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   22-FEB-2023, entry version 41.
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   GlyCosmos; C7GWZ2; 3 sites, No reported glycans.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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; alpha/beta hydrolase; 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:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//