Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vacuolar aminopeptidase 1

Gene

APE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).8 Publications

Catalytic activityi

Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.5 Publications

Cofactori

Zn2+By similarity5 PublicationsNote: Binds 2 Zn2+ ions per subunit. The average amount of Zn2+ bound at physiological metal concentrations will be lower than stoichiometric.By similarity5 Publications

Enzyme regulationi

Strongly and specifically activated by Cl- and Br-, which act as positive allosteric effectors. Inactivated by metal-chelating agents.3 Publications

pH dependencei

Optimum pH is 7-8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi132 – 1321Zinc 1By similarity
Binding sitei210 – 2101SubstrateBy similarity
Metal bindingi303 – 3031Zinc 1By similarity
Metal bindingi303 – 3031Zinc 2By similarity
Binding sitei339 – 3391SubstrateBy similarity
Metal bindingi340 – 3401Zinc 2By similarity
Metal bindingi385 – 3851Zinc 1By similarity
Binding sitei385 – 3851SubstrateBy similarity
Binding sitei388 – 3881SubstrateBy similarity
Metal bindingi479 – 4791Zinc 2By similarity

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • metalloaminopeptidase activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein catabolic process in the vacuole Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YKL103C-MONOMER.
BRENDAi3.4.11.22. 984.

Protein family/group databases

MEROPSiM18.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar aminopeptidase 11 Publication (EC:3.4.11.225 Publications)
Alternative name(s):
Aminopeptidase yscI1 Publication
Leucine aminopeptidase IV1 Publication
Short name:
LAPIV1 Publication
Lysosomal aminopeptidase III1 Publication
Polypeptidase1 Publication
Vacuolar aminopeptidase I1 Publication
Gene namesi
Name:APE11 Publication
Synonyms:API1 Publication, LAP41 Publication, YSC11 Publication
Ordered Locus Names:YKL103CImported
ORF Names:YKL455
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL103C.
SGDiS000001586. APE1.

Subcellular locationi

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1741175.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4545Required for vacuolar localization. Mediates aggregation and vesicle formation in Cvt pathway3 PublicationsPRO_0000026806Add
BLAST
Chaini46 – 514469Vacuolar aminopeptidase 1PRO_0000026807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi110 – 1101N-linked (GlcNAc...)PROSITE-ProRule annotation
Modified residuei356 – 3561PhosphoserineCombined sources
Glycosylationi448 – 4481N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Synthesized in a precursor form (prApe1) that has an amino-terminal propeptide. The N-terminal extension of the 61 kDa precursor is proteolytically processed in two sequential steps. The first step involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable intermediate (iAPI). The second step involves proteinase B (PrB/PRB1) and converts iAPI into the 50 kDa stable, mature enzyme (mApe1).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei45 – 462Cleavage; by protease B (PrB/PRB1)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP14904.
PeptideAtlasiP14904.

PTM databases

iPTMnetiP14904.

Miscellaneous databases

PMAP-CutDBP14904.

Interactioni

Subunit structurei

Homododecamer. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and further aggregates into higher multimers (the Ape1 complex) in the cytoplasm. The Ape1 complex is disaggregated in the vacuolar lumen, but mature aminopeptidase 1 (mApe1) retains its dodecameric form. Dodecamer assembly in the cytoplasm is essential for formation of an enzymatically active complex. If cytoplasmic homododecamerization of prApe1 is disturbed in mutants, homododecamers of mApe1 will form in the vacuole, but they are enzymatically inactive. Interacts with ATG19.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2571,EBI-2571

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi34031. 56 interactions.
DIPiDIP-1409N.
IntActiP14904. 31 interactions.
MINTiMINT-387783.

Chemistry

BindingDBiP14904.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 6210Combined sources
Helixi66 – 7813Combined sources
Turni79 – 813Combined sources
Turni92 – 943Combined sources
Beta strandi100 – 1067Combined sources
Turni107 – 1093Combined sources
Beta strandi110 – 1167Combined sources
Helixi122 – 1243Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi137 – 14913Combined sources
Beta strandi152 – 16312Combined sources
Helixi166 – 1683Combined sources
Beta strandi173 – 1819Combined sources
Beta strandi190 – 1956Combined sources
Helixi244 – 2474Combined sources
Turni250 – 2545Combined sources
Helixi257 – 26711Combined sources
Helixi271 – 2733Combined sources
Beta strandi274 – 28310Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi296 – 3005Combined sources
Helixi302 – 32019Combined sources
Helixi324 – 3263Combined sources
Beta strandi330 – 3378Combined sources
Turni339 – 3424Combined sources
Helixi349 – 3513Combined sources
Helixi353 – 36513Combined sources
Helixi372 – 3776Combined sources
Beta strandi380 – 3845Combined sources
Helixi395 – 3973Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi416 – 4183Combined sources
Turni419 – 4224Combined sources
Helixi424 – 43714Combined sources
Beta strandi441 – 4455Combined sources
Helixi456 – 4649Combined sources
Beta strandi467 – 4726Combined sources
Beta strandi475 – 4773Combined sources
Beta strandi480 – 4889Combined sources
Helixi489 – 50921Combined sources
Turni510 – 5134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R8FX-ray2.50A/B/C/D46-514[»]
ProteinModelPortaliP14904.
SMRiP14904. Positions 47-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

