ID AMPL_YEAST Reviewed; 514 AA.
AC P14904; D6VXI5; P22060;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 10-MAY-2017, entry version 165.
DE RecName: Full=Vacuolar aminopeptidase 1 {ECO:0000303|PubMed:17329814};
DE EC=3.4.11.22 {ECO:0000269|PubMed:19185714, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682};
DE AltName: Full=Aminopeptidase yscI {ECO:0000303|PubMed:3916861};
DE AltName: Full=Leucine aminopeptidase IV {ECO:0000303|PubMed:6352682};
DE Short=LAPIV {ECO:0000303|PubMed:6352682};
DE AltName: Full=Lysosomal aminopeptidase III {ECO:0000303|PubMed:24493041};
DE AltName: Full=Polypeptidase {ECO:0000303|Ref.6};
DE AltName: Full=Vacuolar aminopeptidase I {ECO:0000303|PubMed:363165};
DE Flags: Precursor;
GN Name=APE1 {ECO:0000303|PubMed:2689224};
GN Synonyms=API {ECO:0000303|PubMed:2651436},
GN LAP4 {ECO:0000303|PubMed:6352682}, YSC1 {ECO:0000303|PubMed:2689224};
GN OrderedLocusNames=YKL103C {ECO:0000312|SGD:S000001586};
GN ORFNames=YKL455;
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 [GENOMIC DNA].
RC STRAIN=II-21;
RX PubMed=2689224; DOI=10.1016/0014-5793(89)81510-8;
RA Cueva R., Garcia-Alvarez N., Suarez-Rendueles P.;
RT "Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the
RT APE1 (LAP4) structural gene.";
RL FEBS Lett. 259:125-129(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-63.
RX PubMed=2651436;
RA Chang Y.-H., Smith J.A.;
RT "Molecular cloning and sequencing of genomic DNA encoding
RT aminopeptidase I from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 264:6979-6983(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
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 [6]
RP IDENTIFICATION, AND COFACTOR.
RA Johnson M.J.;
RT "Isolation and properties of a pure yeast polypeptidase.";
RL J. Biol. Chem. 137:575-586(1941).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24493041; DOI=10.1007/BF00397903;
RA Matile P., Wiemken A., Guyer W.;
RT "A lysosomal aminopeptidase isozyme in differentiating yeast cells and
RT protoplasts.";
RL Planta 96:43-53(1971).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP GLYCOSYLATION, SUBUNIT, AND ENZYME REGULATION.
RX PubMed=5147; DOI=10.1016/0005-2744(76)90338-7;
RA Metz G., Roehm K.H.;
RT "Yeast aminopeptidase I. Chemical composition and catalytic
RT properties.";
RL Biochim. Biophys. Acta 429:933-949(1976).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=363165; DOI=10.1016/0005-2744(78)90253-X;
RA Frey J., Roehm K.H.;
RT "Subcellular localization and levels of aminopeptidases and
RT dipeptidase in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 527:31-41(1978).
RN [10]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=6352682;
RA Trumbly R.J., Bradley G.;
RT "Isolation and characterization of aminopeptidase mutants of
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 156:36-48(1983).
RN [11]
RP CATALYTIC ACTIVITY, COFACTOR, AND ENZYME REGULATION.
RX PubMed=3890752; DOI=10.1016/0003-9861(85)90829-X;
RA Roehm K.H.;
RT "Chloride as allosteric effector of yeast aminopeptidase I.";
RL Arch. Biochem. Biophys. 239:216-225(1985).
RN [12]
RP COFACTOR, AND ENZYME REGULATION.
RX PubMed=3882418; DOI=10.1111/j.1432-1033.1985.tb08698.x;
RA Roehm K.H.;
RT "Metal binding to yeast aminopeptidase I.";
RL Eur. J. Biochem. 146:633-639(1985).
RN [13]
RP NOMENCLATURE.
