Q59KZ1 (APE2_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminopeptidase 2
EC=3.4.11.-

Gene names

Name:	APE2
ORF Names:	CaO19.5197, CaO19.12664

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	924 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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 Ref.2.
Sequence similarities	Belongs to the peptidase M1 family.
Biophysicochemical properties	Kinetic parameters: KM=457 µM for L-alanine-AMC Ref.2 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.

Ontologies

Keywords
Cellular component	Cell wall Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Acetylation Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from direct assay. Source: CGD fungal-type cell wall Inferred from direct assay Ref.2. Source: CGD intracellular Inferred from direct assay Ref.2. Source: CGD
Molecular function	metalloaminopeptidase activity Inferred from direct assay Ref.2. Source: CGD serine-type peptidase activity Inferred from direct assay Ref.2. Source: CGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 57	57	Ref.2
	Chain	58 – 924	867	Aminopeptidase 2		PRO_0000370249
Regions
	Region	327 – 331	5	Substrate binding By similarity
Sites
	Active site	364	1	Proton acceptor By similarity
	Metal binding	363	1	Zinc; catalytic By similarity
	Metal binding	367	1	Zinc; catalytic By similarity
	Metal binding	386	1	Zinc; catalytic By similarity
	Binding site	194	1	Substrate By similarity
	Site	449	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	58	1	N-acetylserine; partial Ref.2
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q59KZ1 [UniParc]. Last modified April 14, 2009. Version 2. Checksum: 232D11B39BA03487	FASTA	924	104,368
	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

References

	« Hide 'large scale' referencesShow '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 / ATCC MYA-2876.
[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 / NBRC 1393.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000272 Genomic DNA. Translation: EAK91154.1. Sequence problems. AACQ01000273 Genomic DNA. Translation: EAK91143.1. Sequence problems.
RefSeq	XP_710405.1. XM_705313.1. XP_710416.1. XM_705324.1.
3D structure databases
HSSP	HSSP built from PDB template 1Z5H based on UniProtKB O93655.
ModBase	Search...
Protein-protein interaction databases
STRING	Q59KZ1.
Protein family/group databases
MEROPS	M01.006.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3647979. 3647990.
KEGG	cal:CaO19.12664. cal:CaO19.5197.
Organism-specific databases
CGD	CAL0002735. APE2.
Family and domain databases
InterPro	IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
KO	K13721.
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APE2_CANAL

Accession

Primary (citable) accession number: Q59KZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	April 14, 2009
Last modified:	January 25, 2012
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program