| IED ID | IndEnz0002001339 |
| Enzyme Type ID | protease001339 |
| Protein Name |
Sonic hedgehog protein SHH Cleaved into: Sonic hedgehog protein N-product; Sonic hedgehog protein C-product |
| Gene Name | SHH |
| Organism | Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Caudata Salamandroidea Salamandridae (newts) Pleurodelinae Cynops (firebelly newts) Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster) |
| Enzyme Sequence | MDEMILLRRVLLAGFICALLVPSGLSCGPGRGIGTRKRFKKLTPLAYKQFTPNVPEKTLGASGRYEGKITRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHFEESLHYEGRAVDITTSDRDRSKYGMLARLAAEAGFDWVYFESKAHIHCSVKAENSVAAKSGGCFPGSATVALEQGVRIPVKDLRPGDRVLAADGLGKLVYSDFLLFMDKEETVRKVFYVIETSRERVRLTAAHLLFVGQAHPGNDSGGDFRSVFGSAGFRSMFASSVRAGHRVLTVDREGRGLREATVERVYLEEATGAYAPVTAHGTVVIDRVLASCYAVIEEHSWAHWAFAPLRVGLGILSFFSPQDYSSHSPPAPSQSEGVHWYSEILYRIGTWVLQEDTIHPLGMAAKSS |
| Enzyme Length | 432 |
| Uniprot Accession Number | Q90385 |
| 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 and metamorphosis. Involved in limb formation, patterning of the central nervous system and ventral somite differentiation. Induces ectopic cement gland formation in embryos. 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 (3); Lipidation (2); Metal binding (12); Signal peptide (1); Site (3) |
| Keywords | Autocatalytic cleavage;Calcium;Cell membrane;Developmental protein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Palmitate;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | INDUCTION: Activated by activin, basic fibroblast growth factor (BFGF) and fork head. |
| Subcellular Location | SUBCELLULAR LOCATION: [Sonic hedgehog protein C-product]: Secreted, extracellular space {ECO:0000250|UniProtKB:Q62226}. Note=The C-terminal peptide diffuses from the cell. {ECO:0000250|UniProtKB:Q62226}.; SUBCELLULAR LOCATION: [Sonic hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=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|UniProtKB:Q62226}. |
| 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 of Cys-27 by HHAT is required for N-product multimerization and full activity. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,847 |
| Kinetics | |
| Metal Binding | METAL 92; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 93; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 93; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 98; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 128; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 129; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 129; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 132; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 134; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 143; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 150; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 185; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q15465 |
| Rhea ID | |
| Cross Reference Brenda |