APE3_YEAST
ID APE3_YEAST Reviewed; 537 AA.
AC P37302; D6VQT1; P38154;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Aminopeptidase Y;
DE EC=3.4.11.15;
DE Flags: Precursor;
GN Name=APE3; OrderedLocusNames=YBR286W; ORFNames=YBR2024;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 57-70.
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=8175800; DOI=10.1016/s0021-9258(17)36879-5;
RA Nishizawa M., Yasuhara T., Nakai T., Fujiki Y., Ohashi A.;
RT "Molecular cloning of the aminopeptidase Y gene of Saccharomyces
RT cerevisiae. Sequence analysis and gene disruption of a new
RT aminopeptidase.";
RL J. Biol. Chem. 269:13651-13655(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 57-70, AND CHARACTERIZATION.
RC STRAIN=D273-1B;
RX PubMed=8175799; DOI=10.1016/s0021-9258(17)36878-3;
RA Yasuhara T., Nakai T., Ohashi A.;
RT "Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae.
RT Purification, properties, localization, and processing by protease B.";
RL J. Biol. Chem. 269:13644-13650(1994).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferentially, release of N-terminal lysine.; EC=3.4.11.15;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC -!- MISCELLANEOUS: Present with 4740 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; L31635; AAA19559.1; -; Unassigned_DNA.
DR EMBL; X76053; CAA53649.1; -; Genomic_DNA.
DR EMBL; Z36155; CAA85251.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07401.1; -; Genomic_DNA.
DR PIR; A54134; A54134.
DR RefSeq; NP_009845.2; NM_001178634.1.
DR AlphaFoldDB; P37302; -.
DR SMR; P37302; -.
DR BioGRID; 32980; 75.
DR DIP; DIP-3975N; -.
DR IntAct; P37302; 4.
DR STRING; 4932.YBR286W; -.
DR MEROPS; M28.001; -.
DR iPTMnet; P37302; -.
DR MaxQB; P37302; -.
DR PaxDb; P37302; -.
DR PRIDE; P37302; -.
DR EnsemblFungi; YBR286W_mRNA; YBR286W; YBR286W.
DR GeneID; 852589; -.
DR KEGG; sce:YBR286W; -.
DR SGD; S000000490; APE3.
DR VEuPathDB; FungiDB:YBR286W; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_1_1; -.
DR InParanoid; P37302; -.
DR OMA; YRVNNCV; -.
DR BioCyc; YEAST:YBR286W-MON; -.
DR PRO; PR:P37302; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P37302; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IDA:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
DR InterPro; IPR029514; Ape3.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Vacuole; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..56
FT /evidence="ECO:0000255"
FT /id="PRO_0000026847"
FT CHAIN 57..537
FT /note="Aminopeptidase Y"
FT /id="PRO_0000026848"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 471
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14..15
FT /note="YA -> LR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60137 MW; B34B7819194CF7F3 CRC64;
MHFSLKQLAV AAFYATNLGS AYVIPQFFQE AFQQEEPIEN YLPQLNDDDS SAVAANIPKP
HIPYFMKPHV ESEKLQDKIK VDDLNATAWD LYRLANYSTP DYGHPTRVIG SKGHNKTMEY
ILNVFDDMQD YYDVSLQEFE ALSGKIISFN LSDAETGKSF ANTTAFALSP PVDGFVGKLV
EIPNLGCEEK DYASVVPPRH NEKQIALIER GKCPFGDKSN LAGKFGFTAV VIYDNEPKSK
EGLHGTLGEP TKHTVATVGV PYKVGKKLIA NIALNIDYSL YFAMDSYVEF IKTQNIIADT
KHGDPDNIVA LGAHSDSVEE GPGINDDGSG TISLLNVAKQ LTHFKINNKV RFAWWAAEEE
GLLGSNFYAY NLTKEENSKI RVFMDYDMMA SPNYEYEIYD ANNKENPKGS EELKNLYVDY
YKAHHLNYTL VPFDGRSDYV GFINNGIPAG GIATGAEKNN VNNGKVLDRC YHQLCDDVSN
LSWDAFITNT KLIAHSVATY ADSFEGFPKR ETQKHKEVDI LNAQQPQFKY RADFLII
