ID   KEX1_CANDC              Reviewed;         686 AA.
AC   B9WJJ7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=CD36_70870;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992694; CAX40641.1; -; Genomic_DNA.
DR   RefSeq; XP_002421307.1; XM_002421262.1.
DR   AlphaFoldDB; B9WJJ7; -.
DR   SMR; B9WJJ7; -.
DR   ESTHER; candc-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; B9WJJ7; 4 sites, No reported glycans.
DR   GeneID; 8049274; -.
DR   KEGG; cdu:CD36_70870; -.
DR   CGD; CAL0000171205; Cd36_70870.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002605; Chromosome 7.
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; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..686
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411909"
FT   TOPO_DOM        20..543
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..686
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          489..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   686 AA;  77574 MW;  D6525FC9603CA262 CRC64;
     MKFLLPTFII FIYTLLVSAL PTKEGSDPKA AKKYLVSDLP GLHDNITPDD SIPLMFAGQL
     EIYPESNTHY FFWKFSDSNQ ETITNRTIFW LNGGPGCSSM DGALLETGPF RINSQQQVIS
     NNGSWHKSGD IIYVDQPAGT GFSYSDTYIT DLDQVANYFL KFMEAYYELF PQEINNEIYF
     AGESYAGQYI PYIANAILQR NKKLHEGEQK YDLRGVLIGN GWVSPNEQSL SYLPFFKDHG
     LIDIHHPKWA TLLAKHEQCQ KIVNKIDSTF DDGTVHYYEV SSSTCEAILT DLLEYTQDTA
     NDKNQQCINM YDYTLRDSYP SCGMNWPNEL VNVGPFLRQE KVMHQLNLIN LKKWNECNGK
     VGRTFQARHS IPSVHLLPEL AKEIPVMLFN GANDIICNSQ GVLSYLQKLQ WNGETGFINK
     DNQISWVYDN KEVGYMLWER NISFINIYNS SHMVPYDLPD VSRALIDLIT GEYDEKDVDG
     KKSFVTYPLG SRKENDESKN PVESPSQTID PIISSSSSSV ESSLSSSSAS ATDSDSTSSK
     FTRLIQLAVI LVIFWGVYVL YASYKSRPSS IIKKPTNNTS NITRSSTGKK KNVQWADQLN
     QFEDDERNQE SNQGIIAKAI GKITGSKDTR GRYAPVHREN DNEYIDDIEL GEGISDPNVD
     EFIIGSDDDD EEEQPRSDPA THKSVS
//