| IED ID | IndEnz0002013350 |
| Enzyme Type ID | protease013350 |
| Protein Name |
Tiggy-winkle hedgehog protein Fragment |
| Gene Name | twhh |
| Organism | Carassius auratus (Goldfish) |
| 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 Cyprinidae Cyprininae Carassius Carassius auratus (Goldfish) |
| Enzyme Sequence | NSLAISVMNQWPGVKLRVTEGWDEDGHHFEESLHYEGRAVDITTSDRDKSKYG |
| Enzyme Length | 53 |
| Uniprot Accession Number | P79696 |
| 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. Involved in dorso-ventral patterning of the brain and in early patterning of the developing eyes (By similarity). {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;Membrane;Metal-binding;Protease;Reference proteome;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Note=Tiggy-winkle hedgehog protein N-product: Cell membrane; Lipid-anchor; Extracellular side. The N-terminal peptide remains associated with the cell surface. Tiggy-winkle 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). This covalent modification appears to play an essential role in restricting the spatial distribution of the protein activity to the cell surface. 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}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,063 |
| Kinetics | |
| Metal Binding | METAL 19; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 20; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 20; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 23; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 25; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 34; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 41; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465 |
| Rhea ID | |
| Cross Reference Brenda |