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Protein

Kexin

Gene

KEX2

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

Processing of precursors of alpha-factors and killer toxin.

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 3 Ca2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi135 – 1351Calcium 1
Active sitei175 – 1751Charge relay system
Metal bindingi184 – 1841Calcium 1
Active sitei213 – 2131Charge relay system
Metal bindingi227 – 2271Calcium 1
Metal bindingi277 – 2771Calcium 2
Metal bindingi320 – 3201Calcium 2
Metal bindingi350 – 3501Calcium 2
Active sitei385 – 3851Charge relay system

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: SGD

GO - Biological processi

  • peptide pheromone maturation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YNL238W-MONOMER.
BRENDAi3.4.21.61. 984.

Protein family/group databases

MEROPSiS08.070.

Names & Taxonomyi

Protein namesi
Recommended name:
Kexin (EC:3.4.21.61)
Alternative name(s):
Protease KEX2
Proteinase YSCF
Gene namesi
Name:KEX2
Synonyms:QDS1
Ordered Locus Names:YNL238W
ORF Names:N1122
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL238W.
SGDiS000005182. KEX2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini114 – 678565LumenalSequence analysisAdd
BLAST
Transmembranei679 – 69921HelicalSequence analysisAdd
BLAST
Topological domaini700 – 814115CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 10990PRO_0000027043Add
BLAST
Propeptidei110 – 1134Removed by dipeptidylpeptidase STE13PRO_0000027044
Chaini114 – 814701KexinPRO_0000027045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)
Disulfide bondi230 ↔ 377
Disulfide bondi322 ↔ 352
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP13134.
PeptideAtlasiP13134.

Miscellaneous databases

PMAP-CutDBP13134.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SLA1P3279016EBI-9658,EBI-17313

Protein-protein interaction databases

BioGridi35601. 156 interactions.
DIPiDIP-6287N.
IntActiP13134. 14 interactions.
MINTiMINT-2787516.

Structurei

Secondary structure

1
814
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 1308Combined sources
Helixi138 – 1403Combined sources
Turni142 – 1443Combined sources
Beta strandi147 – 1493Combined sources
Helixi157 – 1615Combined sources
Beta strandi170 – 1767Combined sources
Turni183 – 1886Combined sources
Helixi191 – 1933Combined sources
Turni197 – 2004Combined sources
Turni209 – 2124Combined sources
Helixi213 – 22210Combined sources
Beta strandi225 – 2306Combined sources
Turni234 – 2374Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi246 – 2483Combined sources
Helixi252 – 2587Combined sources
Turni259 – 2657Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi278 – 2803Combined sources
Helixi287 – 30317Combined sources
Beta strandi307 – 3115Combined sources
Helixi316 – 3183Combined sources
Helixi322 – 3243Combined sources
Turni326 – 3294Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi355 – 3606Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi377 – 3815Combined sources
Helixi384 – 40118Combined sources
Helixi407 – 41711Combined sources
Helixi425 – 4273Combined sources
Beta strandi433 – 4397Combined sources
Turni440 – 4423Combined sources
Helixi449 – 4568Combined sources
Beta strandi465 – 4695Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi486 – 4927Combined sources
Helixi494 – 4996Combined sources
Beta strandi502 – 51817Combined sources
Helixi519 – 5213Combined sources
Beta strandi522 – 5276Combined sources
Beta strandi533 – 5375Combined sources
Beta strandi549 – 5579Combined sources
Turni558 – 5614Combined sources
Beta strandi566 – 57611Combined sources
Beta strandi581 – 59515Combined sources
Helixi597 – 5993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT5X-ray2.40A/B123-599[»]
1R64X-ray2.20A/B121-601[»]
2ID4X-ray1.90A/B114-613[»]
ProteinModelPortaliP13134.
SMRiP13134. Positions 121-601.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13134.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 453283Peptidase S8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 599138P-domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi625 – 64218Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
InParanoidiP13134.
KOiK01341.
OMAiQWHLINP.
OrthoDBiEOG7CK3GC.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 3 hits.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVRKYITLC FWWAFSTSAL VSSQQIPLKD HTSRQYFAVE SNETLSRLEE
60 70 80 90 100
MHPNWKYEHD VRGLPNHYVF SKELLKLGKR SSLEELQGDN NDHILSVHDL
110 120 130 140 150
FPRNDLFKRL PVPAPPMDSS LLPVKEAEDK LSINDPLFER QWHLVNPSFP
160 170 180 190 200
GSDINVLDLW YNNITGAGVV AAIVDDGLDY ENEDLKDNFC AEGSWDFNDN
210 220 230 240 250
TNLPKPRLSD DYHGTRCAGE IAAKKGNNFC GVGVGYNAKI SGIRILSGDI
260 270 280 290 300
TTEDEAASLI YGLDVNDIYS CSWGPADDGR HLQGPSDLVK KALVKGVTEG
310 320 330 340 350
RDSKGAIYVF ASGNGGTRGD NCNYDGYTNS IYSITIGAID HKDLHPPYSE
360 370 380 390 400
GCSAVMAVTY SSGSGEYIHS SDINGRCSNS HGGTSAAAPL AAGVYTLLLE
410 420 430 440 450
ANPNLTWRDV QYLSILSAVG LEKNADGDWR DSAMGKKYSH RYGFGKIDAH
460 470 480 490 500
KLIEMSKTWE NVNAQTWFYL PTLYVSQSTN STEETLESVI TISEKSLQDA
510 520 530 540 550
NFKRIEHVTV TVDIDTEIRG TTTVDLISPA GIISNLGVVR PRDVSSEGFK
560 570 580 590 600
DWTFMSVAHW GENGVGDWKI KVKTTENGHR IDFHSWRLKL FGESIDSSKT
610 620 630 640 650
ETFVFGNDKE EVEPAATEST VSQYSASSTS ISISATSTSS ISIGVETSAI
660 670 680 690 700
PQTTTASTDP DSDPNTPKKL SSPRQAMHYF LTIFLIGATF LVLYFMFFMK
710 720 730 740 750
SRRRIRRSRA ETYEFDIIDT DSEYDSTLDN GTSGITEPEE VEDFDFDLSD
760 770 780 790 800
EDHLASLSSS ENGDAEHTID SVLTNENPFS DPIKQKFPND ANAESASNKL
810
QELQPDVPPS SGRS
Length:814
Mass (Da):90,003
Last modified:January 1, 1990 - v1
Checksum:i5DCEEDADCF439C78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22870 Genomic DNA. Translation: AAA34719.1.
M24201 Genomic DNA. Translation: AAA34718.1.
Z69381 Genomic DNA. Translation: CAA93360.1.
Z71514 Genomic DNA. Translation: CAA96143.1.
BK006947 Genomic DNA. Translation: DAA10321.1.
PIRiA28931. KXBY.
RefSeqiNP_014161.1. NM_001183076.1.

