KEX1_YEAS2
ID KEX1_YEAS2 Reviewed; 737 AA.
AC C7GWZ2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE AltName: Full=Killer expression defective protein 1;
DE Flags: Precursor;
GN Name=KEX1; ORFNames=C1Q_05019;
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291;
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.G.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
CC -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC the C-terminal processing of the lysine and arginine residues from the
CC precursors of K1, K2 and K28 killer toxins and a-factor (mating
CC pheromone). Involved in the programmed cell death caused by defective
CC N-glycosylation and contributes also to the active cell death program
CC induced by acetic acid stress or during chronological aging. Promotes
CC cell fusion by proteolytically processing substrates that act in
CC parallel to PRM1 as an alternative fusion machine, as cell wall
CC components, or both (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; ACFL01000397; EEU04662.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GWZ2; -.
DR SMR; C7GWZ2; -.
DR ESTHER; yeast-kex01; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR PRIDE; C7GWZ2; -.
DR Proteomes; UP000008073; Unassembled WGS sequence.
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 InterPro; IPR018202; Ser_caboxypep_ser_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.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Phosphoprotein; Protease; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..737
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411954"
FT TOPO_DOM 23..624
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 502..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..588
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /evidence="ECO:0000250"
FT ACT_SITE 470
FT /evidence="ECO:0000250"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09620"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 737 AA; 83179 MW; 9379A1E2CBC66548 CRC64;
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS
EDADEQDNSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG
KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY
FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN
TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL
LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDVSF VSKFFSTPGV IDSLHLDSDK
IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL
KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS
RGIVDIYSND VMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK
EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDDDDDD DDDEDDNNEK QSNQGLEDSR
HKSSEYEQEE EEVEEFAEEI SMYKHKAVVV TIVTFLIVVL GVYAYDRRVR RKARHTILVD
PNNRQHDSPN KTVSWADDLE SGLGAEDDLE QDEQLEGGAP ISSTSNKAGS KLKTKKKKKY
TSLPNTEIDE SFEMTDF
