KEX1_LODEL
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 03-AUG-2022, entry version 71.
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 / NRRL
RC 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 PRIDE; A5E751; -.
DR EnsemblFungi; EDK47259; EDK47259; LELG_05440.
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; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001996; 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 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.
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
