ID   KEX1_LODEL              Reviewed;         702 AA.
AC   A5E751;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=LELG_05440;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239;
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; CH981533; EDK47259.1; -; Genomic_DNA.
DR   RefSeq; XP_001523214.1; XM_001523164.1.
DR   AlphaFoldDB; A5E751; -.
DR   SMR; A5E751; -.
DR   STRING; 379508.A5E751; -.
DR   ESTHER; lodel-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; A5E751; 4 sites, No reported glycans.
DR   GeneID; 5230460; -.
DR   KEGG; lel:LELG_05440; -.
DR   VEuPathDB; FungiDB:LELG_05440; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   InParanoid; A5E751; -.
DR   OMA; PLMFAGQ; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000001996; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..702
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411924"
FT   TOPO_DOM        20..554
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        576..702
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          501..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   702 AA;  79550 MW;  C72913D44E37B44D CRC64;
     MLISSIYTIC LFIITSVLAI PPKEGSDSDP AKQYLVTDLP GLHENIDDDF KPIMYAGQVE
     LFPENNTMYF FWKFTDPKKS TDSAYSKRSI FWLNGGPGCS SMDGALLETG PFRINQDEKV
     VMNNGSWHKA GDVVYVDQPA GTGFSYTDQG KWLHDLPDMA FYFLKFMEKY YEIYPEEIDN
     DIYFAGESYA GQYIPYIADA ILKRNAKLEE GQKKYNLKSL LIGNGWVSPN EQSLSYLPFF
     IENKLIDKEN PRWMELLGDH EKCQRIVDGI DSKFDDKELN PAELDSNLCE GILTKLLSAT
     VNGDGADDDQ RCINMYDFTL RDSWPGCGIN WPFELKYVTP FLRNDEVKHD LNLRVMKTWR
     ECSGRVGRNF NAQHSFPSVH LLPDLLKQVP IILFSGMNDI ICNSKGTLQY VLKLNWNGRK
     GFENPDAKLD WIHDDKKVGY VIQERNLTFI DIYNSSHMVP YDLPEVSRAL LEIATNNYDI
     RDVDETNQNL VTYPLGVQKK GKIEVNPPST PSSNDDSTTS ETSDSQPDTV SSAGTSAEAE
     TETEAEPTVN KVARLIQLAV ILIVIWGLYL LYASWRARPS PIMKKNGGNG RKKNVQWADQ
     LSRFEEEADA SQLKGFFAKT MDRFRTTEGQ GSYARAQSDD YIDDIELGEG IGETQLDDFI
     IGSDDEREGE LEQPTHKSGN MDTDTNKNMK NSSNESKNKN TV
//