RX PubMed=3916861; DOI=10.1002/yea.320010203;
RA Achstetter T., Wolf D.H.;
RT "Proteinases, proteolysis and biological control in the yeast
RT Saccharomyces cerevisiae.";
RL Yeast 1:139-157(1985).
RN [14]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1400574; DOI=10.1083/jcb.119.2.287;
RA Klionsky D.J., Cueva R., Yaver D.S.;
RT "Aminopeptidase I of Saccharomyces cerevisiae is localized to the
RT vacuole independent of the secretory pathway.";
RL J. Cell Biol. 119:287-299(1992).
RN [15]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8521804;
RA Segui-Real B., Martinez M., Sandoval I.V.;
RT "Yeast aminopeptidase I is post-translationally sorted from the
RT cytosol to the vacuole by a mechanism mediated by its bipartite N-
RT terminal extension.";
RL EMBO J. 14:5476-5484(1995).
RN [16]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=8601598; DOI=10.1083/jcb.132.6.999;
RA Oda M.N., Scott S.V., Hefner-Gravink A., Caffarelli A.D.,
RA Klionsky D.J.;
RT "Identification of a cytoplasm to vacuole targeting determinant in
RT aminopeptidase I.";
RL J. Cell Biol. 132:999-1010(1996).
RN [17]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=8901576; DOI=10.1073/pnas.93.22.12304;
RA Scott S.V., Hefner-Gravink A., Morano K.A., Noda T., Ohsumi Y.,
RA Klionsky D.J.;
RT "Cytoplasm-to-vacuole targeting and autophagy employ the same
RT machinery to deliver proteins to the yeast vacuole.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12304-12308(1996).
RN [18]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9151668; DOI=10.1083/jcb.137.3.609;
RA Kim J., Scott S.V., Oda M.N., Klionsky D.J.;
RT "Transport of a large oligomeric protein by the cytoplasm to vacuole
RT protein targeting pathway.";
RL J. Cell Biol. 137:609-618(1997).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9214379; DOI=10.1083/jcb.138.1.37;
RA Scott S.V., Baba M., Ohsumi Y., Klionsky D.J.;
RT "Aminopeptidase I is targeted to the vacuole by a nonclassical
RT vesicular mechanism.";
RL J. Cell Biol. 138:37-44(1997).
RN [20]
RP FUNCTION.
RX PubMed=9412464; DOI=10.1083/jcb.139.7.1687;
RA Baba M., Osumi M., Scott S.V., Klionsky D.J., Ohsumi Y.;
RT "Two distinct pathways for targeting proteins from the cytoplasm to
RT the vacuole/lysosome.";
RL J. Cell Biol. 139:1687-1695(1997).
RN [21]
RP SUBUNIT.
RX PubMed=11152450; DOI=10.1074/jbc.M003846200;
RA Andrei-Selmer C., Knuppel A., Satyanarayana C., Heese C., Schu P.V.;
RT "A new class of mutants deficient in dodecamerization of
RT aminopeptidase 1 and vacuolar transport.";
RL J. Biol. Chem. 276:11606-11614(2001).
RN [22]
RP FUNCTION, AND INTERACTION WITH ATG19.
RX PubMed=11382752; DOI=10.1074/jbc.M101438200;
RA Leber R., Silles E., Sandoval I.V., Mazon M.J.;
RT "Yol082p, a novel CVT protein involved in the selective targeting of
RT aminopeptidase I to the yeast vacuole.";
RL J. Biol. Chem. 276:29210-29217(2001).
RN [23]
RP FUNCTION, AND INTERACTION WITH ATG19.
RX PubMed=11430817; DOI=10.1016/S1097-2765(01)00263-5;
RA Scott S.V., Guan J., Hutchins M.U., Kim J., Klionsky D.J.;
RT "Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway.";
RL Mol. Cell 7:1131-1141(2001).
RN [24]
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 [25]
RP FUNCTION.
