ID KEX1_CANAW Reviewed; 702 AA. AC C4YTG0; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=Pheromone-processing carboxypeptidase KEX1; DE EC=3.4.16.6; DE AltName: Full=Carboxypeptidase D; DE Flags: Precursor; GN Name=KEX1; ORFNames=CAWG_05452; OS Candida albicans (strain WO-1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=294748; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WO-1; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B., RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., RA Birren B.W., Kellis M., Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in CC the C-terminal processing of the lysine and arginine residues from CC protein precursors. Promotes cell fusion and is involved in the CC programmed cell death (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; CM000313; EEQ46901.1; -; Genomic_DNA. DR AlphaFoldDB; C4YTG0; -. DR SMR; C4YTG0; -. DR ESTHER; canal-q5afp8; Carboxypeptidase_S10. DR MEROPS; S10.007; -. DR GlyCosmos; C4YTG0; 4 sites, No reported glycans. DR PaxDb; 5476-C4YTG0; -. DR VEuPathDB; FungiDB:CAWG_05452; -. DR HOGENOM; CLU_008523_11_2_1; -. DR OMA; PLMFAGQ; -. DR Proteomes; UP000001429; Chromosome 7. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR033124; Ser_caboxypep_his_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. PE 3: Inferred from homology; KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase; KW Membrane; Protease; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..702 FT /note="Pheromone-processing carboxypeptidase KEX1" FT /id="PRO_0000411908" FT TOPO_DOM 20..555 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 556..576 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 577..702 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 491..531 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 582..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 659..702 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..531 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..702 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 184 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075" FT ACT_SITE 394 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075" FT ACT_SITE 452 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075" FT CARBOHYD 85 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 449 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 702 AA; 78757 MW; 7A26B834D7E7ABB8 CRC64; MKLILSTLIV FIHTLLVSAL PTKEGSDPNS AKKYLVSDLP GLHENITPDN SIPLMFAGQL EIYPETDTHY FFWKFSDSNP ETVTNRTIFW LNGGPGCSSM DGALLETGPF RINSQQQVIS NNGSWHRMGD IIYVDQPAGT GFSYSDTYIT DLDQVAEYFL KFMEKYYELF PEEIGYEIYF AGESYAGQYI PYIADAILQR NKKLVDGEHK YDLRGVLIGN GWVSPNEQSL SYLPFFKDHG LIDVHHPKWA TLLAKHEQCQ KIVNKIDSTF DDGVVHYYEV SSSTCEAILT DLLEYTQDTA SEKDQRCVNM YDYTLRDSYP SCGMNWPYEL VNVGPFLRQE KVMHQLNLIN LKKWNECNGR VGRTFQARHS IPAVHLLPEL AKEIPVMLFN GANDIICNSQ GVLSYLQKLQ WNGETGFTNK DNQISWIYDN KEVGYIIWER NISFINIYNS SHMVPYDLPD VSRALIDLIT GKYDEKDVDG KKSFVTYPLG SRKESDASAN GEENAGSDKV PGDSPSQTMD PMISSSTASS SSVESSLSSS TASADSDSTS SKFTRLIQLA VILVIFWGVY VLYASYKSRP SSIIKKPTNN TSNVTRSSAG KKKNVQWADQ LNQFEDDERT QEPNQGIIAK AIGKITGSKD TRGRYAPVQR GNGNEYIDDI ELGEGLSDPN VDEFIIGSDD DEEQGQAHSG AATHNQKQKP MN //