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Protein

Pheromone-processing carboxypeptidase KEX1

Gene

KEX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.11 Publications

Catalytic activityi

Preferential release of a C-terminal arginine or lysine residue.

Kineticsi

  1. KM=284 µM for benzoyl-Phe-Ala-Arg1 Publication
  2. KM=516 µM for furylacryloyl-Ala-Arg1 Publication
  3. KM=962 µM for furylacryloyl-Ala-Lys1 Publication

Vmax=64.25 µmol/min/mg enzyme toward benzoyl-Phe-Ala-Arg1 Publication

Vmax=22.35 µmol/min/mg enzyme toward furylacryloyl-Ala-Arg1 Publication

Vmax=11.55 µmol/min/mg enzyme toward furylacryloyl-Ala-Lys1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981
Active sitei405 – 4051By similarity
Active sitei470 – 4701By similarity

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: SGD

GO - Biological processi

  1. apoptotic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciMetaCyc:YGL203C-MONOMER.
YEAST:YGL203C-MONOMER.
BRENDAi3.4.16.6. 984.

Protein family/group databases

MEROPSiS10.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Pheromone-processing carboxypeptidase KEX1 (EC:3.4.16.6)
Alternative name(s):
Carboxypeptidase D
Killer expression defective protein 1
Gene namesi
Name:KEX1
Ordered Locus Names:YGL203C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL203c.
SGDiS000003171. KEX1.

Subcellular locationi

Golgi apparatustrans-Golgi network membrane 2 Publications; Single-pass type I membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 616594LumenalSequence AnalysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence AnalysisAdd
BLAST
Topological domaini638 – 72992CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981S → A: Inactivates enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 729707Pheromone-processing carboxypeptidase KEX1PRO_0000004287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)1 Publication
Glycosylationi467 – 4671N-linked (GlcNAc...)1 Publication
Modified residuei660 – 6601Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP09620.
PaxDbiP09620.
PeptideAtlasiP09620.

Expressioni

Gene expression databases

GenevestigatoriP09620.

Interactioni

Protein-protein interaction databases

BioGridi33053. 102 interactions.
IntActiP09620. 57 interactions.
MINTiMINT-2780061.
STRINGi4932.YGL203C.

Structurei

Secondary structure

1
729
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283Combined sources
Helixi33 – 353Combined sources
Helixi39 – 413Combined sources
Beta strandi50 – 578Combined sources
Beta strandi61 – 633Combined sources
Beta strandi72 – 798Combined sources
Helixi84 – 863Combined sources
Beta strandi91 – 955Combined sources
Turni98 – 1003Combined sources
Helixi104 – 1096Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi122 – 1243Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1386Combined sources
Helixi154 – 1563Combined sources
Helixi166 – 18318Combined sources
Helixi187 – 1893Combined sources
Beta strandi190 – 1989Combined sources
Helixi200 – 21718Combined sources
Beta strandi226 – 23510Combined sources
Helixi239 – 2435Combined sources
Helixi246 – 2527Combined sources
Helixi263 – 27917Combined sources
Helixi283 – 2864Combined sources
Beta strandi287 – 2893Combined sources
Helixi291 – 2944Combined sources
Helixi296 – 3038Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi320 – 3256Combined sources
Turni327 – 3337Combined sources
Helixi337 – 3459Combined sources
Helixi350 – 3534Combined sources
Turni358 – 3603Combined sources
Helixi369 – 3746Combined sources
Helixi383 – 3864Combined sources
Helixi387 – 3926Combined sources
Beta strandi396 – 4027Combined sources
Helixi410 – 41910Combined sources
Beta strandi425 – 4284Combined sources
Beta strandi433 – 4397Combined sources
Beta strandi452 – 4576Combined sources
Beta strandi460 – 4656Combined sources
Helixi472 – 4754Combined sources
Helixi477 – 48711Combined sources
Beta strandi492 – 4965Combined sources
Beta strandi499 – 5046Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AC5X-ray2.40A23-505[»]
SMRiP09620. Positions 23-505.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09620.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi526 – 5316Poly-Glu
Compositional biasi545 – 56117Poly-AspAdd
BLAST
Compositional biasi567 – 57812Poly-AspAdd
BLAST
Compositional biasi597 – 60711Poly-GluAdd
BLAST
Compositional biasi703 – 7119Poly-Lys

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2939.
GeneTreeiENSGT00770000120640.
HOGENOMiHOG000113220.
InParanoidiP09620.
KOiK01288.
OMAiNYFKIFP.
OrthoDBiEOG7TJ3SJ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ
60 70 80 90 100
MHAGHIPLRS EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG
110 120 130 140 150
CSSMDGALVE SGPFRVNSDG KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ
160 170 180 190 200
NKDEGKIDKN KFDEDLEDVT KHFMDFLENY FKIFPEDLTR KIILSGESYA
210 220 230 240 250
GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN TQSLSYLPFA
260 270 280 290 300
MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL
310 320 330 340 350
LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDISF VSKFFSTPGV
360 370 380 390 400
IDSLHLDSDK IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF
410 420 430 440 450
NGDKDLICNN KGVLDTIDNL KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF
460 470 480 490 500
SGYVKYDRNL TFVSVYNASH MVPFDKSLVS RGIVDIYSND VMIIDNNGKN
510 520 530 540 550
VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK EGNKDKDGDD
560 570 580 590 600
DNDNDDDDED DHNSEGDDDD DDDDDEDDNN EKQSNQGLED SRHKSSEYEQ
610 620 630 640 650
EEEEVEEFAE EISMYKHKAV VVTIVTFLIV VLGVYAYDRR VRRKARHTIL
660 670 680 690 700
VDPNNRQHDS PNKTVSWADD LESGLGAEDD LEQDEQLEGG APISSTSNKA
710 720
GSKLKTKKKK KYTSLPNTEI DESFEMTDF
Length:729
Mass (Da):82,245
Last modified:June 30, 1989 - v1
Checksum:i70583F279AC02A41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17231 Genomic DNA. Translation: AAA34717.1.
Z72725 Genomic DNA. Translation: CAA96915.1.
BK006941 Genomic DNA. Translation: DAA07912.1.
PIRiA29651.
RefSeqiNP_011312.1. NM_001181068.1.

