IED ID | IndEnz0002016414 |
Enzyme Type ID | protease016414 |
Protein Name |
Desert hedgehog protein A Cephalic hedgehog protein Desert hedgehog protein 1 DHH-1 X-CHH Cleaved into: Desert hedgehog protein A N-product; Desert hedgehog protein A C-product |
Gene Name | dhh-a chh |
Organism | Xenopus laevis (African clawed frog) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
Enzyme Sequence | MPAVRIVILAICCGLLLVPVRCCGPGRGPVGRRRYMRKLVPLHYKQFVPNVPEKTLGASGKSEGKIHRGSERFIELVPNYNPDIIFKDEEKTGADRLMTERCKDRVNALAISVMNMWPGVKLRVTEGWDEDGHHAHDSLHYEGRALDITTSDRDRNKYGMLARLAVEAGFDWVYYESKAHIHVSVKADNSLGVRSGGCFPGTAMVMMGTGERKPLSELKIGDTVYTTDETGQLITSVVLLFLHRNPYKTATFVLIEAEGHPSKLLVTPNHLLFIQSSSSAGFLPTFAYRVQIGDLVQIYVNGTQVQSSKVVRVSLEEQTGVYAPMTEHGTLLVDGVLTSCYATVESHTLAHVSLAPLRLFQGIASMLPDLDMSDGVHWYCHILYVLAKYVLWWDMP |
Enzyme Length | 396 |
Uniprot Accession Number | Q91610 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Signal involved in the early induction and patterning of anterodorsal ectoderm, nervous system and somites. Induces ectopic cement gland formation in embryos. {ECO:0000269|PubMed:7671800}. |
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 | |
Subcellular Location | SUBCELLULAR LOCATION: [Desert hedgehog protein A N-product]: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Note=The N-terminal peptide remains associated with the cell surface. {ECO:0000250}.; SUBCELLULAR LOCATION: [Desert hedgehog protein A C-product]: Secreted, extracellular space {ECO:0000250}. Note=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 | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 44,087 |
Kinetics | |
Metal Binding | METAL 89; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:O43323; METAL 90; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:O43323; METAL 90; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:O43323; METAL 95; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:O43323; METAL 125; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O43323; METAL 126; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:O43323; METAL 126; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:O43323; METAL 129; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:O43323; METAL 131; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:O43323; METAL 140; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O43323; METAL 147; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O43323; METAL 182; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O43323 |
Rhea ID | |
Cross Reference Brenda |