KEX1_CANGA
ID KEX1_CANGA Reviewed; 730 AA.
AC Q6FTM9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE Flags: Precursor;
GN Name=KEX1; OrderedLocusNames=CAGL0G01232g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380953; CAG59342.1; -; Genomic_DNA.
DR RefSeq; XP_446415.1; XM_446415.1.
DR AlphaFoldDB; Q6FTM9; -.
DR SMR; Q6FTM9; -.
DR STRING; 5478.XP_446415.1; -.
DR ESTHER; canga-q6ftm9; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAG59342; CAG59342; CAGL0G01232g.
DR GeneID; 2888423; -.
DR KEGG; cgr:CAGL0G01232g; -.
DR CGD; CAL0130288; CAGL0G01232g.
DR VEuPathDB; FungiDB:CAGL0G01232g; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; Q6FTM9; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
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; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 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..730
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411910"
FT TOPO_DOM 20..599
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 475..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..559
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 730 AA; 83259 MW; 4033FFE7B7965132 CRC64;
MLHATVLPIL LWLATLAYGF DRKEFLVDGN ELPGFTKLKN TKHWTVPKMY AGHLPATRDN
DTQYFFWKFE NKKTKKNDET PLIIWLNGGP GCSSMAGALM EIGPFRLNKK AEVIKNDGSW
HMRGSVLFLD QPVGTGFSYS KEDNEVSELD EVADNFMVFL QNYYATFPDD KDRELILAGE
SYAGQFIPYF TKAIIKFNEQ QRDENSKINI KVMFIGNGWL DPKRQYLSYV PFSLEKGIIK
KEDPAFKDIL KQHETCQNYI NSDHTGHSEL SYPPCEAVLG KIISQDKTQC INVYKFDEYD
SYPSCGLEWP VDTKFTKQFL TDKKVLAALH ANDERSWIEC RPDVKLENIK AKPAIELIPS
LLESGIELIL FNGNKDLICN TLGIDNVLKH LQWEGETGFT DEVQIFDWVY RDDLKSDKEK
VAGTVKYERQ LTLITIEDGS HMVSYDKALI SRGILDMYYD DVLLVHRDGK DTLISSKDGD
IDGYLEDDKS QDENKDNESE DESEDENDSD DESDGKEGDK QENKPDDSDD ESDEEDDDED
EDDEDDDDDD DDDDGDDEDK KGDQNSHPSH GDMNGGLDND LETGGEYYQD EDEEGSNFKA
FFLILSLVSA FIIVAAFYIS DYIKSRRHPI LVDGDGRSRL NKSVTWASDI ENGSFDIEDD
DPEFGTEGME DNMELEDVFS IDEEDEEQLE GVVPESTRKS KKGSKKKGKY FSVPNDDSAE
DIELQDIERH