HOGENOMiHOG000253244.
InParanoidiP14904.
KOiK01268.
OMAiENPTIFH.
OrthoDBiEOG75TMP1.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE
60 70 80 90 100
DIAQEFIDFI YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG
110 120 130 140 150
KFYTIRNGTN LSAFILGKNW RAEKGVGVIG SHVDALTVKL KPVSFKDTAE
160 170 180 190 200
GYGRIAVAPY GGTLNELWLD RDLGIGGRLL YKKKGTNEIK SALVDSTPLP
210 220 230 240 250
VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPTPDEEGNE PPTDDEKKSP
260 270 280 290 300
LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP
310 320 330 340 350
RLDDRLCSFA AMIALICYAK DVNTEESDLF STVTLYDNEE IGSLTRQGAK
360 370 380 390 400
GGLLESVVER SSSAFTKKPV DLHTVWANSI ILSADVNHLY NPNFPEVYLK
410 420 430 440 450
NHFPVPNVGI TLSLDPNGHM ATDVVGTALV EELARRNGDK VQYFQIKNNS
460 470 480 490 500
RSGGTIGPSL ASQTGARTID LGIAQLSMHS IRAATGSKDV GLGVKFFNGF
510
FKHWRSVYDE FGEL
Length:514
Mass (Da):57,093
Last modified:February 1, 1994 - v2
Checksum:i702A8C88A2124C24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331T → S in CAA68815 (PubMed:2689224).Curated
Sequence conflicti323 – 3231N → D in CAA68815 (PubMed:2689224).Curated
Sequence conflicti328 – 3281D → E in CAA68815 (PubMed:2689224).Curated
Sequence conflicti369 – 3691P → A in CAA68815 (PubMed:2689224).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07522 Genomic DNA. Translation: CAA68815.1.
M25548 Genomic DNA. Translation: AAA34738.1.
X71133 Genomic DNA. Translation: CAA50454.1.
Z28103 Genomic DNA. Translation: CAA81943.1.
BK006944 Genomic DNA. Translation: DAA09055.1.
PIRiA33879.
RefSeqiNP_012819.1. NM_001179669.1.

Genome annotation databases

EnsemblFungiiYKL103C; YKL103C; YKL103C.
GeneIDi853758.
KEGGisce:YKL103C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07522 Genomic DNA. Translation: CAA68815.1.
M25548 Genomic DNA. Translation: AAA34738.1.
X71133 Genomic DNA. Translation: CAA50454.1.
Z28103 Genomic DNA. Translation: CAA81943.1.
BK006944 Genomic DNA. Translation: DAA09055.1.
PIRiA33879.
RefSeqiNP_012819.1. NM_001179669.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R8FX-ray2.50A/B/C/D46-514[»]
ProteinModelPortaliP14904.
SMRiP14904. Positions 47-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34031. 56 interactions.
DIPiDIP-1409N.
IntActiP14904. 31 interactions.
MINTiMINT-387783.

Chemistry

BindingDBiP14904.
ChEMBLiCHEMBL1741175.

Protein family/group databases

MEROPSiM18.001.

PTM databases

iPTMnetiP14904.

Proteomic databases

MaxQBiP14904.
PeptideAtlasiP14904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL103C; YKL103C; YKL103C.
GeneIDi853758.
KEGGisce:YKL103C.

Organism-specific databases

EuPathDBiFungiDB:YKL103C.
SGDiS000001586. APE1.

Phylogenomic databases

HOGENOMiHOG000253244.
InParanoidiP14904.
KOiK01268.
OMAiENPTIFH.
OrthoDBiEOG75TMP1.

Enzyme and pathway databases

BioCyciYEAST:YKL103C-MONOMER.
BRENDAi3.4.11.22. 984.

