ID   KEX1_CANGA              Reviewed;         730 AA.
AC   Q6FTM9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=KEX1; OrderedLocusNames=CAGL0G01232g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380953; CAG59342.1; -; Genomic_DNA.
DR   RefSeq; XP_446415.1; XM_446415.1.
DR   AlphaFoldDB; Q6FTM9; -.
DR   SMR; Q6FTM9; -.
DR   STRING; 284593.Q6FTM9; -.
DR   ESTHER; canga-q6ftm9; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; Q6FTM9; 3 sites, No reported glycans.
DR   EnsemblFungi; CAGL0G01232g-T; CAGL0G01232g-T-p1; CAGL0G01232g.
DR   GeneID; 2888423; -.
DR   KEGG; cgr:CAGL0G01232g; -.
DR   CGD; CAL0130288; CAGL0G01232g.
DR   VEuPathDB; FungiDB:CAGL0G01232g; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   InParanoid; Q6FTM9; -.
DR   Proteomes; UP000002428; Chromosome G.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..730
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411910"
FT   TOPO_DOM        20..599
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        600..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        621..730
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          475..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..513
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..559
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        376
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   730 AA;  83259 MW;  4033FFE7B7965132 CRC64;
     MLHATVLPIL LWLATLAYGF DRKEFLVDGN ELPGFTKLKN TKHWTVPKMY AGHLPATRDN
     DTQYFFWKFE NKKTKKNDET PLIIWLNGGP GCSSMAGALM EIGPFRLNKK AEVIKNDGSW
     HMRGSVLFLD QPVGTGFSYS KEDNEVSELD EVADNFMVFL QNYYATFPDD KDRELILAGE
     SYAGQFIPYF TKAIIKFNEQ QRDENSKINI KVMFIGNGWL DPKRQYLSYV PFSLEKGIIK
     KEDPAFKDIL KQHETCQNYI NSDHTGHSEL SYPPCEAVLG KIISQDKTQC INVYKFDEYD
     SYPSCGLEWP VDTKFTKQFL TDKKVLAALH ANDERSWIEC RPDVKLENIK AKPAIELIPS
     LLESGIELIL FNGNKDLICN TLGIDNVLKH LQWEGETGFT DEVQIFDWVY RDDLKSDKEK
     VAGTVKYERQ LTLITIEDGS HMVSYDKALI SRGILDMYYD DVLLVHRDGK DTLISSKDGD
     IDGYLEDDKS QDENKDNESE DESEDENDSD DESDGKEGDK QENKPDDSDD ESDEEDDDED
     EDDEDDDDDD DDDDGDDEDK KGDQNSHPSH GDMNGGLDND LETGGEYYQD EDEEGSNFKA
     FFLILSLVSA FIIVAAFYIS DYIKSRRHPI LVDGDGRSRL NKSVTWASDI ENGSFDIEDD
     DPEFGTEGME DNMELEDVFS IDEEDEEQLE GVVPESTRKS KKGSKKKGKY FSVPNDDSAE
     DIELQDIERH
//