Reviewed, UniProtKB/Swiss-Prot P32454 (APE2_YEAST)

Names and origin

Protein names

Recommended name:
    Aminopeptidase 2, mitochondrial
      Short name=Aminopeptidase II
      Short name=AP-II
    EC=3.4.11.-
Alternative name(s):
    YscII

Gene names

Name:	APE2
Synonyms:	LAP1
Ordered Locus Names:	YKL157W/YKL158W
ORF Names:	YKL611/YKL612

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	935 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	Involved in the cellular supply of leucine from externally offered leucine-containing dipeptide substrates.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Periplasm. Cytoplasm. Mitochondrion Ref.5 Ref.7 Ref.8 Ref.10.
Miscellaneous	Present with 2910 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the peptidase M1 family.
Sequence caution	The sequence AAS56682.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA45403.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA81496.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA81497.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA81999.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA82000.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Periplasm
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	peptide catabolic process Inferred from direct assay. Source: SGD proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall-bounded periplasmic space Ref.5 Inferred from direct assay. Source: SGD extracellular region Ref.5 Inferred from direct assay. Source: SGD mitochondrion Ref.7 Inferred from direct assay. Source: SGD
Molecular function	metalloaminopeptidase activity Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Mitochondrion Potential
	Chain	53 – 935	883	Aminopeptidase 2, mitochondrial		PRO_0000095104
Sites
	Active site	397	1	By similarity
	Active site	482	1	Proton donor Potential
	Metal binding	396	1	Zinc; catalytic By similarity
	Metal binding	400	1	Zinc; catalytic By similarity
	Metal binding	419	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	606	1	Phosphothreonine Ref.11
	Glycosylation	381	1	N-linked (GlcNAc...) Potential
	Glycosylation	713	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	73	1	R → A in CAA45403. Ref.4
	Sequence conflict	92 – 93	2	LL → FI in CAA45403. Ref.4
	Sequence conflict	255	1	D → V in CAA45403. Ref.4
	Sequence conflict	533	1	D → E in CAA45403. Ref.4
	Sequence conflict	935	1	G → VNRDRDVVNKYLKENGYY in CAA45403. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P32454-1 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: BD1961FC8CF7DBBD	FASTA	935	105,585
	10 20 30 40 50 60 MPIVRWLLLK SAVRGSSLIG KAHPCLRSIA AHPRYLSNVY SPPAGVSRSL RINVMWKQSK 70 80 90 100 110 120 LTPPRFVKIM NRRPLFTETS HACAKCQKTS QLLNKTPNRE ILPDNVVPLH YDLTVEPDFK 130 140 150 160 170 180 TFKFEGSVKI ELKINNPAID TVTLNTVDTD IHSAKIGDVT SSEIISEEEQ QVTTFAFPKG 190 200 210 220 230 240 TMSSFKGNAF LDIKFTGILN DNMAGFYRAK YEDKLTGETK YMATTQMEPT DARRAFPCFD 250 260 270 280 290 300 EPNLKASFAI TLVSDPSLTH LSNMDVKNEY VKDGKKVTLF NTTPKMSTYL VAFIVAELKY 310 320 330 340 350 360 VESKNFRIPV RVYATPGNEK HGQFAADLTA KTLAFFEKTF GIQYPLPKMD NVAVHEFSAG 370 380 390 400 410 420 AMENWGLVTY RVVDLLLDKD NSTLDRIQRV AEVVQHELAH QWFGNLVTMD WWEGLWLNEG 430 440 450 460 470 480 FATWMSWYSC NEFQPEWKVW EQYVTDTLQH ALSLDSLRSS HPIEVPVKKA DEINQIFDAI 490 500 510 520 530 540 SYSKGASLLR MISKWLGEET FIKGVSQYLN KFKYGNAKTE DLWDALADAS GKDVRSVMNI 550 560 570 580 590 600 WTKKVGFPVI SVSEDGNGKI TFRQNRYLST ADVKPDEDKT IYPVFLALKT KNGVDSSVVL 610 620 630 640 650 660 SERSKTIELE DPTFFKVNSE QSGIYITSYT DERWAKLGQQ ADLLSVEDRV GLVADVKTLS 670 680 690 700 710 720 ASGYTSTTNF LNLVSKWNNE KSFVVWDQII NSISSMKSTW LFEPKETQDA LDNFTKQLIS 730 740 750 760 770 780 GMTHHLGWEF KSSDSFSTQR LKVTMFGAAC AARDADVEKA ALKMFTDYCS GNKEAIPALI 790 800 810 820 830 840 KPIVFNTVAR VGGAENYEKV YKIYLDPISN DEKLAALRSL GRFKEPKLLE RTLGYLFDGT 850 860 870 880 890 900 VLNQDIYIPM QGMRAHQEGV EALWNWVKKN WDELVKRLPP GLSMLGSVVT LGTSGFTSMQ 910 920 930 KIDEIKKFFA TKSTKGFDQS LAQSLDTITS KAQWG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae." Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F. Yeast 10:S35-S40(1994) [PubMed: 8091859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93. Strain: ATCC 204508 / S288c.
[4]	"Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase." Garcia-Alvarez N., Cueva R., Suarez-Rendueles P. Eur. J. Biochem. 202:993-1002(1991) [PubMed: 1765107] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-935. Strain: ATCC 204510 / AB320.
[5]	"External and internal forms of yeast aminopeptidase II." Frey J., Roehm K.-H. Eur. J. Biochem. 97:169-173(1979) [PubMed: 383482] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast." Davis C.A., Grate L., Spingola M., Ares M. Jr. Nucleic Acids Res. 28:1700-1706(2000) [PubMed: 10734188] [Abstract] Cited for: IDENTIFICATION OF INTRON.
[7]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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].
[10]	"The yeast mitochondrial proteome, a study of fermentative and respiratory growth." Ohlmeier S., Kastaniotis A.J., Hiltunen J.K., Bergmann U. J. Biol. Chem. 279:3956-3979(2004) [PubMed: 14597615] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]	"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 THR-606, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z26877 Genomic DNA. Translation: CAA81496.1. Sequence problems. Z26877 Genomic DNA. Translation: CAA81497.1. Sequence problems. Z28157 Genomic DNA. Translation: CAA81999.1. Sequence problems. Z28158 Genomic DNA. Translation: CAA82000.1. Sequence problems. AY558356 Genomic DNA. Translation: AAS56682.1. Sequence problems. X63998 Genomic DNA. Translation: CAA45403.1. Sequence problems.
PIR	S37793. S37794.
RefSeq	NP_012765.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4391N.
IntAct	P32454. 57 interactions.
STRING	P32454.
Protein family/group databases
MEROPS	M01.006.
Proteomic databases
PeptideAtlas	P32454.
Genome annotation databases
Ensembl	YKL157W; YKL157W; YKL157W; Saccharomyces cerevisiae. [Genome view]
GeneID	853699.
KEGG	sce:YKL157W.
NMPDR	fig|4932.3.peg.3743.
Organism-specific databases
CYGD	YKL157w.
SGD	S000001640. APE2.
Phylogenomic databases
HOGENOM	HBG515894.
OMA	HPNIRGS.
OrthoDB	EOG902Z86.
Gene expression databases
ArrayExpress	P32454.
Genevestigator	P32454.
GermOnline	YKL157W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974687.

Entry information

Entry name

APE2_YEAST

Accession

Primary (citable) accession number: P32454
Secondary accession number(s): P36055

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 3, 2006
Last modified:	December 15, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)