ID KEX1_ARTOC Reviewed; 636 AA. AC C5FTV7; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 24-JAN-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=MCYG_06129; OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum. OX NCBI_TaxID=554155; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4605 / CBS 113480; RX PubMed=22951933; DOI=10.1128/mbio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C., RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.; RT "Comparative genome analysis of Trichophyton rubrum and related RT dermatophytes reveals candidate genes involved in infection."; RL MBio 3:E259-E259(2012). 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; DS995705; EEQ33310.1; -; Genomic_DNA. DR RefSeq; XP_002846260.1; XM_002846214.1. DR AlphaFoldDB; C5FTV7; -. DR SMR; C5FTV7; -. DR STRING; 554155.C5FTV7; -. DR ESTHER; artoc-kex1; Carboxypeptidase_S10. DR MEROPS; S10.007; -. DR GlyCosmos; C5FTV7; 4 sites, No reported glycans. DR GeneID; 9228429; -. DR VEuPathDB; FungiDB:MCYG_06129; -. DR eggNOG; KOG1282; Eukaryota. DR HOGENOM; CLU_008523_11_0_1; -. DR OMA; EMADQFV; -. DR OrthoDB; 1647009at2759; -. DR Proteomes; UP000002035; Unassembled WGS sequence. 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; 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..38 FT /evidence="ECO:0000255" FT CHAIN 39..636 FT /note="Pheromone-processing carboxypeptidase KEX1" FT /id="PRO_0000411900" FT TOPO_DOM 39..522 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 523..543 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 544..636 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 575..636 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 575..590 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 190 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 389 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 451 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT CARBOHYD 213 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 440 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 448 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 500 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 636 AA; 71407 MW; 547BA0A159BB67C2 CRC64; MSATHKMRYN LQLVLPSNTR ARWAWLLLLL SNPAAVLAKC ASDYFVHSLP GQPEGSVLKM HAGHIEIDSE HKGNLFFWHY QNRHIANRQR TVIWLNGGPG CSSMDGALME VGPYRLKDDH SLVYNEGSWD EFANLLFVDQ PVGTGFSYVS TDSYVHELGP MADQFIIFLD RWFKLFPEYE NDDIYLAGES YAGQYIPYIA KAIVKRNEKL PANQTAWNVE GLIIGNGWIA PNEQYRSYLT YAYKEGILKE SSEGAQAAEA QLSQCSSKLS EVGKFGIHID ECERVMELIL DTTKINGKCL NMYDIRLDDT SDSCGMNWPP DISSVTTYLR RPDVVKALNI NEDKTTGWRE CSPGVGRNLR ATESVPSIQL LPGLLEGGIP VLLFSGDKDL ICNHVGTEDL IQNMKWSRGT GFELSPGVRA PRHDWVFEGL PAGVYQQARN LTYVKFYNAS HMVPFDFPRR SRDMLDRFLG VDITTIGGDP ADSRIDGLKG TITSVGAHPN STTAEEREKE KMKIAAWQAY YKSGEIALIV VAIAATIWGF FVWRSKRREQ GGEYQGIYPN LESLSSSSLS TFRSKRRGRH DIESTSRSDE AELESLYNGP EISEVLETQD GRQRELSADG SNEKASASLM VERNLR //