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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)DescriptionActionsGraphical viewLength
Metal bindingi135Calcium 11
Active sitei175Charge relay system1
Metal bindingi184Calcium 11
Active sitei213Charge relay system1
Metal bindingi227Calcium 11
Metal bindingi277Calcium 21
Metal bindingi320Calcium 21
Metal bindingi350Calcium 21
Active sitei385Charge relay system1

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)DescriptionActionsGraphical viewLength
Topological domaini114 – 678LumenalSequence analysisAdd BLAST565
Transmembranei679 – 699HelicalSequence analysisAdd BLAST21
Topological domaini700 – 814CytoplasmicSequence analysisAdd BLAST115

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000002704320 – 109Add BLAST90
PropeptideiPRO_0000027044110 – 113Removed by dipeptidylpeptidase STE134
ChainiPRO_0000027045114 – 814KexinAdd BLAST701

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Glycosylationi163N-linked (GlcNAc...)1
Disulfide bondi230 ↔ 377
Disulfide bondi322 ↔ 352
Glycosylationi404N-linked (GlcNAc...)Sequence analysis1
Glycosylationi480N-linked (GlcNAc...)1

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

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

Proteomic databases

MaxQBiP13134.
PRIDEiP13134.

Miscellaneous databases

PMAP-CutDBP13134.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1814
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi123 – 130Combined sources8
Helixi138 – 140Combined sources3
Turni142 – 144Combined sources3
Beta strandi147 – 149Combined sources3
Helixi157 – 161Combined sources5
Beta strandi170 – 176Combined sources7
Turni183 – 188Combined sources6
Helixi191 – 193Combined sources3
Turni197 – 200Combined sources4
Turni209 – 212Combined sources4
Helixi213 – 222Combined sources10
Beta strandi225 – 230Combined sources6
Turni234 – 237Combined sources4
Beta strandi238 – 244Combined sources7
Beta strandi246 – 248Combined sources3
Helixi252 – 258Combined sources7
Turni259 – 265Combined sources7
Beta strandi267 – 271Combined sources5
Beta strandi278 – 280Combined sources3
Helixi287 – 303Combined sources17
Beta strandi307 – 311Combined sources5
Helixi316 – 318Combined sources3
Helixi322 – 324Combined sources3
Turni326 – 329Combined sources4
Beta strandi333 – 339Combined sources7
Beta strandi355 – 360Combined sources6
Beta strandi368 – 371Combined sources4
Beta strandi377 – 381Combined sources5
Helixi384 – 401Combined sources18
Helixi407 – 417Combined sources11
Helixi425 – 427Combined sources3
Beta strandi433 – 439Combined sources7
Turni440 – 442Combined sources3
Helixi449 – 456Combined sources8
Beta strandi465 – 469Combined sources5
Beta strandi477 – 479Combined sources3
Beta strandi486 – 492Combined sources7
Helixi494 – 499Combined sources6
Beta strandi502 – 518Combined sources17
Helixi519 – 521Combined sources3
Beta strandi522 – 527Combined sources6
Beta strandi533 – 537Combined sources5
Beta strandi549 – 557Combined sources9
Turni558 – 561Combined sources4
Beta strandi566 – 576Combined sources11
Beta strandi581 – 595Combined sources15
Helixi597 – 599Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP13134.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 453Peptidase S8Add BLAST283

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni462 – 599P-domainAdd BLAST138

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi625 – 642Ser/Thr-richAdd BLAST18

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.
OrthoDBiEOG092C0JIG.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OT5X-ray2.40A/B123-599[»]
1R64X-ray2.20A/B121-601[»]
2ID4X-ray1.90A/B114-613[»]
ProteinModelPortaliP13134.
SMRiP13134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiS08.070.

Proteomic databases

MaxQBiP13134.
PRIDEiP13134.

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.
OrthoDBiEOG092C0JIG.

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...

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: November 2, 2016
This is version 172 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.