RX PubMed=15138258; DOI=10.1074/jbc.M404399200;
RA Shintani T., Klionsky D.J.;
RT "Cargo proteins facilitate the formation of transport vesicles in the
RT cytoplasm to vacuole targeting pathway.";
RL J. Biol. Chem. 279:29889-29894(2004).
RN [26]
RP CRYSTALLIZATION.
RX PubMed=17329814; DOI=10.1107/S1744309107005441;
RA Adachi W., Suzuki N.N., Fujioka Y., Suzuki K., Ohsumi Y., Inagaki F.;
RT "Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the
RT major cargo protein of the Cvt pathway.";
RL Acta Crystallogr. F 63:200-203(2007).
RN [27]
RP CATALYTIC ACTIVITY.
RX PubMed=19185714; DOI=10.1016/S0076-6879(08)03206-0;
RA Schu P.;
RT "Aminopeptidase I enzymatic activity.";
RL Methods Enzymol. 451:67-78(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth
RT phosphoproteome analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [29]
RP FUNCTION.
RX PubMed=22123825; DOI=10.1074/jbc.M111.311696;
RA Morales Quinones M., Winston J.T., Stromhaug P.E.;
RT "Propeptide of aminopeptidase 1 protein mediates aggregation and
RT vesicle formation in cytoplasm-to-vacuole targeting pathway.";
RL J. Biol. Chem. 287:10121-10133(2012).
CC -!- FUNCTION: Resident vacuolar enzyme that catalyzes the removal of
CC amino acids from the N-terminus of peptides and proteins. Also
CC acts as the major cargo protein of the cytoplasm-to-vacuole
CC targeting (Cvt) pathway. The precursor form of aminopeptidase 1
CC (prApe1) assembles into dodecamers and the propeptide mediates the
CC aggregation of dodecamers into higher multimers. The multimers are
CC then recognized via the propeptide by their receptor ATG19, and
CC ATG19 further interacts with ATG11, which tethers the APE1-ATG19
CC complex to the pre-autophagosomal structure (PAS). The cargo-
CC receptor complex (also Cvt complex) is selectively enwrapped by a
CC double-membrane structure termed the Cvt vesicle under vegetative
CC growth conditions and by a similar but larger double-membrane
CC structure termed the autophagosome under nitrogen starvation
CC conditions. The Cvt vesicle or the autophagosome fuses with the
CC vacuolar membrane and release its content in the vacuolar lumen.
CC In the vacuole, prApe1 is processed into mature aminopeptidase 1
CC (mApe1). {ECO:0000269|PubMed:11382752,
CC ECO:0000269|PubMed:11430817, ECO:0000269|PubMed:15138258,
CC ECO:0000269|PubMed:22123825, ECO:0000269|PubMed:363165,
CC ECO:0000269|PubMed:8901576, ECO:0000269|PubMed:9214379,
CC ECO:0000269|PubMed:9412464}.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC preferably a neutral or hydrophobic one, from a polypeptide.
CC Aminoacyl-arylamides are poor substrates.
CC {ECO:0000269|PubMed:19185714, ECO:0000269|PubMed:363165,
CC ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147,
CC ECO:0000269|PubMed:6352682}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9ULA0,
CC ECO:0000269|PubMed:3882418, ECO:0000269|PubMed:3890752,
CC ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682,
CC ECO:0000269|Ref.6};
CC Note=Binds 2 Zn(2+) ions per subunit. The average amount of Zn(2+)
CC bound at physiological metal concentrations will be lower than
CC stoichiometric. {ECO:0000250|UniProtKB:Q9ULA0,
CC ECO:0000269|PubMed:3882418, ECO:0000269|PubMed:3890752,
CC ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682,
CC ECO:0000269|Ref.6};
CC -!- ENZYME REGULATION: Strongly and specifically activated by Cl(-)
CC and Br(-), which act as positive allosteric effectors. Inactivated
CC by metal-chelating agents. {ECO:0000269|PubMed:3882418,
CC ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8.5. {ECO:0000269|PubMed:5147};
CC -!- SUBUNIT: Homododecamer. The precursor form of aminopeptidase 1
CC (prApe1) assembles into dodecamers and further aggregates into
CC higher multimers (the Ape1 complex) in the cytoplasm. The Ape1
CC complex is disaggregated in the vacuolar lumen, but mature
CC aminopeptidase 1 (mApe1) retains its dodecameric form. Dodecamer
CC assembly in the cytoplasm is essential for formation of an
CC enzymatically active complex. If cytoplasmic homododecamerization
CC of prApe1 is disturbed in mutants, homododecamers of mApe1 will
CC form in the vacuole, but they are enzymatically inactive.
