KEX1_CANAW
ID KEX1_CANAW Reviewed; 702 AA.
AC C4YTG0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=CAWG_05452;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
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; CM000313; EEQ46901.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YTG0; -.
DR SMR; C4YTG0; -.
DR STRING; 5476.C4YTG0; -.
DR ESTHER; canal-q5afp8; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EEQ46901; EEQ46901; CAWG_05452.
DR VEuPathDB; FungiDB:CAWG_05452; -.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OMA; EMADQFV; -.
DR Proteomes; UP000001429; Chromosome 7.
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; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..702
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411908"
FT TOPO_DOM 20..555
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 491..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 702 AA; 78757 MW; 7A26B834D7E7ABB8 CRC64;
MKLILSTLIV FIHTLLVSAL PTKEGSDPNS AKKYLVSDLP GLHENITPDN SIPLMFAGQL
EIYPETDTHY FFWKFSDSNP ETVTNRTIFW LNGGPGCSSM DGALLETGPF RINSQQQVIS
NNGSWHRMGD IIYVDQPAGT GFSYSDTYIT DLDQVAEYFL KFMEKYYELF PEEIGYEIYF
AGESYAGQYI PYIADAILQR NKKLVDGEHK YDLRGVLIGN GWVSPNEQSL SYLPFFKDHG
LIDVHHPKWA TLLAKHEQCQ KIVNKIDSTF DDGVVHYYEV SSSTCEAILT DLLEYTQDTA
SEKDQRCVNM YDYTLRDSYP SCGMNWPYEL VNVGPFLRQE KVMHQLNLIN LKKWNECNGR
VGRTFQARHS IPAVHLLPEL AKEIPVMLFN GANDIICNSQ GVLSYLQKLQ WNGETGFTNK
DNQISWIYDN KEVGYIIWER NISFINIYNS SHMVPYDLPD VSRALIDLIT GKYDEKDVDG
KKSFVTYPLG SRKESDASAN GEENAGSDKV PGDSPSQTMD PMISSSTASS SSVESSLSSS
TASADSDSTS SKFTRLIQLA VILVIFWGVY VLYASYKSRP SSIIKKPTNN TSNVTRSSAG
KKKNVQWADQ LNQFEDDERT QEPNQGIIAK AIGKITGSKD TRGRYAPVQR GNGNEYIDDI
ELGEGLSDPN VDEFIIGSDD DEEQGQAHSG AATHNQKQKP MN
