α1 chain of type XI collagen; the second chain is encoded by COL11A2 , while the third α chain is a post-translationally modified α1 chain of collagen type II. Mutations in this gene can lead to type II Stickler syndrome or Marshall syndrome .
Basic information on collagen synthesis
The collagen synthesis takes place in various cells ( fibroblasts , osteoblasts , myofibroblasts , chondroblasts , odontoblasts , but also in epithelial cells , endothelial cells and smooth muscle cells ). Inside the cells, the site of collagen synthesis is the endoplasmic reticulum . There, with the help of the mRNA and ribosomes, amino acids are linked by covalent bonds and two α1 chains and one α2 chain are formed. In the further course, these three α-chains connect with each other in a right-handed spiral and form a collagen molecule, which is ultimately what the collagen fibers consist of.
The COL11A1 gene codes for the α1 chain of type XI collagen.
Individual evidence
- ↑ a b COL11A1 collagen, type XI, alpha 1 (human)
- ↑ Frans van den Berg: Applied Physiology . 3. Edition. tape 1 : Understand and influence the connective tissue of the musculoskeletal system. Thieme, Stuttgart 2011, ISBN 978-3-13-116033-1 , p. 38 .