| IED ID | IndEnz0002001743 |
| Enzyme Type ID | protease001743 |
| Protein Name |
Sonic hedgehog protein SHH Fragment |
| Gene Name | shh |
| Organism | Pseudorasbora parva |
| 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 Gobionidae Sarcocheilichthyinae Pseudorasbora Pseudorasbora parva |
| Enzyme Sequence | VMNQWPGVNLRVTEGWDEDGHHFEESLHYEGRAVDITTSDRDKSKYGTLSRLAVEAGF |
| Enzyme Length | 58 |
| Uniprot Accession Number | P79839 |
| 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. Signal produced by the notochord that induces somite patterning, dorso-ventral patterning of the brain and early patterning of the developing eyes. Displays floor plate-inducing activity. Binds to the patched (PTC) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTC represses the constitutive signaling activity of SMO (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;Lipoprotein;Membrane;Metal-binding;Palmitate;Protease;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Sonic hedgehog protein C-product: Secreted, extracellular space. Sonic hedgehog protein N-product: Cell membrane; Lipid-anchor. The C-terminal peptide diffuses from the cell, while the N-product either remains associated with lipid rafts at the cell surface, or forms freely diffusible active multimers with its hydrophobic lipid-modified N- and C-termini buried inside. {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.; 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 | 6,608 |
| Kinetics | |
| Metal Binding | METAL 13; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 14; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 14; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 17; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 19; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 28; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 35; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465 |
| Rhea ID | |
| Cross Reference Brenda |