| IED ID | IndEnz0002015404 |
| Enzyme Type ID | protease015404 |
| Protein Name |
Protein hedgehog Cleaved into: Protein hedgehog N-product; Protein hedgehog C-product |
| Gene Name | hh GJ22641 |
| Organism | Drosophila virilis (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Drosophila virilis group Drosophila virilis (Fruit fly) |
| Enzyme Sequence | MDNQTVAAIWSCASATCLSLDAKRHSVETNTNDRQAPPGLSNSNNNNNNNKSTAVDADPRKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYMSGASGPIEGVIQRDSPNFKDLVPNYNRDIIFRDEEGTGADRLMSKRCREKLNTLSYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPFISHVHGCFTPESTALLESGAKKPLSELAIGDRVLSMNGKGQAVYSEVILFMDRNLEQMQNFVQLHTDSGAVLTVTPAHLITVWQPEREALDFVFADRVEELNYVLVHDATGELRPHRVIRVSSVRSRGVVAPLTREGTIVVDSVAASCYAVISSQSLAHWGLAPMRLLYTLQSWMPAKGQLRTAQDKSTPKDATAQQQNGLHWYANALYKVKDYVLPQSWRHD |
| Enzyme Length | 483 |
| Uniprot Accession Number | B4LZT9 |
| 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. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu) (By similarity). {ECO:0000250|UniProtKB:Q02936}.; FUNCTION: The hedgehog protein N-product constitutes the active species in both local and long-range signaling, whereas the C-terminal product has no signaling activity. It acts as a morphogen, and diffuses long distances despite its lipidation. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation (By similarity). {ECO:0000250|UniProtKB:Q02936}.; FUNCTION: The hedgehog protein C-product, which mediates the autocatalytic activity, has no signaling activity. {ECO:0000250|UniProtKB:Q02936}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Compositional bias (1); Lipidation (2); Metal binding (9); Propeptide (1); Region (1); Signal peptide (1); Site (4) |
| Keywords | Autocatalytic cleavage;Calcium;Cell membrane;Cytoplasm;Developmental protein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Morphogen;Nucleus;Palmitate;Protease;Reference proteome;Secreted;Segmentation polarity protein;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}; Extracellular side {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog C-product]: Secreted, extracellular space {ECO:0000250|UniProtKB:Q02936}. |
| Modified Residue | |
| Post Translational Modification | PTM: The C-terminal domain displays autoproteolytic activity. Cleavage of the full-length hedgehog protein is followed by the covalent attachment of a cholesterol moiety to the C-terminus of the newly generated N-terminal fragment (N-product) (By similarity). {ECO:0000250}.; PTM: Cholesterol attachment plays an essential role in restricting the spatial distribution of hedgehog activity to the cell surface. {ECO:0000250}.; PTM: N-terminal palmitoylation of the hedgehog N-product is required for the embryonic and larval patterning activities of the hedgehog signal. Rasp acts within the secretory pathway to catalyze the N-terminal palmitoylation of Hh (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,979 |
| Kinetics | |
| Metal Binding | METAL 157; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 158; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 158; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 163; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 193; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 194; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 194; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 197; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 199; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465 |
| Rhea ID | |
| Cross Reference Brenda |