CC Interacts with ATG19. {ECO:0000269|PubMed:11152450,
CC ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817,
CC ECO:0000269|PubMed:5147, ECO:0000269|PubMed:9151668}.
CC -!- INTERACTION:
CC Self; NbExp=4; IntAct=EBI-2571, EBI-2571;
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:24493041,
CC ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8601598}.
CC Note=Transported to the vacuole by the cytosol-to-vacuole
CC targeting (Cvt) pathway. {ECO:0000269|PubMed:9151668,
CC ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}.
CC -!- PTM: Synthesized in a precursor form (prApe1) that has an amino-
CC terminal propeptide. The N-terminal extension of the 61 kDa
CC precursor is proteolytically processed in two sequential steps.
CC The first step involves proteinase A (PrA/PEP4) and produces a 55
CC kDa unstable intermediate (iAPI). The second step involves
CC proteinase B (PrB/PRB1) and converts iAPI into the 50 kDa stable,
CC mature enzyme (mApe1). {ECO:0000269|PubMed:8521804}.
CC -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC -!- CAUTION: It is unsure whether this protein is glycosylated or not.
CC PubMed:5147 has shown that a preparation of aminopeptidase 1
CC contains about 12% of conjugated carbohydrate, while
CC PubMed:1400574 could not identify any glycosylation, which is in
CC agreement with the fact that aminopeptidase 1 does not transit
CC through the secretory pathway. {ECO:0000305|PubMed:1400574,
CC ECO:0000305|PubMed:5147}.
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DR EMBL; Y07522; CAA68815.1; -; Genomic_DNA.
DR EMBL; M25548; AAA34738.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50454.1; -; Genomic_DNA.
DR EMBL; Z28103; CAA81943.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09055.1; -; Genomic_DNA.
DR PIR; A33879; A33879.
DR RefSeq; NP_012819.1; NM_001179669.1.
DR PDB; 4R8F; X-ray; 2.50 A; A/B/C/D=46-514.
DR PDB; 5JGE; X-ray; 1.91 A; C/F=1-20.
DR PDB; 5JGF; X-ray; 1.83 A; A/B/C/D=46-514.
DR PDB; 5JH9; X-ray; 2.10 A; A/B/C/D=1-514.
DR PDB; 5JHC; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-22.
DR PDB; 5JM9; EM; 24.00 A; A=1-514.
DR PDBsum; 4R8F; -.
DR PDBsum; 5JGE; -.
DR PDBsum; 5JGF; -.
DR PDBsum; 5JH9; -.
DR PDBsum; 5JHC; -.
DR PDBsum; 5JM9; -.
DR ProteinModelPortal; P14904; -.
DR SMR; P14904; -.
DR BioGrid; 34031; 64.
DR DIP; DIP-1409N; -.
DR IntAct; P14904; 31.
DR MINT; MINT-387783; -.
DR BindingDB; P14904; -.
DR ChEMBL; CHEMBL1741175; -.
DR MEROPS; M18.001; -.
DR iPTMnet; P14904; -.
DR MaxQB; P14904; -.
DR PRIDE; P14904; -.
DR EnsemblFungi; YKL103C; YKL103C; YKL103C.
DR GeneID; 853758; -.
DR KEGG; sce:YKL103C; -.