Miscellaneous databases

NextBioi974837.
PMAP-CutDBP14904.
PROiP14904.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene."
    Cueva R., Garcia-Alvarez N., Suarez-Rendueles P.
    FEBS Lett. 259:125-129(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: II-21.
  2. "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae."
    Chang Y.-H., Smith J.A.
    J. Biol. Chem. 264:6979-6983(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-63.
  3. "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of Saccharomyces cerevisiae suggests the presence of a second aspartate aminotransferase gene in yeast."
    Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H., Bolotin-Fukuhara M., Sor F.
    Yeast 9:1259-1265(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Isolation and properties of a pure yeast polypeptidase."
    Johnson M.J.
    J. Biol. Chem. 137:575-586(1941)
    Cited for: IDENTIFICATION, COFACTOR.
  7. "A lysosomal aminopeptidase isozyme in differentiating yeast cells and protoplasts."
    Matile P., Wiemken A., Guyer W.
    Planta 96:43-53(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Yeast aminopeptidase I. Chemical composition and catalytic properties."
    Metz G., Roehm K.H.
    Biochim. Biophys. Acta 429:933-949(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, GLYCOSYLATION, SUBUNIT, ENZYME REGULATION.
  9. "Subcellular localization and levels of aminopeptidases and dipeptidase in Saccharomyces cerevisiae."
    Frey J., Roehm K.H.
    Biochim. Biophys. Acta 527:31-41(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  10. "Isolation and characterization of aminopeptidase mutants of Saccharomyces cerevisiae."
    Trumbly R.J., Bradley G.
    J. Bacteriol. 156:36-48(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR.
  11. "Chloride as allosteric effector of yeast aminopeptidase I."
    Roehm K.H.
    Arch. Biochem. Biophys. 239:216-225(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
  12. "Metal binding to yeast aminopeptidase I."
    Roehm K.H.
    Eur. J. Biochem. 146:633-639(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, ENZYME REGULATION.
  13. "Proteinases, proteolysis and biological control in the yeast Saccharomyces cerevisiae."
    Achstetter T., Wolf D.H.
    Yeast 1:139-157(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  14. "Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway."
    Klionsky D.J., Cueva R., Yaver D.S.
    J. Cell Biol. 119:287-299(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  15. "Yeast aminopeptidase I is post-translationally sorted from the cytosol to the vacuole by a mechanism mediated by its bipartite N-terminal extension."
    Segui-Real B., Martinez M., Sandoval I.V.
    EMBO J. 14:5476-5484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  16. "Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I."
    Oda M.N., Scott S.V., Hefner-Gravink A., Caffarelli A.D., Klionsky D.J.
    J. Cell Biol. 132:999-1010(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  17. "Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole."
    Scott S.V., Hefner-Gravink A., Morano K.A., Noda T., Ohsumi Y., Klionsky D.J.
    Proc. Natl. Acad. Sci. U.S.A. 93:12304-12308(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING.
  18. "Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway."
    Kim J., Scott S.V., Oda M.N., Klionsky D.J.
    J. Cell Biol. 137:609-618(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  19. "Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism."
    Scott S.V., Baba M., Ohsumi Y., Klionsky D.J.
    J. Cell Biol. 138:37-44(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. "Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome."
    Baba M., Osumi M., Scott S.V., Klionsky D.J., Ohsumi Y.
    J. Cell Biol. 139:1687-1695(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "A new class of mutants deficient in dodecamerization of aminopeptidase 1 and vacuolar transport."
    Andrei-Selmer C., Knuppel A., Satyanarayana C., Heese C., Schu P.V.
    J. Biol. Chem. 276:11606-11614(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  22. "Yol082p, a novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole."
    Leber R., Silles E., Sandoval I.V., Mazon M.J.
    J. Biol. Chem. 276:29210-29217(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG19.
  23. "Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway."
    Scott S.V., Guan J., Hutchins M.U., Kim J., Klionsky D.J.
    Mol. Cell 7:1131-1141(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG19.
  24. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  25. "Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway."
    Shintani T., Klionsky D.J.
    J. Biol. Chem. 279:29889-29894(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathway."
    Adachi W., Suzuki N.N., Fujioka Y., Suzuki K., Ohsumi Y., Inagaki F.
    Acta Crystallogr. F 63:200-203(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  27. "Aminopeptidase I enzymatic activity."
    Schu P.
    Methods Enzymol. 451:67-78(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  28. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle formation in cytoplasm-to-vacuole targeting pathway."
    Morales Quinones M., Winston J.T., Stromhaug P.E.
    J. Biol. Chem. 287:10121-10133(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiAMPL_YEAST
AccessioniPrimary (citable) accession number: P14904
Secondary accession number(s): D6VXI5, P22060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5730 molecules/cell in log phase SD medium.1 Publication

Caution

It is unsure whether this protein is glycosylated or not. PubMed:5147 has shown that a preparation of aminopeptidase 1 contains about 12% of conjugated carbohydrate, while PubMed:1400574 could not identify any glycosylation, which is in agreement with the fact that aminopeptidase 1 does not transit through the secretory pathway.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.