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Reviewed, UniProtKB/Swiss-Prot O13359 (KEX2_CANAL)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kexin
    EC=3.4.21.61
Alternative name(s):
    KEX2 protease
Gene names
Name: KEX2
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length924 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

O-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase S8 family. Furin subfamily.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal
Transmembrane
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – ? PotentialPRO_0000027041
Chain? – 924KexinPRO_0000027042

Regions

Topological domain? – 774Lumenal Potential
Transmembrane775 – 79521 Potential
Topological domain796 – 924129Cytoplasmic Potential
Region190 – 447258Catalytic
Compositional bias675 – 72955Ser/Thr-rich
Compositional bias678 – 6814Poly-Thr
Compositional bias803 – 8086Poly-Arg
Compositional bias894 – 90310Poly-Glu

Sites

Active site2131Charge relay system By similarity
Active site2511Charge relay system By similarity
Active site4221Charge relay system By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Disulfide bond267 ↔ 414 By similarity
Disulfide bond359 ↔ 389 By similarity

Sequences

Sequence LengthMass (Da)Tools
O13359-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 49E5C2093FCCCCE2

FASTA924103,497
        10         20         30         40         50         60 
MLPIKLLIFI LGYLLSPTLQ QYQQIPPRDY ENKNYFLVEL NTTNSQKPLI DFISHYRGHY 

        70         80         90        100        110        120 
NFEHQLSSLD NHYVFSIDKS HPHNSFLGNH NSNEYNLMKR QLGHEQDYDE LISHVESIHL 

       130        140        150        160        170        180 
LPMKKLSKRI PVPIEMEDVV FDNRDDTGSD NHEATDEAHQ KLIEIAKKLD IHDPEFTTQW 

       190        200        210        220        230        240 
HLINLKYPGH DVNVTGLWLE DILGQGIVTA LVDDGVDAES DDIKQNFNSE GSWDFNNKGK 

       250        260        270        280        290        300 
SPLPRLFDDY HGTRCAGEIA AVKNDVCGIG VAWKSQVSGI RILSGPITSS DEAEAMVYGL 

       310        320        330        340        350        360 
DTNDIYSCSW GPTDNGKVLS EPDVIVKKAM IKGIQEGRDK KGAIYVFASG NGGRFGDSCN 

       370        380        390        400        410        420 
FDGYTNSIYS ITVGAIDYKG LHPQYSEACS AVMVVTYSSG SGEHIHTTDI KKKCSATHGG 

       430        440        450        460        470        480 
TSAAAPLASG IYSLILSANP NLTWRDVQYI SVLSATPINE EDGNYQTTAL NRKYSHKYGY 

       490        500        510        520        530        540 
GKTDAYKMVH FAKTWVNVKP QAWYYSDIIE VNQTITTTPE QKAPSKRDSP QKIIHSSVNV 

       550        560        570        580        590        600 
SEKDLKIMNV ERVEHITVKV NIDSTYRGRV GMRIISPTGV ISDLATFRVN DASTRGFQNW 

       610        620        630        640        650        660 
TFMSVAHWGE TGIGEWKVEV FVDDSKGDQV EINFKDWQFR IFGESIDGDK AEVYDITKDY 

       670        680        690        700        710        720 
AAIRRELLEK EKQNSKSTTT TSSTTTATTT SGGEGDQKTT TSAENKESTT KVDNSASITT 

       730        740        750        760        770        780 
SQTASLTSSN EQHQPTESNS DSDSDTDDEN KQEGEEDNDN DNDNGNKKAN SDNTGFYLMS 

       790        800        810        820        830        840 
IAVVGFIAVL LVMKFHKTPG SGRRRRRRDG YEFDIIPGED YSDSDDDEDD SDTRRADDDS 

       850        860        870        880        890        900 
FDLGHRNDQR VVSASQQQRQ YDRQQDEARD RLFDDFNAES LPDYENDMFK IGDEEEEEEE 

       910        920 
EEEGQQSAKA PSNSEGNSGT STKK 

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References

[1]"KEX2 influences Candida albicans proteinase secretion and hyphal formation."
Newport G.R., Agabian N.
J. Biol. Chem. 272:28954-28961(1997) [PubMed: 9360967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: WO-1.

Cross-references

Sequence databases

AF022372 Genomic DNA. Translation: AAB80929.1.

3D structure databases

HSSPHSSP built from PDB template 1OT5 based on UniProtKB P13134.
ModBaseSearch...

Protein family/group databases

MEROPSS08.070.

Enzyme and pathway databases

BRENDA3.4.21.61. 1124.

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. False negative.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKEX2_CANAL
AccessionPrimary (citable) accession number: O13359
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Candida albicans

Candida albicans: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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