DR EuPathDB; FungiDB:YKL103C; -.
DR SGD; S000001586; APE1.
DR HOGENOM; HOG000253244; -.
DR InParanoid; P14904; -.
DR KO; K01268; -.
DR OMA; KETQAVP; -.
DR OrthoDB; EOG092C3JCE; -.
DR BioCyc; YEAST:YKL103C-MONOMER; -.
DR BRENDA; 3.4.11.22; 984.
DR PMAP-CutDB; P14904; -.
DR PRO; PR:P14904; -.
DR Proteomes; UP000002311; Chromosome XI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; ISS:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd05639; M18; 1.
DR InterPro; IPR033818; Aminopeptidase_I.
DR InterPro; IPR001948; Peptidase_M18.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Complete proteome;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Protein transport;
KW Reference proteome; Transport; Vacuole; Zinc; Zymogen.
FT PROPEP 1 45 Required for vacuolar localization.
FT Mediates aggregation and vesicle
FT formation in Cvt pathway.
FT {ECO:0000269|PubMed:2651436,
FT ECO:0000269|PubMed:8521804,
FT ECO:0000269|PubMed:8601598}.
FT /FTId=PRO_0000026806.
FT CHAIN 46 514 Vacuolar aminopeptidase 1.
FT /FTId=PRO_0000026807.
FT METAL 132 132 Zinc 1. {ECO:0000250|UniProtKB:Q9ULA0}.
FT METAL 303 303 Zinc 1. {ECO:0000250|UniProtKB:Q9ULA0}.
FT METAL 303 303 Zinc 2. {ECO:0000250|UniProtKB:Q9ULA0}.
FT METAL 340 340 Zinc 2. {ECO:0000250|UniProtKB:Q9ULA0}.
FT METAL 385 385 Zinc 1. {ECO:0000250|UniProtKB:Q9ULA0}.
FT METAL 479 479 Zinc 2. {ECO:0000250|UniProtKB:Q9ULA0}.
FT BINDING 210 210 Substrate.
FT {ECO:0000250|UniProtKB:Q9ULA0}.
FT BINDING 339 339 Substrate.
FT {ECO:0000250|UniProtKB:Q9ULA0}.
FT BINDING 385 385 Substrate.
FT {ECO:0000250|UniProtKB:Q9ULA0}.
FT BINDING 388 388 Substrate.
FT {ECO:0000250|UniProtKB:Q9ULA0}.
FT SITE 45 46 Cleavage; by protease B (PrB/PRB1).
FT {ECO:0000269|PubMed:1400574}.
FT MOD_RES 356 356 Phosphoserine.
FT {ECO:0000244|PubMed:18407956}.
FT CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT CONFLICT 233 233 T -> S (in Ref. 1; CAA68815).
FT {ECO:0000305}.
FT CONFLICT 323 323 N -> D (in Ref. 1; CAA68815).
FT {ECO:0000305}.
FT CONFLICT 328 328 D -> E (in Ref. 1; CAA68815).
FT {ECO:0000305}.
FT CONFLICT 369 369 P -> A (in Ref. 1; CAA68815).
FT {ECO:0000305}.
FT HELIX 1 17 {ECO:0000244|PDB:5JGE}.
FT HELIX 34 43 {ECO:0000244|PDB:5JH9}.
FT STRAND 45 47 {ECO:0000244|PDB:5JH9}.
FT HELIX 48 62 {ECO:0000244|PDB:5JGF}.
FT HELIX 66 79 {ECO:0000244|PDB:5JGF}.
FT TURN 92 94 {ECO:0000244|PDB:5JGF}.
FT STRAND 100 106 {ECO:0000244|PDB:5JGF}.
FT TURN 107 109 {ECO:0000244|PDB:5JGF}.
FT STRAND 110 116 {ECO:0000244|PDB:5JGF}.
FT HELIX 122 124 {ECO:0000244|PDB:5JGF}.
