ID   KEX1_TUBMM              Reviewed;         625 AA.
AC   D5G4B1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
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=GSTUM_00004029001;
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28;
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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; FN429986; CAZ79354.1; -; Genomic_DNA.
DR   RefSeq; XP_002835233.1; XM_002835187.1.
DR   AlphaFoldDB; D5G4B1; -.
DR   SMR; D5G4B1; -.
DR   STRING; 656061.D5G4B1; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; CAZ79354; CAZ79354; GSTUM_00004029001.
DR   GeneID; 9184979; -.
DR   KEGG; tml:GSTUM_00004029001; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; D5G4B1; -.
DR   OMA; EMADQFV; -.
DR   Proteomes; UP000006911; 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; IPR033124; Ser_caboxypep_his_AS.
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; 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; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..625
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411948"
FT   TOPO_DOM        25..516
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        517..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        538..625
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          601..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   625 AA;  69432 MW;  B5055DB7C13107F9 CRC64;
     MRLAASSLLL GAAASLLSSA TALAVRSDNP GSSAGYFVRS LPGQPPGPLI KMHAGHIEVD
     HATNGNLFFW HFQNKHIANR QRTVIWLNGG PGCSSMDGAL MEVGPYRLKD DHTLAENEGS
     WHEFANLLFV DQPVGTGFSY VNTDSYLTEL TQMSDHFIKF LTKFFELFPE YESDDIYLSG
     ESYAGQHIPY IADAILKRNA DASIKWNVKG LLIGNGWIDP SNQYLSYLPF AYESGIVEKG
     SPIADQIEKQ VAVCVKTIAE KGRHHVDLNQ CEQILQDILA KTKHHKDGKE VCWNMYDVRL
     EDTYPSCGMN WPPDLSSLTP YLRRKDVLQA LHVNPDKTAG WTECAGAVSS SFRALKSKPS
     VELLPDLLKE MPILLFSGNK DLICNHIGTE ELIHNMEWNG GKGFELDGAP GTWAPREDWV
     FEDEPAGIYQ SARNLTYVLI YNSSHMVPFD FSRRTRDMLD RFMEVDIGKI GGTPADSVIG
     GEKAPITSVG GTPNSTAAVE KEKERVDQAR WAAYYRSGEV ALVLVASAAA IWGIFIWRQR
     HRRRGRRGSY AGLGGLKMTG GSRDRLADGR ESFDEDELRD LTVASPMFER DRDLEAAEAR
     RYSLGGVSDD ESDDEGRIEK RPSVG