Genome annotation databases

EnsemblFungiiYNL238W; YNL238W; YNL238W.
GeneIDi855483.
KEGGisce:YNL238W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22870 Genomic DNA. Translation: AAA34719.1.
M24201 Genomic DNA. Translation: AAA34718.1.
Z69381 Genomic DNA. Translation: CAA93360.1.
Z71514 Genomic DNA. Translation: CAA96143.1.
BK006947 Genomic DNA. Translation: DAA10321.1.
PIRiA28931. KXBY.
RefSeqiNP_014161.1. NM_001183076.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT5X-ray2.40A/B123-599[»]
1R64X-ray2.20A/B121-601[»]
2ID4X-ray1.90A/B114-613[»]
ProteinModelPortaliP13134.
SMRiP13134. Positions 121-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35601. 156 interactions.
DIPiDIP-6287N.
IntActiP13134. 14 interactions.
MINTiMINT-2787516.

Protein family/group databases

MEROPSiS08.070.

Proteomic databases

MaxQBiP13134.
PeptideAtlasiP13134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL238W; YNL238W; YNL238W.
GeneIDi855483.
KEGGisce:YNL238W.

Organism-specific databases

EuPathDBiFungiDB:YNL238W.
SGDiS000005182. KEX2.

Phylogenomic databases

GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
InParanoidiP13134.
KOiK01341.
OMAiQWHLINP.
OrthoDBiEOG7CK3GC.

Enzyme and pathway databases

BioCyciYEAST:YNL238W-MONOMER.
BRENDAi3.4.21.61. 984.

Miscellaneous databases

EvolutionaryTraceiP13134.
PMAP-CutDBP13134.
PROiP13134.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 3 hits.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, CHARACTERIZATION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  8. "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] [Europe PMC] [Abstract]
    Cited for: POST-TRANSLATIONAL MODIFICATIONS.
  9. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 123-599 IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiKEX2_YEAST
AccessioniPrimary (citable) accession number: P13134
Secondary accession number(s): D6W0V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 8, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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 one 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.