Detail Information for IndEnz0002003384
IED ID IndEnz0002003384
Enzyme Type ID protease003384
Protein Name Protein hedgehog
Cleaved into: Protein hedgehog N-product; Protein hedgehog C-product
Gene Name hh GK12833
Organism Drosophila willistoni (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) Sophophora willistoni group willistoni subgroup Drosophila willistoni (Fruit fly)
Enzyme Sequence MDSQSNQTPWASASVTCLSLDAKRHSQCLDDAIKSGHQVNYSPARSLRYIAYTQRCGIRLTMLMLIMCLTFMPAHSCGPGRGLGRRRVQNLYPLVLKQTVPNLSEHQLGASGPLEGEIPRDSPKFKDLVPNYNRDIVFKDEEGTGADRLMTKRCREKLNALAYSVMNEWPGVRLLVIESWDEDHDHGQESLHYEGRAVTIGTNDRDLSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSTISHVHGCFTPESTAQMENGEKKPLSQLSIGDRVLSMGSNGQPVYSEVILFMDRNLEQLENFVQLHTDGGAVLTVTPAHLISVWQPDSQQLNYVFADRVEEMNYVLVNDVVTGELLPQRVIKVTSVHSKGVVAPLTREGTIVVNSVVASCYAVINSQSLAHWGLAPMRLLSSLQSLMPAKGQLRTTSSATQPTKEVSRAEQQNGIHWYANALYKVKDYVLPKSWRHE
Enzyme Length 469
Uniprot Accession Number B4NJP3
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); Lipidation (2); Metal binding (8); Propeptide (1); Signal peptide (1); Site (4)
Keywords Autocatalytic cleavage;Calcium;Cell membrane;Cytoplasm;Developmental protein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Morphogen;Nucleus;Palmitate;Protease;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..?; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 52,389
Kinetics
Metal Binding METAL 141; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 142; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 142; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 147; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 178; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 178; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 181; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465; METAL 183; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q15465
Rhea ID
Cross Reference Brenda