Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q59KZ1 (APE2_CANAL)

Last modified November 24, 2009. Version 32. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Aminopeptidase 2
    EC=3.4.11.-
Gene names
Name: APE2
ORF Names: CaO19.5197, CaO19.12664
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Hide | Top

Protein attributes

Sequence length924 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Metalloprotease that specifically hydrolyzes peptides with N-terminal alanine, arginine and leucine residues. Ref.2

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inactivated by metal-chelating agents phenanthroline and EDTA. Inhibited by bestatin, an aminopeptidase inhibitor. Not inhibited by pepstatin A and PMSF, inhibitors of aspartic and the serine proteases, respectively. Not inhibited by carboxypeptidase inhibitor.

Subcellular location

Secreted › cell wall.

Sequence similarities

Belongs to the peptidase M1 family.

Biophysicochemical properties

Kinetic parameters:

KM=457 µM for L-alanine-AMC

KM=46.9 µM for L-arginine-AMC

KM=82 µM for L-leucine-AMC

Vmax=16.9 µmol/min/mg enzyme for L-alanine-AMC

Vmax=25.4 µmol/min/mg enzyme for L-arginine-AMC

Vmax=18.4 µmol/min/mg enzyme for L-leucine-AMC

pH dependence:

Optimum pH is 7.2.

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Sequence caution

The sequence EAK91143.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAK91154.1 differs from that shown. Reason: Erroneous gene model prediction.

Hide | Top

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMAcetylation
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757 Ref.2
Chain58 – 924867Aminopeptidase 2
PRO_0000370249

Sites

Active site3641 By similarity
Active site4491Proton donor Potential
Metal binding3631Zinc; catalytic By similarity
Metal binding3671Zinc; catalytic By similarity
Metal binding3861Zinc; catalytic By similarity

Amino acid modifications

Modified residue581N-acetylserine; partial Ref.2
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q59KZ1-1 [UniParc].

Last modified April 14, 2009. Version 2.
Checksum: 232D11B39BA03487

FASTA924104,368
        10         20         30         40         50         60 
MASNNTSQRS GFSSFFCRLK TYFCNHFLCL FVLSFFPLSF RRLCLLCHLC EKSNLWLSSD 

        70         80         90        100        110        120 
NSASVVNQER EVLPTNVKPL HYDLTIEPIF DNFTFKGEET IDFQVNEKTN FITLNSLEIE 

       130        140        150        160        170        180 
VQEAKIDGKS VTDISFDAGK QTVTFKFDDD LSTGSIAKLY IKFTGELNDK MAGFYRASYQ 

       190        200        210        220        230        240 
EDGKTKYMAT TQMEPTDCRR AFPSYDEPAA KSKFTISLIA DKELVCLSNS SEKETVSLDG 

       250        260        270        280        290        300 
NKKKVTFQTT PLMSTYLVAF IVGDLRYISN DNYRVPIRVY STPGTEHLGE YSANIAAQTL 

       310        320        330        340        350        360 
KFFDQQFGID YPYDKLDMVA VPSFSAGAME NCGLVTFRTV DLLIDADNAN VNTKQRVTEV 

       370        380        390        400        410        420 
VMHELAHQWF GDLVTMEFWD GLWLNEGFAT WMSWYACNSL YPDWKVWESY VSDSLQHALT 

       430        440        450        460        470        480 
LDALRASHPI EVPVKRADEI NQIFDAISYS KGSSLLRMIS KWLGEDVFVK GVSNYLKKHK 

       490        500        510        520        530        540 
WGNTKTSDLW EALSEASGED VVKVMDIWTK NIGFPIVKVE EIGNGEIKVT QNRFLATGDV 

       550        560        570        580        590        600 
KESEDKTLYP VFLGLKTSEG VDESSVLETR SKTIKLPTSD DFFKINGDQS GIYRTAYEPA 

       610        620        630        640        650        660 
RWTKLGKAGV EGKLSVEDRV GLVADAGSLA SSGFIKTSSL LDLVKSWSKE SNYVVWNEIL 

       670        680        690        700        710        720 
TRIGSIKAAL MFEDEATKKA LEIFTRDLIS EKLKETGWEF SADDSFADQQ LKSSLFASAA 

       730        740        750        760        770        780 
NAEDPEAVAF AKEAFAKFIA GDKKAIHPNL RASIFNTNAK YGDEKTFDEL YNIYRNPSSV 

       790        800        810        820        830        840 
EEKIAALRSF GRFTKPEILD KVTGLLLQTD IVKQQDIYIP MQGLRAHKLG VEKLWTWLSE 

       850        860        870        880        890        900 
NWDQIYILLP PGLSMLGSVV TLGTSGFTKE EQKKKVEEFF AQKDNKGYDQ SLAQSLDIIT 

       910        920 
AKSKWTDRDA KSIYEWLEAN EYTK

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.
[2]"Identification and characterization of CaApe2 -- a neutral arginine/alanine/leucine-specific metallo-aminopeptidase from Candida albicans."
Klinke T., Rump A., Poenisch R., Schellenberger W., Mueller E.-C., Otto A., Klimm W., Kriegel T.M.
FEMS Yeast Res. 8:858-869(2008) [PubMed: 18637841] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-70, PARTIAL ACETYLATION AT SER-58, GENE MODEL REVISION, MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 2091 / CBS 2730 / DSM 1665 / CIP 1180.79 / IFO 1393.

Hide | Top

Cross-references

Sequence databases

AACQ01000272 Genomic DNA. Translation: EAK91154.1. Sequence problems.
AACQ01000273 Genomic DNA. Translation: EAK91143.1. Sequence problems.
RefSeqXP_710405.1.
XP_710416.1.

3D structure databases

HSSPHSSP built from PDB template 1Z5H based on UniProtKB O93655.
ModBaseSearch...

Protein family/group databases

MEROPSM01.006.

Genome annotation databases

GeneID3647979.
3647990.
KEGGcal:CaO19.12664.
cal:CaO19.5197.

Organism-specific databases

CGDCAL0002735. APE2.

Phylogenomic databases

OrthoDBEOG902Z86

Family and domain databases

InterProIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. Peptidase_M1. 1 hit.
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameAPE2_CANAL
AccessionPrimary (citable) accession number: Q59KZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 14, 2009
Last modified: November 24, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

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