AMPL_YEAST
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 03-AUG-2022, entry version 200.
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}; ORFNames=YKL455;
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].
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 APE1
RT (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; DOI=10.1016/s0021-9258(18)83527-x;
RA Chang Y.-H., Smith J.A.;
RT "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I
RT 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., Bossier P.,
RA 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., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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, GLYCOSYLATION,
RP SUBUNIT, AND ACTIVITY 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 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 dipeptidase in
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 527:31-41(1978).
RN [10]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=6352682; DOI=10.1128/jb.156.1.36-48.1983;
RA Trumbly R.J., Bradley G.;
RT "Isolation and characterization of aminopeptidase mutants of Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 156:36-48(1983).
RN [11]
RP CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY 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 ACTIVITY 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 Saccharomyces
RT 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 vacuole
RT independent of the secretory pathway.";
RL J. Cell Biol. 119:287-299(1992).
RN [15]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8521804; DOI=10.1002/j.1460-2075.1995.tb00234.x;
RA Segui-Real B., Martinez M., Sandoval I.V.;
RT "Yeast aminopeptidase I is post-translationally sorted from the cytosol to
RT the vacuole by a mechanism mediated by its bipartite N-terminal
RT 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., 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 machinery to
RT 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 vesicular
RT 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 the
RT 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 aminopeptidase 1
RT 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., Dephoure N.,
RA 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 major
RT 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 BY
RP 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 phosphoproteome
RT 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 vesicle
RT 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 amino
CC acids from the N-terminus of peptides and proteins. Also acts as the
CC major cargo protein of the cytoplasm-to-vacuole targeting (Cvt)
CC pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into
CC dodecamers and the propeptide mediates the aggregation of dodecamers
CC into higher multimers. The multimers are then recognized via the
CC propeptide by their receptor ATG19, and ATG19 further interacts with
CC ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal
CC structure (PAS). The cargo-receptor complex (also Cvt complex) is
CC selectively enwrapped by a double-membrane structure termed the Cvt
CC vesicle under vegetative growth conditions and by a similar but larger
CC double-membrane structure termed the autophagosome under nitrogen
CC starvation conditions. The Cvt vesicle or the autophagosome fuses with
CC the vacuolar membrane and release its content in the vacuolar lumen. In
CC the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).
CC {ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817,
CC ECO:0000269|PubMed:15138258, ECO:0000269|PubMed:22123825,
CC ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8901576,
CC ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferably a neutral or
CC hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor
CC substrates.; EC=3.4.11.22; Evidence={ECO:0000269|PubMed:19185714,
CC ECO:0000269|PubMed:363165, ECO:0000269|PubMed:3890752,
CC ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9ULA0, ECO:0000269|PubMed:3882418,
CC ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147,
CC ECO:0000269|PubMed:6352682, 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 -!- ACTIVITY REGULATION: Strongly and specifically activated by Cl(-) and
CC Br(-), which act as positive allosteric effectors. Inactivated by
CC 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 (prApe1)
CC assembles into dodecamers and further aggregates into higher multimers
CC (the Ape1 complex) in the cytoplasm. The Ape1 complex is disaggregated
CC in the vacuolar lumen, but mature aminopeptidase 1 (mApe1) retains its
CC dodecameric form. Dodecamer assembly in the cytoplasm is essential for
CC formation of an enzymatically active complex. If cytoplasmic
CC homododecamerization of prApe1 is disturbed in mutants, homododecamers
CC of mApe1 will 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 P14904; P14904: APE1; NbExp=3; IntAct=EBI-2571, EBI-2571;
CC P14904; P35193: ATG19; NbExp=3; IntAct=EBI-2571, EBI-29291;
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 targeting
CC (Cvt) pathway. {ECO:0000269|PubMed:9151668, ECO:0000269|PubMed:9214379,
CC 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 precursor
CC is proteolytically processed in two sequential steps. The first step
CC involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable
CC intermediate (iAPI). The second step involves proteinase B (PrB/PRB1)
CC and converts iAPI into the 50 kDa stable, mature enzyme (mApe1).
CC {ECO:0000269|PubMed:8521804}.
CC -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium.
CC {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 contains
CC about 12% of conjugated carbohydrate, while PubMed:1400574 could not
CC identify any glycosylation, which is in agreement with the fact that
CC aminopeptidase 1 does not transit through the secretory pathway.
CC {ECO:0000305|PubMed:1400574, 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 AlphaFoldDB; P14904; -.
DR SMR; P14904; -.
DR BioGRID; 34031; 70.
DR DIP; DIP-1409N; -.
DR IntAct; P14904; 56.
DR MINT; P14904; -.
DR STRING; 4932.YKL103C; -.
DR BindingDB; P14904; -.
DR ChEMBL; CHEMBL1741175; -.
DR MEROPS; M18.001; -.
DR CarbonylDB; P14904; -.
DR iPTMnet; P14904; -.
DR MaxQB; P14904; -.
DR PaxDb; P14904; -.
DR PRIDE; P14904; -.
DR EnsemblFungi; YKL103C_mRNA; YKL103C; YKL103C.
DR GeneID; 853758; -.
DR KEGG; sce:YKL103C; -.
DR SGD; S000001586; APE1.
DR VEuPathDB; FungiDB:YKL103C; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_3_0_1; -.
DR InParanoid; P14904; -.
DR OMA; WPIAKIP; -.
DR BioCyc; YEAST:YKL103C-MON; -.
DR BRENDA; 3.4.11.22; 984.
DR PRO; PR:P14904; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P14904; protein.
DR GO; GO:0034270; C:Cvt complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Protein transport; Reference proteome; Transport; Vacuole; Zinc; Zymogen.
FT PROPEP 1..45
FT /note="Required for vacuolar localization. Mediates
FT aggregation and vesicle formation in Cvt pathway"
FT /evidence="ECO:0000269|PubMed:2651436,
FT ECO:0000269|PubMed:8521804, ECO:0000269|PubMed:8601598"
FT /id="PRO_0000026806"
FT CHAIN 46..514
FT /note="Vacuolar aminopeptidase 1"
FT /id="PRO_0000026807"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT SITE 45..46
FT /note="Cleavage; by protease B (PrB/PRB1)"
FT /evidence="ECO:0000269|PubMed:1400574"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 233
FT /note="T -> S (in Ref. 1; CAA68815)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> D (in Ref. 1; CAA68815)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="D -> E (in Ref. 1; CAA68815)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="P -> A (in Ref. 1; CAA68815)"
FT /evidence="ECO:0000305"
FT HELIX 1..17
FT /evidence="ECO:0007829|PDB:5JGE"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:5JH9"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5JH9"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:5JGF"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:5JGF"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5JGF"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5JGF"
FT TURN 250..254
FT /evidence="ECO:0007829|PDB:4R8F"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 302..319
FT /evidence="ECO:0007829|PDB:5JGF"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 424..437
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:5JGF"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 489..508
FT /evidence="ECO:0007829|PDB:5JGF"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5JH9"
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
