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Database: UniProt
Entry: P14904
LinkDB: P14904
Original site: P14904 
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   23-MAY-2018, entry version 175.
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=3; IntAct=EBI-2571, EBI-2571;
CC       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
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}.
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; 67.
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; 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; SIVNWEL; -.
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:0032258; P:protein localization by the Cvt pathway; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd05639; M18; 1.
DR   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR033818; Aminopeptidase_I.
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; 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}.
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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