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P09620

- KEX1_YEAST

UniProt

P09620 - KEX1_YEAST

Protein

Pheromone-processing carboxypeptidase KEX1

Gene

KEX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BioCyciMetaCyc:YGL203C-MONOMER.
    YEAST:YGL203C-MONOMER.

    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: 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

    GO - Cellular componenti

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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AC5X-ray2.40A23-505[»]
    ProteinModelPortaliP09620.
    SMRiP09620. Positions 23-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09620.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei617 – 63721HelicalSequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00730000111054.
    HOGENOMiHOG000113220.
    KOiK01288.
    OMAiSVYNASH.
    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

    MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ    50
    MHAGHIPLRS EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG 100
    CSSMDGALVE SGPFRVNSDG KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ 150
    NKDEGKIDKN KFDEDLEDVT KHFMDFLENY FKIFPEDLTR KIILSGESYA 200
    GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN TQSLSYLPFA 250
    MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL 300
    LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDISF VSKFFSTPGV 350
    IDSLHLDSDK IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF 400
    NGDKDLICNN KGVLDTIDNL KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF 450
    SGYVKYDRNL TFVSVYNASH MVPFDKSLVS RGIVDIYSND VMIIDNNGKN 500
    VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK EGNKDKDGDD 550
    DNDNDDDDED DHNSEGDDDD DDDDDEDDNN EKQSNQGLED SRHKSSEYEQ 600
    EEEEVEEFAE EISMYKHKAV VVTIVTFLIV VLGVYAYDRR VRRKARHTIL 650
    VDPNNRQHDS PNKTVSWADD LESGLGAEDD LEQDEQLEGG APISSTSNKA 700
    GSKLKTKKKK KYTSLPNTEI DESFEMTDF 729
    Length:729
    Mass (Da):82,245
    Last modified:July 1, 1989 - v1
    Checksum:i70583F279AC02A41
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17231 Genomic DNA. Translation: AAA34717.1 .
    Z72725 Genomic DNA. Translation: CAA96915.1 .
    BK006941 Genomic DNA. Translation: DAA07912.1 .
    PIRi A29651.
    RefSeqi NP_011312.1. NM_001181068.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AC5 X-ray 2.40 A 23-505 [» ]
    ProteinModelPortali P09620.
    SMRi P09620. Positions 23-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33053. 102 interactions.
    IntActi P09620. 57 interactions.
    MINTi MINT-2780061.
    STRINGi 4932.YGL203C.

    Protein family/group databases

    MEROPSi S10.007.

    Proteomic databases

    MaxQBi P09620.
    PaxDbi P09620.
    PeptideAtlasi P09620.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL203C ; YGL203C ; YGL203C .
    GeneIDi 852670.
    KEGGi sce:YGL203C.

    Organism-specific databases

    CYGDi YGL203c.
    SGDi S000003171. KEX1.

    Phylogenomic databases

    eggNOGi COG2939.
    GeneTreei ENSGT00730000111054.
    HOGENOMi HOG000113220.
    KOi K01288.
    OMAi SVYNASH.
    OrthoDBi EOG7TJ3SJ.

    Enzyme and pathway databases

    BioCyci MetaCyc:YGL203C-MONOMER.
    YEAST:YGL203C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P09620.
    NextBioi 971968.

    Gene expression databases

    Genevestigatori P09620.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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(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.

    Entry informationi

    Entry nameiKEX1_YEAST
    AccessioniPrimary (citable) accession number: P09620
    Secondary accession number(s): D6VTV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 137 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