The domain within your query sequence starts at position 157 and ends at position 254; the E-value for the LINK domain shown below is 2.22e-56.
TGVVFHYRAARDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVR YPITQSRPGCYGDRSSLPGVRSYGRRDPQELYDVYCFA
LINKLink (Hyaluronan-binding) |
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SMART accession number: | SM00445 |
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Description: | - |
Interpro abstract (IPR000538): | The link domain [ (PUBMED:8318021) ] is a hyaluronan(HA)-binding region found in proteins of vertebrates that are involved in the assembly of extracellular matrix, cell adhesion, and migration. The structure has been shown [ (PUBMED:8797823) ] to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core similar to that of C-type lectin. This domain contains four conserved cysteines involved in two disulphide bonds. The link domain has also been termed HABM [ (PUBMED:8318021) ] (HA binding module) and PTR [ (PUBMED:8690089) ] (proteoglycan tandem repeat). Proteins with such a domain include the proteoglycans aggrecan, brevican, neurocan and versican, which are expressed in the CNS; the cartilage link protein (LP), a proteoglycan that together with HA and aggrecan forms multimolecular aggregates; Tumour necrosis factor-inducible protein TSG-6, which may be involved in cell-cell and cell-matrix interactions during inflammation and tumourgenesis; and CD44 antigen, the main cell surface receptor for HA. |
GO process: | cell adhesion (GO:0007155) |
GO function: | hyaluronic acid binding (GO:0005540) |
Family alignment: |
There are 10282 LINK domains in 6262 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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