Detail Information for IndEnz0002016414
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