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Protein

Kexin

Gene

KEX2

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei213Charge relay systemBy similarity1
Active sitei251Charge relay systemBy similarity1
Active sitei422Charge relay systemBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
LigandCalcium

Names & Taxonomyi

Protein namesi
Recommended name:
Kexin (EC:3.4.21.61)
Alternative name(s):
KEX2 protease
Gene namesi
Name:KEX2
ORF Names:CAWG_00530
OrganismiCandida albicans (strain WO-1) (Yeast)
Taxonomic identifieri294748 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000001429 Componenti: Chromosome 1, Supercontig 1.1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini? – 774LumenalSequence analysis
Transmembranei775 – 795HelicalSequence analysisAdd BLAST21
Topological domaini796 – 924CytoplasmicSequence analysisAdd BLAST129

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000027042? – 938Kexin
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002704121 – ?Sequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi193N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi267 ↔ 414By similarity
Disulfide bondi359 ↔ 389By similarity
Glycosylationi441N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi512N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi539N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi599N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliO13359.
SMRiO13359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini210 – 489Peptidase S8Add BLAST280
Domaini498 – 647P/Homo BPROSITE-ProRule annotationAdd BLAST150

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi678 – 727Thr-richAdd BLAST50
Compositional biasi809 – 875Asp-richAdd BLAST67

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000192536.
OMAiEACSAVM.
OrthoDBiEOG092C0JIG.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like_sf.
IPR034182. Kexin/furin.
IPR000209. Peptidase_S8/S53_dom.
IPR036852. Peptidase_S8/S53_dom_sf.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
PfamiView protein in Pfam
PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PRINTSiPR00723. SUBTILISIN.
PROSITEiView protein in PROSITE
PS51829. P_HOMO_B. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O13359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPIKLLIFI LGYLLSPTLQ QYQQIPPRDY ENKNYFLVEL NTTNSQKPLI
60 70 80 90 100
DFISHYRGHY NFEHQLSSLD NHYVFSIDKS HPHNSFLGNH NSNEYNLMKR
110 120 130 140 150
QLGHEQDYDE LISHVESIHL LPMKKLSKRI PVPIEMEDVV FDNRDDTGSD
160 170 180 190 200
NHEATDEAHQ KLIEIAKKLD IHDPEFTTQW HLINLKYPGH DVNVTGLWLE
210 220 230 240 250
NILGQGIVTA LVDDGVDAES DDIKQNFNSE GSWDFNNKGK SPLPRLFDDY
260 270 280 290 300
HGTRCAGEIA AVKNDVCGIG VAWKSQVSGI RILSGPITSS DEAEAMVYGL
310 320 330 340 350
DTNDIYSCSW GPTDNGKVLS EPDVIVKKAM IKGIQEGRDK KGAIYVFASG
360 370 380 390 400
NGGRFGDSCN FDGYTNSIYS ITVGAIDYKG LHPQYSEACS AVMVVTYSSG
410 420 430 440 450
SGEHIHTTDI KKKCSATHGG TSAAAPLASG IYSLILSANP NLTWRDVQYI
460 470 480 490 500
SVLSATPINE EDGNYQTTAL NRKYSHKYGY GKTDAYKMVH FAKTWVNVKP
510 520 530 540 550
QAWYYSDIIE VNQTITTTPE QKAPSKRDSP QKIIHSSVNV SEKDLKIMNV
560 570 580 590 600
ERVEHITVKV NIDSTYRGRV GMRIISPTGV ISDLATFRVN DASTRGFQNW
610 620 630 640 650
TFMSVAHWGE TGIGEWKVEV FVDDSKGDQV EINFKDWQFR IFGESIDGDK
660 670 680 690 700
AEVYDITKDY AAIRRELLEK EKQNSKSTTT TSSTTTATTT SGGEGDQKTT
710 720 730 740 750
TSAENKESTT KVDNSASITT SQTASLTSSN EQHQPTESNS DSDSDTDDEN
760 770 780 790 800
KQEGEEDNDN DNDNGNKKAN SDNTGFYLMS IAVVGFIAVL LVMKFHKTPG
810 820 830 840 850
SGRRRRRRDG YEFDIIPGED YSDSDDDEDD FDTRRADDDS FDLGHRNDQR
860 870 880 890 900
VVSASQQQRQ YDRQQDETRD RLFDDFNAES LPDYENDMFK IGDEEEEEEE
910 920 930
GQQSAKAPSN SEGNSGTSTK KYKDNEADED HKDVVGTQ
Length:938
Mass (Da):105,144
Last modified:October 19, 2011 - v2
Checksum:i7E72BE8AD9FAA9FF
GO

Sequence cautioni

The sequence AAB80929 differs from that shown. Reason: Frameshift at position 922.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201N → D in AAB80929 (PubMed:9360967).Curated1
Sequence conflicti831F → S in AAB80929 (PubMed:9360967).Curated1
Sequence conflicti868T → A in AAB80929 (PubMed:9360967).Curated1
Sequence conflicti899E → EEEE in AAB80929 (PubMed:9360967).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022372 Genomic DNA. Translation: AAB80929.1. Frameshift.
CH672346 Genomic DNA. Translation: EEQ42323.1.

Genome annotation databases

EnsemblFungiiEEQ42323; EEQ42323; CAWG_00530.

Entry informationi

Entry nameiKEX2_CANAW
AccessioniPrimary (citable) accession number: O13359
Secondary accession number(s): C4YDD7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 19, 2011
Last modified: November 22, 2017
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families