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P09620 (KEX1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pheromone-processing carboxypeptidase KEX1

EC=3.4.16.6
Alternative name(s):
Carboxypeptidase D
Killer expression defective protein 1
Gene names
Name:KEX1
Ordered Locus Names:YGL203C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.17

Catalytic activity

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

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein Ref.9 Ref.13.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase S10 family.

Biophysicochemical properties

Kinetic parameters:

KM=284 µM for benzoyl-Phe-Ala-Arg Ref.10

KM=516 µM for furylacryloyl-Ala-Arg

KM=962 µM for furylacryloyl-Ala-Lys

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 729707Pheromone-processing carboxypeptidase KEX1
PRO_0000004287

Regions

Topological domain23 – 616594Lumenal Potential
Transmembrane617 – 63721Helical; Potential
Topological domain638 – 72992Cytoplasmic Potential
Compositional bias526 – 5316Poly-Glu
Compositional bias545 – 56117Poly-Asp
Compositional bias567 – 57812Poly-Asp
Compositional bias597 – 60711Poly-Glu
Compositional bias703 – 7119Poly-Lys

Sites

Active site1981
Active site4051 By similarity
Active site4701 By similarity

Amino acid modifications

Modified residue6601Phosphoserine Ref.16
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation4591N-linked (GlcNAc...)
Glycosylation4671N-linked (GlcNAc...)

Experimental info

Mutagenesis1981S → A: Inactivates enzyme. Ref.1

Secondary structure

......................................................................................... 729
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09620 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 70583F279AC02A41

FASTA72982,245
        10         20         30         40         50         60 
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS 

        70         80         90        100        110        120 
EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG 

       130        140        150        160        170        180 
KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY 

       190        200        210        220        230        240 
FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN 

       250        260        270        280        290        300 
TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL 

       310        320        330        340        350        360 
LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDISF VSKFFSTPGV IDSLHLDSDK 

       370        380        390        400        410        420 
IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL 

       430        440        450        460        470        480 
KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS 

       490        500        510        520        530        540 
RGIVDIYSND VMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK 

       550        560        570        580        590        600 
EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDEDDNN EKQSNQGLED SRHKSSEYEQ 

       610        620        630        640        650        660 
EEEEVEEFAE EISMYKHKAV VVTIVTFLIV VLGVYAYDRR VRRKARHTIL VDPNNRQHDS 

       670        680        690        700        710        720 
PNKTVSWADD LESGLGAEDD LEQDEQLEGG APISSTSNKA GSKLKTKKKK KYTSLPNTEI 


DESFEMTDF 

« Hide

References

« Hide 'large scale' references
[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(1987) [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. expand/collapse author list , 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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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(1974) [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(1976) [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(1987) [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(1987) [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(1989) [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(1992) [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(1993) [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(2000) [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(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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(2007) [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(2007) [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(2008) [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(2009) [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(1996) [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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-505.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17231 Genomic DNA. Translation: AAA34717.1.
Z72725 Genomic DNA. Translation: CAA96915.1.
BK006941 Genomic DNA. Translation: DAA07912.1.
PIRA29651.
RefSeqNP_011312.1. NM_001181068.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AC5X-ray2.40A23-505[»]
ProteinModelPortalP09620.
SMRP09620. Positions 23-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33053. 102 interactions.
IntActP09620. 57 interactions.
MINTMINT-2780061.
STRING4932.YGL203C.

Protein family/group databases

MEROPSS10.007.

Proteomic databases

MaxQBP09620.
PaxDbP09620.
PeptideAtlasP09620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL203C; YGL203C; YGL203C.
GeneID852670.
KEGGsce:YGL203C.

Organism-specific databases

CYGDYGL203c.
SGDS000003171. KEX1.

Phylogenomic databases

eggNOGCOG2939.
GeneTreeENSGT00730000111054.
HOGENOMHOG000113220.
KOK01288.
OMASVYNASH.
OrthoDBEOG7TJ3SJ.

Enzyme and pathway databases

BioCycMetaCyc:YGL203C-MONOMER.
YEAST:YGL203C-MONOMER.

Gene expression databases

GenevestigatorP09620.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09620.
NextBio971968.

Entry information

Entry nameKEX1_YEAST
AccessionPrimary (citable) accession number: P09620
Secondary accession number(s): D6VTV1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references