KEX1_CANTT
ID KEX1_CANTT Reviewed; 707 AA.
AC C5MFP8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, 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; ORFNames=CTRG_04891;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
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; GG692401; EER31161.1; -; Genomic_DNA.
DR RefSeq; XP_002550593.1; XM_002550547.1.
DR AlphaFoldDB; C5MFP8; -.
DR SMR; C5MFP8; -.
DR STRING; 5482.XP_002550593.1; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EER31161; EER31161; CTRG_04891.
DR GeneID; 8298894; -.
DR KEGG; ctp:CTRG_04891; -.
DR VEuPathDB; FungiDB:CTRG_04891; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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; 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..707
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411911"
FT TOPO_DOM 18..564
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 496..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 707 AA; 80574 MW; 1858B0F08F8E0492 CRC64;
MLLSVFIILI NTLFVLAIPP KEGSDNNPSK KYLVTDLPGL YENVKPKISV PLMFSGQLEL
YPENNTHYFF WKFVDSELNQ DTSKKTIFWL NGGPGCSSMD GALLETGPFR IDENEKVIYN
NGSWHKFGDI IYVDQPAGTG FSFTNEYITD LDQVAWYFLK FMEEYYKLFP NEINNEIYFA
GESYAGQYIP YIADAILKRN KNLKENDVKY DLKGILIGNG WVSPNQQSLS YLPFFINHGL
IDKSHPRWGS LLSKHEKCQK IVNKIDGHFD EADVHPYEVN SATCESILTD LLNYSQDRES
DSDHRCINMY DYTLRDSYPS CGMNWPFELK YVAPFLRKEE VMHDLNLVDL KYWRECSGKV
GRMFGARNSL PAVHLLPNIS QEIPIILFNG ANDIICNSDG VLSYLDKLQW GGKVGFTNKD
DQINWIYDNK EVGYILMERN ISFINIYNSS HMVPYDLPDV SRALMDLVSG KYEEKEKDGK
REFITYPLGE VRNKLGQEIP ADESSKPIED KPDDKPIEDK PEETKPEQTK PEDETSSSTS
EIIPTSEASF IPEPEESTSS KFTRLIQLGV IFIIFWGVYI LYVSYRARPS SIIKKPARST
NSSGRKKNVQ WADQLNRFEE DENELGSPPP QGIIAKTISK ITGNTSNRGR YAPAGDGSRE
FTDDIELGEG ISDPNVDEFI IGSDDDEDDD EDVETHEGNP KKTESKS
