ID KEX1_PENRW Reviewed; 607 AA. AC B6H7A4; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 24-JAN-2024, entry version 64. 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=Pc16g01980; OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin OS 54-1255) (Penicillium chrysogenum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium; OC Penicillium chrysogenum species complex. OX NCBI_TaxID=500485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255; RX PubMed=18820685; DOI=10.1038/nbt.1498; RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M., RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F., RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J., RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R., RA Bovenberg R.A.L.; RT "Genome sequencing and analysis of the filamentous fungus Penicillium RT chrysogenum."; RL Nat. Biotechnol. 26:1161-1168(2008). 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; AM920431; CAP92868.1; -; Genomic_DNA. DR RefSeq; XP_002560571.1; XM_002560525.1. DR AlphaFoldDB; B6H7A4; -. DR SMR; B6H7A4; -. DR STRING; 500485.B6H7A4; -. DR ESTHER; penrw-kex1; Carboxypeptidase_S10. DR MEROPS; S10.007; -. DR GlyCosmos; B6H7A4; 3 sites, No reported glycans. DR GeneID; 8313930; -. DR KEGG; pcs:Pc16g01980; -. DR VEuPathDB; FungiDB:PCH_Pc16g01980; -. DR eggNOG; KOG1282; Eukaryota. DR HOGENOM; CLU_008523_11_0_1; -. DR OMA; EMADQFV; -. DR OrthoDB; 1647009at2759; -. DR BioCyc; PCHR:PC16G01980-MONOMER; -. DR Proteomes; UP000000724; Contig Pc00c16. 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:0017000; P:antibiotic biosynthetic process; IEA:UniProt. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt. 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; 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; PS00131; CARBOXYPEPT_SER_SER; 1. PE 3: Inferred from homology; KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase; KW Membrane; Protease; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..607 FT /note="Pheromone-processing carboxypeptidase kex1" FT /id="PRO_5000409185" FT TOPO_DOM 20..502 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 503..523 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 524..607 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 458..487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..607 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 534..552 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 553..598 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 168 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 369 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 431 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT CARBOHYD 420 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 428 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 480 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 607 AA; 67721 MW; CDE50C5072988A69 CRC64; MLLSALSLLL SPLVSASSAA DYYVRSLPGA PEGPFLKMHA GHIEVDPDTN GNLFFWHFQN RHIANRQRTV IWLNGGPGCS SMDGAFMEVG PYRLQDDHTL KYNEGRWDEF ANLLFVDNPV GTGFSYANTN SYLHELDEMA AHFVIFLEKF FELFPEYAND DLYIAGESYA GQHIPYIAKA IQDRNKGITE NGGTKWPLKG LLIGNGWISP ADQYPSYFKF IEREGLAKPG TSLHHNINAL NEVCLSKLET PGAKNKLDVG ACELVLQQFL DLTTEDHQCY NMYDVRLKDE AKSCGMNWPP DLKNIEPYLQ RPDVVKALNI NPAKKSGWTE CAGMVHMAFT AKNSIPSVHL LPGLIESGIN VLLFSGDKDL ICNHIGTETL IHNMDWKGGT GFETSPGVWA PRHDWSFEGE PAGIYQSARN LTYVLFYNSS HMVPFDNPRQ SRDMLDRFMK VDIASIGGQP SDSRIDGEKL PQTAVGGQAN STAAEQNEKE RLKQTEMHAY TKSGEAVLII VIIGVIAWGF FIWRSRRTRR GYKGVSNNDM SDSTSVLSRF QNKHSGRDVE AGDFDEAELD QLHSPSIERE DYAVGEASDD DDHIISHPET GGNRQSS //