| IED ID | IndEnz0002015746 |
| Enzyme Type ID | protease015746 |
| Protein Name |
Pheromone-processing carboxypeptidase KEX1 EC 3.4.16.6 Carboxypeptidase D Killer expression defective protein 1 |
| Gene Name | KEX1 YGL203C |
| 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 | MFYNRWLGTWLAMSALIRISVSLPSSEEYKVAYELLPGLSEVPDPSNIPQMHAGHIPLRSEDADEQDSSDLEYFFWKFTNNDSNGNVDRPLIIWLNGGPGCSSMDGALVESGPFRVNSDGKLYLNEGSWISKGDLLFIDQPTGTGFSVEQNKDEGKIDKNKFDEDLEDVTKHFMDFLENYFKIFPEDLTRKIILSGESYAGQYIPFFANAILNHNKFSKIDGDTYDLKALLIGNGWIDPNTQSLSYLPFAMEKKLIDESNPNFKHLTNAHENCQNLINSASTDEAAHFSYQECENILNLLLSYTRESSQKGTADCLNMYNFNLKDSYPSCGMNWPKDISFVSKFFSTPGVIDSLHLDSDKIDHWKECTNSVGTKLSNPISKPSIHLLPGLLESGIEIVLFNGDKDLICNNKGVLDTIDNLKWGGIKGFSDDAVSFDWIHKSKSTDDSEEFSGYVKYDRNLTFVSVYNASHMVPFDKSLVSRGIVDIYSNDVMIIDNNGKNVMITTDDDSDQDATTESGDKPKENLEEEEQEAQNEEGKEKEGNKDKDGDDDNDNDDDDEDDHNSEGDDDDDDDDDEDDNNEKQSNQGLEDSRHKSSEYEQEEEEVEEFAEEISMYKHKAVVVTIVTFLIVVLGVYAYDRRVRRKARHTILVDPNNRQHDSPNKTVSWADDLESGLGAEDDLEQDEQLEGGAPISSTSNKAGSKLKTKKKKKYTSLPNTEIDESFEMTDF |
| Enzyme Length | 729 |
| Uniprot Accession Number | P09620 |
| Absorption | |
| Active Site | ACT_SITE 198; ACT_SITE 405; /evidence=ECO:0000250; ACT_SITE 470; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; |
| DNA Binding | |
| EC Number | 3.4.16.6 |
| Enzyme Function | FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both. {ECO:0000269|PubMed:10972812, ECO:0000269|PubMed:11988505, ECO:0000269|PubMed:1469044, ECO:0000269|PubMed:17210951, ECO:0000269|PubMed:18474590, ECO:0000269|PubMed:3301004, ECO:0000269|PubMed:3301840, ECO:0000269|PubMed:3305079, ECO:0000269|PubMed:4364866, ECO:0000269|PubMed:773743, ECO:0000269|PubMed:8416959}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (19); Chain (1); Compositional bias (2); Glycosylation (3); Helix (24); Modified residue (1); Mutagenesis (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) |
| Keywords | 3D-structure;Apoptosis;Carboxypeptidase;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Phosphoprotein;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}; Single-pass type I membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}. |
| Modified Residue | MOD_RES 660; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17287358 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1AC5; |
| Mapped Pubmed ID | 10341419; 1444259; 16429126; 16554755; 1843279; 18467557; 19536198; 2022624; 20931186; 21496492; 21765803; 2193026; 21936842; 22188402; 22396539; 22533807; 22876361; 23498901; 23656787; 26272996; 27048816; 27305947; 3288097; 6353202; 6397123; 8307029; 8308064; 8982451; 9185853; |
| Motif | |
| Gene Encoded By | |
| Mass | 82,245 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=284 uM for benzoyl-Phe-Ala-Arg {ECO:0000269|PubMed:8416959}; KM=516 uM for furylacryloyl-Ala-Arg {ECO:0000269|PubMed:8416959}; KM=962 uM for furylacryloyl-Ala-Lys {ECO:0000269|PubMed:8416959}; Vmax=64.25 umol/min/mg enzyme toward benzoyl-Phe-Ala-Arg {ECO:0000269|PubMed:8416959}; Vmax=22.35 umol/min/mg enzyme toward furylacryloyl-Ala-Arg {ECO:0000269|PubMed:8416959}; Vmax=11.55 umol/min/mg enzyme toward furylacryloyl-Ala-Lys {ECO:0000269|PubMed:8416959}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.16.6; |