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Reviewed, UniProtKB/Swiss-Prot P13134 (KEX2_YEAST)

Last modified June 16, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Kexin
    EC=3.4.21.61
Alternative name(s):
    KEX2 protease
    Proteinase YSCF
Gene names
Name: KEX2
Synonyms: QDS1
Ordered Locus Names: YNL238W
ORF Names: N1122
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length814 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Processing of precursors of alpha-factors and killer toxin.

Catalytic activity

Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.

Cofactor

Binds 3 calcium ions per subunit.

Subcellular location

Golgi apparatus › trans-Golgi network membrane; Single-pass type I membrane protein.

Post-translational modification

O-glycosylated.

Sequence similarities

Belongs to the peptidase S8 family. Furin subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 10990
PRO_0000027043
Propeptide110 – 1134Removed by dipeptidylpeptidase STE13
PRO_0000027044
Chain114 – 814701Kexin
PRO_0000027045

Regions

Topological domain114 – 678565Lumenal Potential
Transmembrane679 – 69921 Potential
Topological domain700 – 814115Cytoplasmic Potential
Region114 – 461348Catalytic
Region462 – 599138P-domain
Compositional bias625 – 64218Ser/Thr-rich

Sites

Active site1751Charge relay system
Active site2131Charge relay system
Active site3851Charge relay system
Metal binding1351Calcium 1
Metal binding1841Calcium 1
Metal binding2271Calcium 1
Metal binding2771Calcium 2
Metal binding3201Calcium 2
Metal binding3501Calcium 2

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...)
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...)
Disulfide bond230 ↔ 377
Disulfide bond322 ↔ 352

Secondary structure

1 ........................................................................................ 814
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13134-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 5DCEEDADCF439C78

FASTA81490,003
        10         20         30         40         50         60 
MKVRKYITLC FWWAFSTSAL VSSQQIPLKD HTSRQYFAVE SNETLSRLEE MHPNWKYEHD 

        70         80         90        100        110        120 
VRGLPNHYVF SKELLKLGKR SSLEELQGDN NDHILSVHDL FPRNDLFKRL PVPAPPMDSS 

       130        140        150        160        170        180 
LLPVKEAEDK LSINDPLFER QWHLVNPSFP GSDINVLDLW YNNITGAGVV AAIVDDGLDY 

       190        200        210        220        230        240 
ENEDLKDNFC AEGSWDFNDN TNLPKPRLSD DYHGTRCAGE IAAKKGNNFC GVGVGYNAKI 

       250        260        270        280        290        300 
SGIRILSGDI TTEDEAASLI YGLDVNDIYS CSWGPADDGR HLQGPSDLVK KALVKGVTEG 

       310        320        330        340        350        360 
RDSKGAIYVF ASGNGGTRGD NCNYDGYTNS IYSITIGAID HKDLHPPYSE GCSAVMAVTY 

       370        380        390        400        410        420 
SSGSGEYIHS SDINGRCSNS HGGTSAAAPL AAGVYTLLLE ANPNLTWRDV QYLSILSAVG 

       430        440        450        460        470        480 
LEKNADGDWR DSAMGKKYSH RYGFGKIDAH KLIEMSKTWE NVNAQTWFYL PTLYVSQSTN 

       490        500        510        520        530        540 
STEETLESVI TISEKSLQDA NFKRIEHVTV TVDIDTEIRG TTTVDLISPA GIISNLGVVR 

       550        560        570        580        590        600 
PRDVSSEGFK DWTFMSVAHW GENGVGDWKI KVKTTENGHR IDFHSWRLKL FGESIDSSKT 

       610        620        630        640        650        660 
ETFVFGNDKE EVEPAATEST VSQYSASSTS ISISATSTSS ISIGVETSAI PQTTTASTDP 

       670        680        690        700        710        720 
DSDPNTPKKL SSPRQAMHYF LTIFLIGATF LVLYFMFFMK SRRRIRRSRA ETYEFDIIDT 

       730        740        750        760        770        780 
DSEYDSTLDN GTSGITEPEE VEDFDFDLSD EDHLASLSSS ENGDAEHTID SVLTNENPFS 

       790        800        810 
DPIKQKFPND ANAESASNKL QELQPDVPPS SGRS

« Hide

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References

« Hide 'large scale' references
[1]"Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases."
Mizuno K., Nakamura T., Ohshima T., Tanaka S., Matsuo H.
Biochem. Biophys. Res. Commun. 156:246-254(1988) [PubMed: 2845974] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease."
Fuller R.S., Brake A., Thorner J.
Proc. Natl. Acad. Sci. U.S.A. 86:1434-1438(1989) [PubMed: 2646633] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
Yeast 12:1071-1076(1996) [PubMed: 8896273] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed: 9169873] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[5]"Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease."
Brenner C., Fuller R.S.
Proc. Natl. Acad. Sci. U.S.A. 89:922-926(1992) [PubMed: 1736307] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, CHARACTERIZATION.
[6]"The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing."
Germain D., Dumas F., Vernet T., Bourbonnais Y., Thomas D.Y., Boileau G.
FEBS Lett. 299:283-286(1992) [PubMed: 1544507] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[7]"Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway."
Wilcox C.A., Fuller R.S.
J. Cell Biol. 115:297-307(1991) [PubMed: 1918142] [Abstract]
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[8]"2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor."
Holyoak T., Wilson M.A., Fenn T.D., Kettner C.A., Petsko G.A., Fuller R.S., Ringe D.
Biochemistry 42:6709-6718(2003) [PubMed: 12779325] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 123-599 IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M22870 Genomic DNA. Translation: AAA34719.1.
M24201 Genomic DNA. Translation: AAA34718.1.
Z69381 Genomic DNA. Translation: CAA93360.1.
Z71514 Genomic DNA. Translation: CAA96143.1.
PIRKXBY. A28931.
RefSeqNP_014161.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OT5X-ray2.40A/B123-599[»]
1R64X-ray2.20A/B121-601[»]
2ID4X-ray1.90A/B114-613[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6287N.
IntActP13134. 20 interactions.

Protein family/group databases

MEROPSS08.070.

Proteomic databases

PeptideAtlasP13134.

Genome annotation databases

EnsemblYNL238W. Saccharomyces cerevisiae. [Contig view]
GeneID855483.
GenomeReviewsGene locus YNL238W in contig Y13139_GR.
KEGGsce:YNL238W.
NMPDRfig|4932.3.peg.5226.

Organism-specific databases

CYGDYNL238w.
SGDS000005182. KEX2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP13134.
OMAP13134. EACSAVM.

Enzyme and pathway databases

BRENDA3.4.21.61. 250.

Gene expression databases

ArrayExpressP13134.
GermOnlineYNL238W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
ProDomPD000717. PrprotnconvertsP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio979454.
PMAP-CutDBP13134.

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Entry information

Entry nameKEX2_YEAST
AccessionPrimary (citable) accession number: P13134
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 16, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIV

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents