ID   KEX1_CANTT              Reviewed;         707 AA.
AC   C5MFP8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=CTRG_04891;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; GG692401; EER31161.1; -; Genomic_DNA.
DR   RefSeq; XP_002550593.1; XM_002550547.1.
DR   AlphaFoldDB; C5MFP8; -.
DR   SMR; C5MFP8; -.
DR   STRING; 294747.C5MFP8; -.
DR   ESTHER; cantt-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; C5MFP8; 6 sites, No reported glycans.
DR   EnsemblFungi; CTRG_04891-t43_1; CTRG_04891-t43_1-p1; CTRG_04891.
DR   GeneID; 8298894; -.
DR   KEGG; ctp:CTRG_04891; -.
DR   VEuPathDB; FungiDB:CTRG_04891; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002037; 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; IPR033124; Ser_caboxypep_his_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; PS00560; CARBOXYPEPT_SER_HIS; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..707
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411911"
FT   TOPO_DOM        18..564
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        586..707
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          496..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..694
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
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"
SQ   SEQUENCE   707 AA;  80574 MW;  1858B0F08F8E0492 CRC64;
     MLLSVFIILI NTLFVLAIPP KEGSDNNPSK KYLVTDLPGL YENVKPKISV PLMFSGQLEL
     YPENNTHYFF WKFVDSELNQ DTSKKTIFWL NGGPGCSSMD GALLETGPFR IDENEKVIYN
     NGSWHKFGDI IYVDQPAGTG FSFTNEYITD LDQVAWYFLK FMEEYYKLFP NEINNEIYFA
     GESYAGQYIP YIADAILKRN KNLKENDVKY DLKGILIGNG WVSPNQQSLS YLPFFINHGL
     IDKSHPRWGS LLSKHEKCQK IVNKIDGHFD EADVHPYEVN SATCESILTD LLNYSQDRES
     DSDHRCINMY DYTLRDSYPS CGMNWPFELK YVAPFLRKEE VMHDLNLVDL KYWRECSGKV
     GRMFGARNSL PAVHLLPNIS QEIPIILFNG ANDIICNSDG VLSYLDKLQW GGKVGFTNKD
     DQINWIYDNK EVGYILMERN ISFINIYNSS HMVPYDLPDV SRALMDLVSG KYEEKEKDGK
     REFITYPLGE VRNKLGQEIP ADESSKPIED KPDDKPIEDK PEETKPEQTK PEDETSSSTS
     EIIPTSEASF IPEPEESTSS KFTRLIQLGV IFIIFWGVYI LYVSYRARPS SIIKKPARST
     NSSGRKKNVQ WADQLNRFEE DENELGSPPP QGIIAKTISK ITGNTSNRGR YAPAGDGSRE
     FTDDIELGEG ISDPNVDEFI IGSDDDEDDD EDVETHEGNP KKTESKS
//