ID KEX1_YEASO Reviewed; 738 AA.
AC E7NHF8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=FOSTERSO_1568;
OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FostersO;
RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "Whole-genome comparison reveals novel genetic elements that characterize
RT the genome of industrial strains of Saccharomyces cerevisiae.";
RL PLoS Genet. 7:E1001287-E1001287(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEEZ01000037; EGA62437.1; -; Genomic_DNA.
DR AlphaFoldDB; E7NHF8; -.
DR SMR; E7NHF8; -.
DR ESTHER; yeast-kex01; Carboxypeptidase_S10.
DR GlyCosmos; E7NHF8; 3 sites, No reported glycans.
DR HOGENOM; CLU_008523_11_2_1; -.
DR OMA; PLMFAGQ; -.
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..738
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411956"
FT TOPO_DOM 23..625
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 503..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..608
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 669
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 738 AA; 83279 MW; EE0BDADFD4ACF26B CRC64;
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS
EDADEQDSSD 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 IMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK
EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDDDDDD DDDEDDNNEK TKVNQGLEDS
RHKSSEYEQE EEEVEEFAEE ISMYKHKAVV VTIVTFLIVV LGVYAYDRRV RRKARHTILV
DPNNRQHDSP NKTVSWADDL ESGLGAEDDL EQDEQLEGGA PISSTSNKAG SKLKTKKKKK
YTSLPNTEID ESFEMTDF
//
