KEX2_CANAW
ID KEX2_CANAW Reviewed; 938 AA.
AC O13359; C4YDD7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Kexin;
DE EC=3.4.21.61;
DE AltName: Full=KEX2 protease;
DE Flags: Precursor;
GN Name=KEX2; ORFNames=CAWG_00530;
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 [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=9360967; DOI=10.1074/jbc.272.46.28954;
RA Newport G.R., Agabian N.;
RT "KEX2 influences Candida albicans proteinase secretion and hyphal
RT formation.";
RL J. Biol. Chem. 272:28954-28961(1997).
RN [2]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to
CC process yeast alpha-factor pheromone and killer toxin precursors.;
CC EC=3.4.21.61;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80929.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF022372; AAB80929.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CH672346; EEQ42323.1; -; Genomic_DNA.
DR AlphaFoldDB; O13359; -.
DR SMR; O13359; -.
DR STRING; 5476.O13359; -.
DR EnsemblFungi; EEQ42323; EEQ42323; CAWG_00530.
DR VEuPathDB; FungiDB:CAWG_00530; -.
DR HOGENOM; CLU_002976_2_1_1; -.
DR OMA; AYEFDII; -.
DR PHI-base; PHI:306; -.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000027041"
FT CHAIN ?..938
FT /note="Kexin"
FT /id="PRO_0000027042"
FT TOPO_DOM ?..774
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..924
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 179..489
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 498..647
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 671..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..835
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
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 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 267..414
FT /evidence="ECO:0000250"
FT DISULFID 359..389
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="N -> D (in Ref. 1; AAB80929)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="F -> S (in Ref. 1; AAB80929)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="T -> A (in Ref. 1; AAB80929)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="E -> EEEE (in Ref. 1; AAB80929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 938 AA; 105144 MW; 7E72BE8AD9FAA9FF CRC64;
MLPIKLLIFI LGYLLSPTLQ QYQQIPPRDY ENKNYFLVEL NTTNSQKPLI DFISHYRGHY
NFEHQLSSLD NHYVFSIDKS HPHNSFLGNH NSNEYNLMKR QLGHEQDYDE LISHVESIHL
LPMKKLSKRI PVPIEMEDVV FDNRDDTGSD NHEATDEAHQ KLIEIAKKLD IHDPEFTTQW
HLINLKYPGH DVNVTGLWLE NILGQGIVTA LVDDGVDAES DDIKQNFNSE GSWDFNNKGK
SPLPRLFDDY HGTRCAGEIA AVKNDVCGIG VAWKSQVSGI RILSGPITSS DEAEAMVYGL
DTNDIYSCSW GPTDNGKVLS EPDVIVKKAM IKGIQEGRDK KGAIYVFASG NGGRFGDSCN
FDGYTNSIYS ITVGAIDYKG LHPQYSEACS AVMVVTYSSG SGEHIHTTDI KKKCSATHGG
TSAAAPLASG IYSLILSANP NLTWRDVQYI SVLSATPINE EDGNYQTTAL NRKYSHKYGY
GKTDAYKMVH FAKTWVNVKP QAWYYSDIIE VNQTITTTPE QKAPSKRDSP QKIIHSSVNV
SEKDLKIMNV ERVEHITVKV NIDSTYRGRV GMRIISPTGV ISDLATFRVN DASTRGFQNW
TFMSVAHWGE TGIGEWKVEV FVDDSKGDQV EINFKDWQFR IFGESIDGDK AEVYDITKDY
AAIRRELLEK EKQNSKSTTT TSSTTTATTT SGGEGDQKTT TSAENKESTT KVDNSASITT
SQTASLTSSN EQHQPTESNS DSDSDTDDEN KQEGEEDNDN DNDNGNKKAN SDNTGFYLMS
IAVVGFIAVL LVMKFHKTPG SGRRRRRRDG YEFDIIPGED YSDSDDDEDD FDTRRADDDS
FDLGHRNDQR VVSASQQQRQ YDRQQDETRD RLFDDFNAES LPDYENDMFK IGDEEEEEEE
GQQSAKAPSN SEGNSGTSTK KYKDNEADED HKDVVGTQ
