KEX1_CRYGW
ID KEX1_CRYGW Reviewed; 687 AA.
AC E6R6G5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=CGB_E0630W;
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071;
RX PubMed=21304167; DOI=10.1128/mbio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
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; CP000290; ADV22286.1; -; Genomic_DNA.
DR RefSeq; XP_003194073.1; XM_003194025.1.
DR AlphaFoldDB; E6R6G5; -.
DR SMR; E6R6G5; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; ADV22286; ADV22286; CGB_E0630W.
DR GeneID; 10190080; -.
DR KEGG; cgi:CGB_E0630W; -.
DR VEuPathDB; FungiDB:CGB_E0630W; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_1_1; -.
DR Proteomes; UP000007805; Chromosome E.
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 PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..687
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411918"
FT TOPO_DOM ?..573
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /evidence="ECO:0000250"
FT ACT_SITE 446
FT /evidence="ECO:0000250"
FT ACT_SITE 503
FT /evidence="ECO:0000250"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 687 AA; 76275 MW; F6E945C8D8CB3B77 CRC64;
MSGNDARARV RSLPSTSSPL ETRDSDEQES SSSQSQRGSR KRGPQRRATE LPSAADLYVP
SLPGLPDMAT HPTHPLNIYA GMLPSYPGEG KVGGEGETGK DAKLYFLMAK ARRNAGKERV
IFWFNGGPGC SSFDGSLMEV GPFRTVPASE TTTGMVEAKL VEGGWEEFAT VVFVDQPPGT
GYSYAATNGY LHDFDELSAH FIEFLQNFYT VFPELKGVDT YLAGESFAGQ YIPFFADALI
NSAELPNFPL KGIAIGNGWI DPKEQYPGYV EFAYEKGLID SGTPVSAAFV DLHKERADQM
LTDQEAEEME AALKRCQEEM DKYTDPFTTP VNIDHCGEVM DSVTRPFTQE LNGKKVCMNV
YDVRLVDDFP ACGMNWPPDL PDVYTFLRQD EVISALHASS KETAWVECNN KVSYELNLKH
SHMSAALLPS ILEAGVPILM FAGAEDLICN YKGIERIVNG LEWGGEKGFA NATSQEWYLN
GTQVGTWQTS RGLSYAKIFD SSHMVGFDVP HVTNDMIMRF MDVDVSLLPG MISQWSSRIG
DDERTMIHVG DAGEAGGVPL IKGGNTDWEA WYNAVFAFLV LGILVSIVGL YFYFRRKPVS
YRSRIALKQR GRHRQSHDRD EGDTAERMPL GSERLELDDI ERAEGYEFDD RDDEGYSGKG
KGKGKELADD REEVMFALGD DDEDDRH