ID KEX1_YEAS2 Reviewed; 737 AA. AC C7GWZ2; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 13-OCT-2009, sequence version 1. DT 02-SEP-2026, entry version 49. DE RecName: Full=Pheromone-processing carboxypeptidase KEX1; DE EC=3.4.16.6; DE AltName: Full=Carboxypeptidase D; DE AltName: Full=Killer expression defective protein 1; DE Flags: Precursor; GN Name=KEX1; ORFNames=C1Q_05019; OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=574961; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAY291; RX PubMed=19812109; DOI=10.1101/gr.091777.109; RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C., RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F., RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H., RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D., RA Pereira G.A.G.; RT "Genome structure of a Saccharomyces cerevisiae strain widely used in RT bioethanol production."; RL Genome Res. 19:2258-2270(2009). CC -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in CC the C-terminal processing of the lysine and arginine residues from the CC precursors of K1, K2 and K28 killer toxins and a-factor (mating CC pheromone). Involved in the programmed cell death caused by defective CC N-glycosylation and also contributes to the active cell death program CC induced by acetic acid stress or during chronological aging. Promotes CC cell fusion by proteolytically processing substrates that act in CC parallel to PRM1 as an alternative fusion machine, as cell wall CC components, or both (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential release of a C-terminal arginine or lysine CC residue.; EC=3.4.16.6; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACFL01000397; EEU04662.1; -; Genomic_DNA. DR AlphaFoldDB; C7GWZ2; -. DR SMR; C7GWZ2; -. DR ESTHER; yeast-kex01; Carboxypeptidase_S10. DR MEROPS; S10.007; -. DR GlyCosmos; C7GWZ2; 3 sites, No reported glycans. DR GO; GO:0005802; C:trans-Golgi network; IEA:TreeGrafter. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR FunFam; 3.40.50.1820:FF:000289; Pheromone-processing carboxypeptidase KEX1; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR033124; Ser_caboxypep_his_AS. DR InterPro; IPR018202; Ser_caboxypep_ser_AS. DR PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. PE 3: Inferred from homology; KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase; KW Membrane; Phosphoprotein; Protease; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..737 FT /note="Pheromone-processing carboxypeptidase KEX1" FT /id="PRO_0000411954" FT TOPO_DOM 23..624 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 625..645 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 646..737 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 502..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 682..737 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 525..534 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 535..547 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..587 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 682..695 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 710..720 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 727..737 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 198 FT /evidence="ECO:0000250" FT ACT_SITE 405 FT /evidence="ECO:0000250" FT ACT_SITE 470 FT /evidence="ECO:0000250" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09620" FT CARBOHYD 81 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 459 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 467 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 737 AA; 83179 MW; 9379A1E2CBC66548 CRC64; MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS EDADEQDNSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDVSF VSKFFSTPGV IDSLHLDSDK IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS RGIVDIYSND VMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDDDDDD DDDEDDNNEK QSNQGLEDSR HKSSEYEQEE EEVEEFAEEI SMYKHKAVVV TIVTFLIVVL GVYAYDRRVR RKARHTILVD PNNRQHDSPN KTVSWADDLE SGLGAEDDLE QDEQLEGGAP ISSTSNKAGS KLKTKKKKKY TSLPNTEIDE SFEMTDF //