| ENSCAFG00000005386 |
GO:0005518 |
collagen binding |
Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
IEA |
molecular_function |
| ENSCAFG00000005386 |
GO:0005518 |
collagen binding |
Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
IBA |
molecular_function |
| ENSCAFG00000005386 |
GO:0004867 |
serine-type endopeptidase inhibitor activity |
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
IBA |
molecular_function |
| ENSCAFG00000005386 |
GO:0004867 |
serine-type endopeptidase inhibitor activity |
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
IEA |
molecular_function |
| ENSCAFG00000005386 |
GO:0003723 |
RNA binding |
Interacting selectively and non-covalently with an RNA molecule or a portion thereof. |
IEA |
molecular_function |
| ENSCAFG00000005386 |
GO:0051082 |
unfolded protein binding |
Interacting selectively and non-covalently with an unfolded protein. |
IEA |
molecular_function |