KEX1_CANDC
ID KEX1_CANDC Reviewed; 686 AA.
AC B9WJJ7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=CD36_70870;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992694; CAX40641.1; -; Genomic_DNA.
DR RefSeq; XP_002421307.1; XM_002421262.1.
DR AlphaFoldDB; B9WJJ7; -.
DR SMR; B9WJJ7; -.
DR STRING; 42374.XP_002421307.1; -.
DR MEROPS; S10.007; -.
DR PRIDE; B9WJJ7; -.
DR EnsemblFungi; CAX40641; CAX40641; CD36_70870.
DR GeneID; 8049274; -.
DR KEGG; cdu:CD36_70870; -.
DR CGD; CAL0000171205; Cd36_70870.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000002605; 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..686
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411909"
FT TOPO_DOM 20..543
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 489..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..519
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 686 AA; 77574 MW; D6525FC9603CA262 CRC64;
MKFLLPTFII FIYTLLVSAL PTKEGSDPKA AKKYLVSDLP GLHDNITPDD SIPLMFAGQL
EIYPESNTHY FFWKFSDSNQ ETITNRTIFW LNGGPGCSSM DGALLETGPF RINSQQQVIS
NNGSWHKSGD IIYVDQPAGT GFSYSDTYIT DLDQVANYFL KFMEAYYELF PQEINNEIYF
AGESYAGQYI PYIANAILQR NKKLHEGEQK YDLRGVLIGN GWVSPNEQSL SYLPFFKDHG
LIDIHHPKWA TLLAKHEQCQ KIVNKIDSTF DDGTVHYYEV SSSTCEAILT DLLEYTQDTA
NDKNQQCINM YDYTLRDSYP SCGMNWPNEL VNVGPFLRQE KVMHQLNLIN LKKWNECNGK
VGRTFQARHS IPSVHLLPEL AKEIPVMLFN GANDIICNSQ GVLSYLQKLQ WNGETGFINK
DNQISWVYDN KEVGYMLWER NISFINIYNS SHMVPYDLPD VSRALIDLIT GEYDEKDVDG
KKSFVTYPLG SRKENDESKN PVESPSQTID PIISSSSSSV ESSLSSSSAS ATDSDSTSSK
FTRLIQLAVI LVIFWGVYVL YASYKSRPSS IIKKPTNNTS NITRSSTGKK KNVQWADQLN
QFEDDERNQE SNQGIIAKAI GKITGSKDTR GRYAPVHREN DNEYIDDIEL GEGISDPNVD
EFIIGSDDDD EEEQPRSDPA THKSVS
