APE2_CANAL
ID APE2_CANAL Reviewed; 924 AA.
AC Q59KZ1; A0A1D8PDA3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Aminopeptidase 2;
DE EC=3.4.11.-;
DE Flags: Precursor;
GN Name=APE2; OrderedLocusNames=CAALFM_C104400CA;
GN ORFNames=CaO19.12664, CaO19.5197;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 58-70, ACETYLATION AT SER-58, GENE MODEL REVISION,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 2091 / CBS 2730 / DSM 1665 / CIP 1180.79 / NBRC 1393;
RX PubMed=18637841; DOI=10.1111/j.1567-1364.2008.00411.x;
RA Klinke T., Rump A., Poenisch R., Schellenberger W., Mueller E.-C., Otto A.,
RA Klimm W., Kriegel T.M.;
RT "Identification and characterization of CaApe2 -- a neutral
RT arginine/alanine/leucine-specific metallo-aminopeptidase from Candida
RT albicans.";
RL FEMS Yeast Res. 8:858-869(2008).
CC -!- FUNCTION: Metalloprotease that specifically hydrolyzes peptides with N-
CC terminal alanine, arginine and leucine residues.
CC {ECO:0000269|PubMed:18637841}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inactivated by metal-chelating agents
CC phenanthroline and EDTA. Inhibited by bestatin, an aminopeptidase
CC inhibitor. Not inhibited by pepstatin A and PMSF, inhibitors of
CC aspartic and the serine proteases, respectively. Not inhibited by
CC carboxypeptidase inhibitor.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=457 uM for L-alanine-AMC {ECO:0000269|PubMed:18637841};
CC KM=46.9 uM for L-arginine-AMC {ECO:0000269|PubMed:18637841};
CC KM=82 uM for L-leucine-AMC {ECO:0000269|PubMed:18637841};
CC Vmax=16.9 umol/min/mg enzyme for L-alanine-AMC
CC {ECO:0000269|PubMed:18637841};
CC Vmax=25.4 umol/min/mg enzyme for L-arginine-AMC
CC {ECO:0000269|PubMed:18637841};
CC Vmax=18.4 umol/min/mg enzyme for L-leucine-AMC
CC {ECO:0000269|PubMed:18637841};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:18637841};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:18637841};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:18637841}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26114.1; -; Genomic_DNA.
DR RefSeq; XP_019330640.1; XM_019475095.1.
DR AlphaFoldDB; Q59KZ1; -.
DR SMR; Q59KZ1; -.
DR STRING; 237561.Q59KZ1; -.
DR MEROPS; M01.006; -.
DR iPTMnet; Q59KZ1; -.
DR PRIDE; Q59KZ1; -.
DR GeneID; 3647990; -.
DR KEGG; cal:CAALFM_C104400CA; -.
DR CGD; CAL0000186164; APE2.
DR VEuPathDB; FungiDB:C1_04400C_A; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q59KZ1; -.
DR OMA; MMEYVAI; -.
DR OrthoDB; 110058at2759; -.
DR PRO; PR:Q59KZ1; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0005771; C:multivesicular body; IEA:EnsemblFungi.
DR GO; GO:0061957; C:NVT complex; IEA:EnsemblFungi.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IEA:EnsemblFungi.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cell wall; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..45
FT /evidence="ECO:0000303|PubMed:18637841"
FT PROPEP 46..57
FT /evidence="ECO:0000303|PubMed:18637841"
FT /id="PRO_0000434587"
FT CHAIN 58..924
FT /note="Aminopeptidase 2"
FT /id="PRO_0000370249"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327..331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 449
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="N-acetylserine; partial"
FT /evidence="ECO:0000269|PubMed:18637841"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="K -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 924 AA; 104382 MW; 43EE4E58B565BCE8 CRC64;
MASNNTSQRS GFSSFFCRLK TYFCNHFLCL FVLSFFPLSF RRLCLLCHLC EKSNLWLSSD
NSASVVKQER EVLPTNVKPL HYDLTIEPIF DNFTFKGEET IDFQVNEKTN FITLNSLEIE
VQEAKIDGKS VTDISFDAGK QTVTFKFDDD LSTGSIAKLY IKFTGELNDK MAGFYRASYQ
EDGKTKYMAT TQMEPTDCRR AFPSYDEPAA KSKFTISLIA DKELVCLSNS SEKETVSLDG
NKKKVTFQTT PLMSTYLVAF IVGDLRYISN DNYRVPIRVY STPGTEHLGE YSANIAAQTL
KFFDQQFGID YPYDKLDMVA VPSFSAGAME NCGLVTFRTV DLLIDADNAN VNTKQRVTEV
VMHELAHQWF GDLVTMEFWD GLWLNEGFAT WMSWYACNSL YPDWKVWESY VSDSLQHALT
LDALRASHPI EVPVKRADEI NQIFDAISYS KGSSLLRMIS KWLGEDVFVK GVSNYLKKHK
WGNTKTSDLW EALSEASGED VVKVMDIWTK NIGFPIVKVE EIGNGEIKVT QNRFLATGDV
KESEDKTLYP VFLGLKTSEG VDESSVLETR SKTIKLPTSD DFFKINGDQS GIYRTAYEPA
RWTKLGKAGV EGKLSVEDRV GLVADAGSLA SSGFIKTSSL LDLVKSWSKE SNYVVWNEIL
TRIGSIKAAL MFEDEATKKA LEIFTRDLIS EKLKETGWEF SADDSFADQQ LKSSLFASAA
NAEDPEAVAF AKEAFAKFIA GDKKAIHPNL RASIFNTNAK YGDEKTFDEL YNIYRNPSSV
EEKIAALRSF GRFTKPEILD KVTGLLLQTD IVKQQDIYIP MQGLRAHKLG VEKLWTWLSE
NWDQIYILLP PGLSMLGSVV TLGTSGFTKE EQKKKVEEFF AQKDNKGYDQ SLAQSLDIIT
AKSKWTDRDA KSIYEWLEAN EYTK
