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Database: UniProt
Entry: DNPEP_YEAST
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Original site: DNPEP_YEAST 
ID   DNPEP_YEAST             Reviewed;         490 AA.
AC   P38821; D3DL63;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   22-NOV-2017, entry version 133.
DE   RecName: Full=Aspartyl aminopeptidase 4;
DE            EC=3.4.11.21;
GN   Name=APE4; OrderedLocusNames=YHR113W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=11914276; DOI=10.1101/gad.970902;
RA   Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M.,
RA   Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H.,
RA   Miller P., Gerstein M., Roeder G.S., Snyder M.;
RT   "Subcellular localization of the yeast proteome.";
RL   Genes Dev. 16:707-719(2002).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND ENZYME REGULATION.
RX   PubMed=16367759; DOI=10.1111/j.1742-4658.2005.05057.x;
RA   Yokoyama R., Kawasaki H., Hirano H.;
RT   "Identification of yeast aspartyl aminopeptidase gene by purifying and
RT   characterizing its product from yeast cells.";
RL   FEBS J. 273:192-198(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=17651441; DOI=10.1111/j.1742-4658.2007.05959.x;
RA   Sarry J.E., Chen S., Collum R.P., Liang S., Peng M., Lang A.,
RA   Naumann B., Dzierszinski F., Yuan C.X., Hippler M., Rea P.A.;
RT   "Analysis of the vacuolar luminal proteome of Saccharomyces
RT   cerevisiae.";
RL   FEBS J. 274:4287-4305(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ATG19.
RX   PubMed=21343297; DOI=10.1074/jbc.M110.173906;
RA   Yuga M., Gomi K., Klionsky D.J., Shintani T.;
RT   "Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole
RT   by selective autophagy in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 286:13704-13713(2011).
CC   -!- FUNCTION: Aspartyl aminopeptidase that contributes to peptide
CC       degradation both in the cytosol and the vacuole. Cells may respond
CC       to environmental conditions by changing the distributions of the
CC       cytosolic enzyme to the vacuole when cells need more active
CC       vacuolar degradation. {ECO:0000269|PubMed:16367759}.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal aspartate or
CC       glutamate from a peptide, with a preference for aspartate.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ENZYME REGULATION: The metalloproteases inhibitors EDTA and 1.10-
CC       phenanthroline both inhibit the activity, whereas bestatin, an
CC       inhibitor of most aminopeptidases, does not affect enzyme
CC       activity. {ECO:0000269|PubMed:16367759}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=64 uM for angiotensin I {ECO:0000269|PubMed:16367759};
CC       pH dependence:
CC         Optimum pH is 7.5-7.9. {ECO:0000269|PubMed:16367759};
CC   -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six
CC       homodimers. {ECO:0000269|PubMed:16367759}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21343297}.
CC       Vacuole lumen {ECO:0000269|PubMed:17651441,
CC       ECO:0000269|PubMed:21343297}. Note=In growing conditions, a small
CC       portion localizes in the vacuole, but actively transported to the
CC       vacuole under nutrient starvation conditions.
CC       {ECO:0000269|PubMed:21343297}.
CC   -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
DR   EMBL; U00059; AAB68851.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06807.1; -; Genomic_DNA.
DR   PIR; S48955; S48955.
DR   RefSeq; NP_011981.1; NM_001179243.1.
DR   ProteinModelPortal; P38821; -.
DR   SMR; P38821; -.
DR   BioGrid; 36546; 62.
DR   DIP; DIP-2097N; -.
DR   IntAct; P38821; 20.
DR   MINT; MINT-484319; -.
DR   STRING; 4932.YHR113W; -.
DR   MEROPS; M18.002; -.
DR   MaxQB; P38821; -.
DR   PRIDE; P38821; -.
DR   TopDownProteomics; P38821; -.
DR   EnsemblFungi; YHR113W; YHR113W; YHR113W.
DR   GeneID; 856513; -.
DR   KEGG; sce:YHR113W; -.
DR   EuPathDB; FungiDB:YHR113W; -.
DR   SGD; S000001155; APE4.
DR   GeneTree; ENSGT00390000003164; -.
DR   HOGENOM; HOG000253244; -.
DR   InParanoid; P38821; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   BioCyc; YEAST:G3O-31155-MONOMER; -.
DR   BRENDA; 3.4.11.21; 984.
DR   PRO; PR:P38821; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:SGD.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; ISS:SGD.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Vacuole;
KW   Zinc.
FT   CHAIN         1    490       Aspartyl aminopeptidase 4.
FT                                /FTId=PRO_0000173455.
FT   METAL        97     97       Zinc 1. {ECO:0000250}.
FT   METAL       273    273       Zinc 1. {ECO:0000250}.
FT   METAL       273    273       Zinc 2. {ECO:0000250}.
FT   METAL       309    309       Zinc 2. {ECO:0000250}.
FT   METAL       362    362       Zinc 1. {ECO:0000250}.
FT   METAL       456    456       Zinc 2. {ECO:0000250}.
FT   BINDING     173    173       Substrate. {ECO:0000250}.
FT   BINDING     308    308       Substrate. {ECO:0000250}.
FT   BINDING     362    362       Substrate. {ECO:0000250}.
FT   BINDING     365    365       Substrate. {ECO:0000250}.
FT   BINDING     390    390       Substrate. {ECO:0000250}.
FT   BINDING     397    397       Substrate. {ECO:0000250}.
SQ   SEQUENCE   490 AA;  54174 MW;  511CD6EB85C4EA53 CRC64;
     MFRIQLRTMS SKTCKSDYPK EFVSFLNSSH SPYHTVHNIK KHLVSNGFKE LSERDSWAGH
     VAQKGKYFVT RNGSSIIAFA VGGKWEPGNP IAITGAHTDS PALRIKPISK RVSEKYLQVG
     VETYGGAIWH SWFDKDLGVA GRVFVKDAKT GKSIARLVDL NRPLLKIPTL AIHLDRDVNQ
     KFEFNRETQL LPIGGLQEDK TEAKTEKEIN NGEFTSIKTI VQRHHAELLG LIAKELAIDT
     IEDIEDFELI LYDHNASTLG GFNDEFVFSG RLDNLTSCFT SMHGLTLAAD TEIDRESGIR
     LMACFDHEEI GSSSAQGADS NFLPNILERL SILKGDGSDQ TKPLFHSAIL ETSAKSFFLS
     SDVAHAVHPN YANKYESQHK PLLGGGPVIK INANQRYMTN SPGLVLVKRL AEAAKVPLQL
     FVVANDSPCG STIGPILASK TGIRTLDLGN PVLSMHSIRE TGGSADLEFQ IKLFKEFFER
     YTSIESEIVV
//
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