KEX1_PICGU
ID KEX1_PICGU Reviewed; 656 AA.
AC A5DAT0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 60.
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=PGUG_00385;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408155; EDK36287.2; -; Genomic_DNA.
DR RefSeq; XP_001487008.1; XM_001486958.1.
DR AlphaFoldDB; A5DAT0; -.
DR SMR; A5DAT0; -.
DR STRING; 4929.XP_001487008.1; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EDK36287; EDK36287; PGUG_00385.
DR GeneID; 5129177; -.
DR KEGG; pgu:PGUG_00385; -.
DR VEuPathDB; FungiDB:PGUG_00385; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; A5DAT0; -.
DR OMA; NGWIDPD; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001997; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..656
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411938"
FT TOPO_DOM 18..536
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 626..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 656 AA; 73287 MW; 0A0643FE4686AA27 CRC64;
MFFHAILVLI QVALALGASP RAGSSERSKY FVTSLPGMYS NLPKEEIPIM FSGQLELFPE
NNTHYYFWKF VNPNPIAEAE RRTIFWLNGG PGCSSMDGAL MEAGPFRVND DKEIVYNNGS
WHKAGDIVFV DQPAGTGFSY SDEYEHELPD VSVHFLKFLE KYFEVFPEDR QNQIFFAGES
YAGQYIPYIA DGILKRNKNL KAGESPYDLR GLLIGNGWIA PNEQSLSYVQ YALQAGFVSP
SMPGWSRLLA SQERCQNVVN SVNTQDDSVS DYKVVSDVCD QVLNTLLEVA RDRDAPADQQ
CVNMYDYTLR DEFPSCGMNW PPDLVNVKPF LNIPGVQSQL NLVHKKPWLE CSGRVGRNFV
AQRSKPAVHL LPSLLEDVPI LLFNGNRDII CNYIGTEAFI KELEWNGQKG WDDDNVFDWN
FDGNLAGYVR NSRNLTFVNV FNSSHMVPFD LPDTSRSLMD LVTGNFDIKD DKILTYKLGT
RGQAKQSDKK PASTSSIPSE ISATALASGS SSASAQASAT ANEADGDNNT SHKIERAIQL
LVIIVLLWGI YALYSSYKSR PSSIIKSGPT GKKKNVQWAD QLRRFQEDDQ VRVQPHGIFA
KALNKFKGNS DGAYAPVQGR YEDIEMSSAS PIDDFVVVSD DEEEEPSRNE PSSNQK