FT STRAND 127 132 {ECO:0000244|PDB:5JGF}.
FT STRAND 136 140 {ECO:0000244|PDB:5JGF}.
FT STRAND 152 154 {ECO:0000244|PDB:5JGF}.
FT STRAND 157 162 {ECO:0000244|PDB:5JGF}.
FT HELIX 166 168 {ECO:0000244|PDB:5JGF}.
FT STRAND 173 181 {ECO:0000244|PDB:5JGF}.
FT STRAND 190 195 {ECO:0000244|PDB:5JGF}.
FT HELIX 209 211 {ECO:0000244|PDB:5JGF}.
FT HELIX 213 215 {ECO:0000244|PDB:5JGF}.
FT TURN 221 224 {ECO:0000244|PDB:5JGF}.
FT STRAND 228 230 {ECO:0000244|PDB:5JGF}.
FT HELIX 246 248 {ECO:0000244|PDB:5JGF}.
FT TURN 250 254 {ECO:0000244|PDB:4R8F}.
FT HELIX 257 267 {ECO:0000244|PDB:5JGF}.
FT HELIX 271 273 {ECO:0000244|PDB:5JGF}.
FT STRAND 274 283 {ECO:0000244|PDB:5JGF}.
FT STRAND 288 291 {ECO:0000244|PDB:5JGF}.
FT STRAND 296 300 {ECO:0000244|PDB:5JGF}.
FT HELIX 302 319 {ECO:0000244|PDB:5JGF}.
FT TURN 324 326 {ECO:0000244|PDB:5JGF}.
FT STRAND 330 337 {ECO:0000244|PDB:5JGF}.
FT HELIX 339 341 {ECO:0000244|PDB:5JGF}.
FT HELIX 349 351 {ECO:0000244|PDB:5JGF}.
FT HELIX 353 365 {ECO:0000244|PDB:5JGF}.
FT HELIX 372 377 {ECO:0000244|PDB:5JGF}.
FT STRAND 380 384 {ECO:0000244|PDB:5JGF}.
FT HELIX 395 397 {ECO:0000244|PDB:5JGF}.
FT STRAND 411 413 {ECO:0000244|PDB:5JGF}.
FT STRAND 418 420 {ECO:0000244|PDB:5JGF}.
FT HELIX 424 437 {ECO:0000244|PDB:5JGF}.
FT STRAND 442 444 {ECO:0000244|PDB:5JGF}.
FT HELIX 457 464 {ECO:0000244|PDB:5JGF}.
FT STRAND 467 472 {ECO:0000244|PDB:5JGF}.
FT STRAND 474 477 {ECO:0000244|PDB:5JGF}.
FT STRAND 480 486 {ECO:0000244|PDB:5JGF}.
FT HELIX 489 508 {ECO:0000244|PDB:5JGF}.
FT HELIX 509 511 {ECO:0000244|PDB:5JH9}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 59 501 ipfam:Peptidase_M18 [T]
SQ SEQUENCE 514 AA; 57093 MW; 702A8C88A2124C24 CRC64;
MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE DIAQEFIDFI
YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG KFYTIRNGTN LSAFILGKNW
RAEKGVGVIG SHVDALTVKL KPVSFKDTAE GYGRIAVAPY GGTLNELWLD RDLGIGGRLL
YKKKGTNEIK SALVDSTPLP VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPTPDEEGNE
PPTDDEKKSP LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP
RLDDRLCSFA AMIALICYAK DVNTEESDLF STVTLYDNEE IGSLTRQGAK GGLLESVVER
SSSAFTKKPV DLHTVWANSI ILSADVNHLY NPNFPEVYLK NHFPVPNVGI TLSLDPNGHM
ATDVVGTALV EELARRNGDK VQYFQIKNNS RSGGTIGPSL ASQTGARTID LGIAQLSMHS
IRAATGSKDV GLGVKFFNGF FKHWRSVYDE FGEL
//
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