Genome annotation databases

EnsemblFungiiYGL203C; YGL203C; YGL203C.
GeneIDi852670.
KEGGisce:YGL203C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17231 Genomic DNA. Translation: AAA34717.1.
Z72725 Genomic DNA. Translation: CAA96915.1.
BK006941 Genomic DNA. Translation: DAA07912.1.
PIRiA29651.
RefSeqiNP_011312.1. NM_001181068.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AC5X-ray2.40A23-505[»]
SMRiP09620. Positions 23-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33053. 102 interactions.
IntActiP09620. 57 interactions.
MINTiMINT-2780061.
STRINGi4932.YGL203C.

Protein family/group databases

MEROPSiS10.007.

Proteomic databases

MaxQBiP09620.
PaxDbiP09620.
PeptideAtlasiP09620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL203C; YGL203C; YGL203C.
GeneIDi852670.
KEGGisce:YGL203C.

Organism-specific databases

CYGDiYGL203c.
SGDiS000003171. KEX1.

Phylogenomic databases

eggNOGiCOG2939.
GeneTreeiENSGT00770000120640.
HOGENOMiHOG000113220.
InParanoidiP09620.
KOiK01288.
OMAiNYFKIFP.
OrthoDBiEOG7TJ3SJ.

Enzyme and pathway databases

BioCyciMetaCyc:YGL203C-MONOMER.
YEAST:YGL203C-MONOMER.
BRENDAi3.4.16.6. 984.

Miscellaneous databases

EvolutionaryTraceiP09620.
NextBioi971968.

Gene expression databases

GenevestigatoriP09620.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing."
    Dmochowska A., Dignard D., Henning D., Thomas D.Y., Bussey H.
    Cell 50:573-584(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF SER-198.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Chromosomal and nonchromosomal mutations affecting the 'killer character' of Saccharomyces cerevisiae."
    Wickner R.B.
    Genetics 76:423-432(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae."
    Wickner R.B., Leibowitz M.J.
    Genetics 82:429-442(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Hormone (pheromone) processing enzymes in yeast. The carboxy-terminal processing enzyme of the mating pheromone alpha-factor, carboxypeptidase ysc alpha, is absent in alpha-factor maturation-defective kex1 mutant cells."
    Wagner J.C., Wolf D.H.
    FEBS Lett. 221:423-426(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Determination of the carboxyl termini of the alpha and beta subunits of yeast K1 killer toxin. Requirement of a carboxypeptidase B-like activity for maturation."
    Zhu H., Bussey H., Thomas D.Y., Gagnon J., Bell A.W.
    J. Biol. Chem. 262:10728-10732(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins."
    Cooper A., Bussey H.
    Mol. Cell. Biol. 9:2706-2714(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane."
    Cooper A., Bussey H.
    J. Cell Biol. 119:1459-1468(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, FUNCTION, SUBCELLULAR LOCATION.
  10. "Expression, purification, and characterization of the yeast KEX1 gene product, a polypeptide precursor processing carboxypeptidase."
    Latchinian-Sadek L., Thomas D.Y.
    J. Biol. Chem. 268:534-540(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Endocytotic uptake and retrograde transport of a virally encoded killer toxin in yeast."
    Eisfeld K., Riffer F., Mentges J., Schmitt M.J.
    Mol. Microbiol. 37:926-940(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Mutational analysis of K28 preprotoxin processing in the yeast Saccharomyces cerevisiae."
    Riffer F., Eisfeld K., Breinig F., Schmitt M.J.
    Microbiology 148:1317-1328(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating."
    Heiman M.G., Engel A., Walter P.
    J. Cell Biol. 176:209-222(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Kex1 protease is involved in yeast cell death induced by defective N-glycosylation, acetic acid, and chronological aging."
    Hauptmann P., Lehle L.
    J. Biol. Chem. 283:19151-19163(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae."
    Shilton B.H., Li Y., Tessier D., Thomas D.Y., Cygler M.
    Protein Sci. 5:395-397(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  20. "Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae."
    Shilton B.H., Thomas D.Y., Cygler M.
    Biochemistry 36:9002-9012(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-505.

Entry informationi

Entry nameiKEX1_YEAST
AccessioniPrimary (citable) accession number: P09620
Secondary accession number(s): D6VTV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1989
Last sequence update: June 30, 1989
Last modified: March 31, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.