Detail Information for IndEnz0002015745
IED ID IndEnz0002015745
Enzyme Type ID protease015745
Protein Name Kexin
EC 3.4.21.61
Protease KEX2
Proteinase YSCF
Gene Name KEX2 QDS1 YNL238W N1122
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MKVRKYITLCFWWAFSTSALVSSQQIPLKDHTSRQYFAVESNETLSRLEEMHPNWKYEHDVRGLPNHYVFSKELLKLGKRSSLEELQGDNNDHILSVHDLFPRNDLFKRLPVPAPPMDSSLLPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVVAAIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGEIAAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYSCSWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGDNCNYDGYTNSIYSITIGAIDHKDLHPPYSEGCSAVMAVTYSSGSGEYIHSSDINGRCSNSHGGTSAAAPLAAGVYTLLLEANPNLTWRDVQYLSILSAVGLEKNADGDWRDSAMGKKYSHRYGFGKIDAHKLIEMSKTWENVNAQTWFYLPTLYVSQSTNSTEETLESVITISEKSLQDANFKRIEHVTVTVDIDTEIRGTTTVDLISPAGIISNLGVVRPRDVSSEGFKDWTFMSVAHWGENGVGDWKIKVKTTENGHRIDFHSWRLKLFGESIDSSKTETFVFGNDKEEVEPAATESTVSQYSASSTSISISATSTSSISIGVETSAIPQTTTASTDPDSDPNTPKKLSSPRQAMHYFLTIFLIGATFLVLYFMFFMKSRRRIRRSRAETYEFDIIDTDSEYDSTLDNGTSGITEPEEVEDFDFDLSDEDHLASLSSSENGDAEHTIDSVLTNENPFSDPIKQKFPNDANAESASNKLQELQPDVPPSSGRS
Enzyme Length 814
Uniprot Accession Number P13134
Absorption
Active Site ACT_SITE 175; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 213; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 385; /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 FUNCTION: Processing of precursors of alpha-factors and killer toxin.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (22); Chain (1); Compositional bias (2); Disulfide bond (2); Domain (2); Glycosylation (4); Helix (16); Metal binding (6); Propeptide (2); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (9)
Keywords 3D-structure;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen
Interact With P32790
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein.
Modified Residue
Post Translational Modification PTM: O-glycosylated.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1OT5; 1R64; 2ID4;
Mapped Pubmed ID 10393104; 10409610; 10438739; 10564262; 10567340; 10704473; 10848621; 10918038; 11092829; 11160819; 11284720; 11297433; 11728446; 11805837; 11893737; 11995965; 12221112; 12244127; 12827498; 12832612; 1367896; 1368916; 1444259; 14528262; 1483466; 1493334; 14992578; 14999401; 15090613; 15102434; 15140896; 15299026; 15364946; 1543492; 15647379; 15710404; 1574114; 15913810; 16029153; 16167351; 1618297; 16229820; 16429126; 16554755; 16913836; 17210951; 17363896; 1740121; 17426142; 17630978; 17975704; 18415848; 1843278; 1843279; 18467557; 18625069; 18784256; 18979235; 18987790; 18998772; 19536198; 19688096; 19726565; 1988035; 20150508; 2022624; 20232931; 20953094; 2099807; 21252230; 21377728; 21496492; 2165411; 2193026; 21987636; 22396539; 22533807; 22679642; 22933563; 23408788; 23498901; 25886139; 26070720; 26344761; 2647083; 26709839; 2683070; 26849222; 27693354; 27720750; 27965112; 27977123; 2902090; 3059713; 32800900; 3288097; 3297783; 6353202; 6397123; 6430565; 7819327; 7845204; 7957171; 8162413; 8194519; 8224490; 8308064; 8328974; 8420571; 8488726; 8495725; 8509444; 8887651; 8917107; 8930891; 8987562; 8991091; 9070434; 9314526; 9360297; 9417119; 9724712;
Motif
Gene Encoded By
Mass 90,003
Kinetics
Metal Binding METAL 135; /note=Calcium 1; METAL 184; /note=Calcium 1; METAL 227; /note=Calcium 1; METAL 277; /note=Calcium 2; METAL 320; /note=Calcium 2; METAL 350; /note=Calcium 2
Rhea ID
Cross Reference Brenda 3.4.21.61;