COL23A1
| Collagen type XXIII, alpha 1 | ||
|---|---|---|
| other names |
|
|
| Properties of human protein | ||
| Mass / length primary structure | 540 amino acids , 51,944 Da | |
| Isoforms | 2 | |
| Identifier | ||
| Gene name | COL23A1 | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Sarcopterygii , Nothobranchiidae | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 91522 | 237759 |
| Ensemble | ENSG00000050767 | ENSMUSG00000063564 |
| UniProt | Q86Y22 | Q8K4G2 |
| Refseq (mRNA) | NM_173465 | NM_153393 |
| Refseq (protein) | NP_775736.2 | NP_700442.2 |
| Gene locus | Chr 5: 178.24 - 178.59 Mb | Chr 11: 51.29 - 51.58 Mb |
| PubMed search | 91522 |
237759
|
Collagen type XXIII, alpha 1 is a collagen with a transmembrane domain , which the gene COL23A1 is encoded. It forms homotrimers , which in turn form collagen fibrils of type XXIII.
properties
Type XXIII, alpha 1 collagen has two forms: a full-length membrane-bound form and the ectodomain shed form . The distribution of these two forms is tissue-specific. In organs such as the brain, the shed form predominates, whereas the membrane-bound form is preferred in the lungs.
Cells are able to regulate the amount of collagen XXIII in membrane-bound and shed form in order to control the production of the respective form. For this reason, shedding is described as selective proteolysis , which is mainly carried out by the protein furin , but also by enzymes such as serine or cysteine proteases. When the collagen XXIII is inside the Golgi apparatus , the protein is cleaved by the furin, creating the shed shape. This gets into the extracellular matrix through exocytosis .
But even the full-length membrane-bound form can reach the cell surface by introducing it into the plasma membrane. It is stabilized by non-collagenous, transmembrane domains outside the cell. The membrane-bound form is usually found in lipid rafts . The furin cannot reach the collagen XXIII molecules when they are inside lipid rafts. This allows collagen XXIII molecules to retain their membrane-bound form.
If these molecules lose their lipid raft protection (e.g. due to a decrease in the concentration of cholesterol ), the furin can break them down outside the cell and thus release the shed form directly into the extracellular matrix.
Web links
Individual evidence
- ↑ Guido Veit, Elena P. Zimina, Claus-Werner Franzke, Stefanie Kutsch, Udo Siebolds, Marion K. Gordon, Leena Bruckner-Tuderman, Manuel Koch: Shedding of collagen XXIII is mediated by furin and depends on the plasma membrane microenvironment . In: J Biol Chem . 282, No. 37, September 14, 2007, pp. 27424-27435. doi : 10.1074 / jbc.M703425200 . PMID 17627939 .