KEX1_ZYGRC
ID KEX1_ZYGRC Reviewed; 684 AA.
AC C5DT72;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=ZYRO0C06006g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(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; CU928175; CAR26983.1; -; Genomic_DNA.
DR RefSeq; XP_002495916.1; XM_002495871.1.
DR AlphaFoldDB; C5DT72; -.
DR SMR; C5DT72; -.
DR STRING; 559307.C5DT72; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; CAR26983; CAR26983; ZYRO0C06006g.
DR GeneID; 8203117; -.
DR KEGG; zro:ZYRO0C06006g; -.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; C5DT72; -.
DR Proteomes; UP000008536; Chromosome C.
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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..684
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411957"
FT TOPO_DOM 17..588
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 498..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..549
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 78284 MW; BDC4CF4CFF0A311E CRC64;
MRFWYFSAIL WVVCQALPSK KQYSVAPELL PGLSEIEDKS TIPEMYAGHM PLAQSNSDDK
DEIDYFFWKF SRPDKVLNTL IIWLNGGPGC SSMDGALVEN GPFRVNKDLK LVVNEGSWHT
RADMLYVDQP VNTGFSVSNS KEKKYDEDLT LTTQHFMDFL ESYFKVFPDD QFKDLIIAGE
SYSGQYVPFL AEAIQKRNAE TSDDLAKYNL RGILVGNGWM DPDTQSLAYL PFALSKGLID
QNNPHFSTLL RQQEKCQDRI ISRNPNEHQP FQYEECENIL QSILTATRDV SADTPSNQVC
MNIYSYNLRD SYPACGSNWP DEVLHVPGFF DRPGILEALN LDPSKVPQWK ECNLEVYYHL
KNRKAVPSVR KLPALLDSGL KVILYNGEMD LLCNERGVLD MIDKLQWGGA KGFSSKTKEY
DWNYRDFETN TDHIAGNVLH DRNLTYISVH NASHMVPNDK SLYSRGVVDI YLDDIFLEEL
HGKDVLVTTS EKDMDDFDNS KLGVLGITDG KPSEEEELEE EFDQYVDELE EGESESGLLD
DDKEDETVGA TDQNDDKNKG GEDKPNENPD KEKEEQDRQR KRRKGTFKIF GITILVVLTL
GSFVFYIYIR KHTNKTRAIL IDPSRRQHDS QNKRVSWADD LEHGYDFETD QSQPRSGQSA
PKKNGSYTRV PNTELDESFE LENL
