Detail Information for IndEnz0002002716
IED ID IndEnz0002002716
Enzyme Type ID protease002716
Protein Name Kexin
EC 3.4.21.61
KEX2 protease
Gene Name KEX2 CAWG_00530
Organism Candida albicans (strain WO-1) (Yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain WO-1) (Yeast)
Enzyme Sequence MLPIKLLIFILGYLLSPTLQQYQQIPPRDYENKNYFLVELNTTNSQKPLIDFISHYRGHYNFEHQLSSLDNHYVFSIDKSHPHNSFLGNHNSNEYNLMKRQLGHEQDYDELISHVESIHLLPMKKLSKRIPVPIEMEDVVFDNRDDTGSDNHEATDEAHQKLIEIAKKLDIHDPEFTTQWHLINLKYPGHDVNVTGLWLENILGQGIVTALVDDGVDAESDDIKQNFNSEGSWDFNNKGKSPLPRLFDDYHGTRCAGEIAAVKNDVCGIGVAWKSQVSGIRILSGPITSSDEAEAMVYGLDTNDIYSCSWGPTDNGKVLSEPDVIVKKAMIKGIQEGRDKKGAIYVFASGNGGRFGDSCNFDGYTNSIYSITVGAIDYKGLHPQYSEACSAVMVVTYSSGSGEHIHTTDIKKKCSATHGGTSAAAPLASGIYSLILSANPNLTWRDVQYISVLSATPINEEDGNYQTTALNRKYSHKYGYGKTDAYKMVHFAKTWVNVKPQAWYYSDIIEVNQTITTTPEQKAPSKRDSPQKIIHSSVNVSEKDLKIMNVERVEHITVKVNIDSTYRGRVGMRIISPTGVISDLATFRVNDASTRGFQNWTFMSVAHWGETGIGEWKVEVFVDDSKGDQVEINFKDWQFRIFGESIDGDKAEVYDITKDYAAIRRELLEKEKQNSKSTTTTSSTTTATTTSGGEGDQKTTTSAENKESTTKVDNSASITTSQTASLTSSNEQHQPTESNSDSDSDTDDENKQEGEEDNDNDNDNGNKKANSDNTGFYLMSIAVVGFIAVLLVMKFHKTPGSGRRRRRRDGYEFDIIPGEDYSDSDDDEDDFDTRRADDDSFDLGHRNDQRVVSASQQQRQYDRQQDETRDRLFDDFNAESLPDYENDMFKIGDEEEEEEEGQQSAKAPSNSEGNSGTSTKKYKDNEADEDHKDVVGTQ
Enzyme Length 938
Uniprot Accession Number O13359
Absorption
Active Site ACT_SITE 213; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 251; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 422; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.; EC=3.4.21.61;
DNA Binding
EC Number 3.4.21.61
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (6); Disulfide bond (2); Domain (2); Frameshift (1); Glycosylation (6); Propeptide (1); Region (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Calcium;Disulfide bond;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Protease;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: O-glycosylated. {ECO:0000250}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 105,144
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda