| IED ID | IndEnz0002015334 |
| Enzyme Type ID | protease015334 |
| Protein Name |
Indian hedgehog protein IHH Fragment |
| Gene Name | ihh |
| Organism | Devario malabaricus (Malabar danio) (Danio malabaricus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Devario Devario malabaricus (Malabar danio) (Danio malabaricus) |
| Enzyme Sequence | VMNLWPGIRLRVTEGWDEDGHHSEESLHYEGRAVDITTEDRDRNKYAMLARLAVEAGF |
| Enzyme Length | 58 |
| Uniprot Accession Number | O13215 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Intercellular signal essential for a variety of patterning events during development. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (7); Non-terminal residue (2) |
| Keywords | Autocatalytic cleavage;Calcium;Cell membrane;Developmental protein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Palmitate;Protease;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Note=Indian hedgehog protein N-product: Cell membrane; Lipid-anchor; Extracellular side. The N-terminal peptide remains associated with the cell surface. Indian hedgehog protein C-product: Secreted, extracellular space. The C-terminal peptide diffuses from the cell. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (N-product). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250}.; PTM: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250}.; PTM: N-palmitoylation is required for N-product multimerization and full activity. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,714 |
| Kinetics | |
| Metal Binding | METAL 13; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 14; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 14; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 17; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 19; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 28; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q14623; METAL 35; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q14623 |
| Rhea ID | |
| Cross Reference Brenda |