Detail Information for IndEnz0002004589
IED ID IndEnz0002004589
Enzyme Type ID protease004589
Protein Name Clotting factor G alpha subunit
EC 3.2.1.-
Gene Name
Organism Tachypleus tridentatus (Japanese horseshoe crab)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Merostomata (horseshoe crabs) Xiphosura Limulidae Tachypleus Tachypleus tridentatus (Japanese horseshoe crab)
Enzyme Sequence MLVLLCCVVLHVGVARICCSHEPKWQLVWSDEFTNGISSDWEFEMGNGLNGWGNNELQYYRRENAQVEGGKLVITAKREDYDGFKYTSARLKTQFDKSWKYGKIEAKMAIPSFRGVWVMFWMSGDNTNYVRWPSSGEIDFIEHRNTNNEKVRGTIHWSTPDGAHAHHNRESNTNGIDYHIYSVEWNSSIVKWFVNGNQYFEVKIQGGVNGKSAFRNKVFVILNMAIGGNWPGFDVADEAFPAKMYIDYVRVYQDASTSSPVGDTSLDGYYFVQNRHSELYLDVTDASNEDGAFLQQWSYSGNENQQFDFEHLENNVYKITNKKSGKSLDVYNFGTENGVRIQQWSYGGARNQQFTVQSVGDGYYKIIPRGSGKLVEVADFSKDAGGKIQQWSDNNQLSGQWKLIKSKSYSKLIQAESYFDSSKVQLEDTSDVGGGKNVKCDNEGAWMAYKDIDFPSSGNYRIEYRVASERAGGKLSLDLNAGSIVLGMLDVPSTGGWQKWTTISHTVNVDSGTYNLGIYVQRASWNINWIKITKIPEQSNLNQGRRNSKLIQAESYFSYSEVQLEDTLDVGGGKNVKCDKEGAWMAYKDIDFPSSGSYRVEYRVASERAGGKLSLDLNAGSIVLGMLDIPSTGGLQKWTTISHIVNVDLGTYNLGIYVQKASWNINWIRITKV
Enzyme Length 673
Uniprot Accession Number Q27082
Absorption
Active Site ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01098; ACT_SITE 142; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01098
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.2.1.-
Enzyme Function FUNCTION: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme (PubMed:7822328). {ECO:0000269|PubMed:7822328, ECO:0000305|PubMed:7822328}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Domain (4); Glycosylation (1); Signal peptide (1); Site (1)
Keywords Direct protein sequencing;Glycoprotein;Glycosidase;Hemolymph clotting;Hydrolase;Lectin;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: In presence of (1->3)-beta-glucan, proteolytically cleaved into a 55kDa and a 17kDa forms. {ECO:0000269|PubMed:7822328}.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000269|PubMed:8288603
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 75,952
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda