Reviewed, UniProtKB/Swiss-Prot P14904 (AMPL_YEAST)

Names and origin

Protein names

Recommended name:
    Vacuolar aminopeptidase 1
    EC=3.4.11.22
Alternative name(s):
    Vacuolar aminopeptidase I
    Polypeptidase
    Leucine aminopeptidase IV
      Short name=LAPIV
    Aminopeptidase III
    Aminopeptidase yscI

Gene names

Name:	APE1
Synonyms:	LAP4
Ordered Locus Names:	YKL103C
ORF Names:	YKL455

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This vacuolar enzyme catalyzes the removal of amino acids from the N-terminus of peptides and proteins.
Catalytic activity	Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.
Cofactor	Binds 1 zinc ion per subunit.
Enzyme regulation	Inactivated by metal-chelating agents and specifically activated by Zn(2+) and Cl(-).
Subunit structure	Homododecamer.
Subcellular location	Vacuole.
Post-translational modification	After a zymogenic synthesis this vacuolar peptidase might be processed by proteinase yscA (PEP4).
Miscellaneous	Present with 5730 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase M18 family.

Ontologies

Keywords
Cellular component	Vacuole
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	fungal-type vacuole Inferred from direct assay. Source: SGD
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct metalloaminopeptidase activity Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-2571,EBI-2571
ADY3	Q07732	1	EBI-2571,EBI-33406
ATG19	P35193	2	EBI-2571,EBI-29291
SRP1	Q02821	1	EBI-2571,EBI-1797
TEM1	P38987	1	EBI-2571,EBI-19113
TFB1	P32776	1	EBI-2571,EBI-19146

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 45	45	May target aminopeptidase I to vacuoles		PRO_0000026806
	Chain	46 – 514	469	Vacuolar aminopeptidase 1		PRO_0000026807
Sites
	Metal binding	132	1	Zinc Potential
	Metal binding	210	1	Zinc Potential
	Metal binding	479	1	Zinc Potential
Amino acid modifications
	Modified residue	356	1	Phosphoserine
	Modified residue	452	1	Phosphoserine
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	110	1	N-linked (GlcNAc...) Potential
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	233	1	T → S in CAA68815. Ref.1
	Sequence conflict	323	1	N → D in CAA68815. Ref.1
	Sequence conflict	328	1	D → E in CAA68815. Ref.1
	Sequence conflict	369	1	P → A in CAA68815. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14904-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 702A8C88A2124C24	FASTA	514	57,093
	10 20 30 40 50 60 MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE DIAQEFIDFI 70 80 90 100 110 120 YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG KFYTIRNGTN LSAFILGKNW 130 140 150 160 170 180 RAEKGVGVIG SHVDALTVKL KPVSFKDTAE GYGRIAVAPY GGTLNELWLD RDLGIGGRLL 190 200 210 220 230 240 YKKKGTNEIK SALVDSTPLP VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPTPDEEGNE 250 260 270 280 290 300 PPTDDEKKSP LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP 310 320 330 340 350 360 RLDDRLCSFA AMIALICYAK DVNTEESDLF STVTLYDNEE IGSLTRQGAK GGLLESVVER 370 380 390 400 410 420 SSSAFTKKPV DLHTVWANSI ILSADVNHLY NPNFPEVYLK NHFPVPNVGI TLSLDPNGHM 430 440 450 460 470 480 ATDVVGTALV EELARRNGDK VQYFQIKNNS RSGGTIGPSL ASQTGARTID LGIAQLSMHS 490 500 510 IRAATGSKDV GLGVKFFNGF FKHWRSVYDE FGEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2689224] [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: 2651436] [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: 8109175] [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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-452, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y07522 Genomic DNA. Translation: CAA68815.1. M25548 Genomic DNA. Translation: AAA34738.1. X71133 Genomic DNA. Translation: CAA50454.1. Z28103 Genomic DNA. Translation: CAA81943.1.
PIR	A33879.
RefSeq	NP_012819.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1409N.
IntAct	P14904.
Protein family/group databases
MEROPS	M18.001.
Proteomic databases
PeptideAtlas	P14904.
Genome annotation databases
Ensembl	YKL103C. Saccharomyces cerevisiae. [Contig view]
GeneID	853758.
GenomeReviews	Gene locus YKL103C in contig Y13137_GR.
KEGG	sce:YKL103C.
NMPDR	fig|4932.3.peg.3801.
Organism-specific databases
CYGD	YKL103c.
SGD	S000001586. LAP4.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P14904.
Gene expression databases
GermOnline	YKL103C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001948. Peptidase_M18. [Graphical view]
Pfam	PF02127. Peptidase_M18. 1 hit. [Graphical view]
PRINTS	PR00932. AMINO1PTASE.
ProtoNet	Search...
Other Resources
LinkHub	P14904.
NextBio	974837.

Entry information

Entry name

AMPL_YEAST

Accession

Primary (citable) accession number: P14904
Secondary accession number(s): P22060

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	February 1, 1994
Last modified:	November 25, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)