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   03-AUG-2022, entry version 56.
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}.
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DR   EMBL; DS995705; EEQ33310.1; -; Genomic_DNA.
DR   RefSeq; XP_002846260.1; XM_002846214.1.
DR   AlphaFoldDB; C5FTV7; -.
DR   SMR; C5FTV7; -.
DR   STRING; 63405.XP_002846260.1; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EEQ33310; EEQ33310; MCYG_06129.
DR   GeneID; 9228429; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 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