APE2_YEAST
ID APE2_YEAST Reviewed; 952 AA.
AC P32454; D6VX41; P36055;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Aminopeptidase 2, mitochondrial;
DE Short=AP-II;
DE Short=Aminopeptidase II;
DE EC=3.4.11.-;
DE AltName: Full=YscII;
DE Flags: Precursor;
GN Name=APE2; Synonyms=LAP1; OrderedLocusNames=YKL157W;
GN ORFNames=YKL158W, YKL611, YKL612;
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=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 935.
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-952.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1765107; DOI=10.1111/j.1432-1033.1991.tb16461.x;
RA Garcia-Alvarez N., Cueva R., Suarez-Rendueles P.;
RT "Molecular cloning of soluble aminopeptidases from Saccharomyces
RT cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-
RT metallopeptidase.";
RL Eur. J. Biochem. 202:993-1002(1991).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=383482; DOI=10.1111/j.1432-1033.1979.tb13099.x;
RA Frey J., Roehm K.-H.;
RT "External and internal forms of yeast aminopeptidase II.";
RL Eur. J. Biochem. 97:169-173(1979).
RN [7]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14597615; DOI=10.1074/jbc.m310160200;
RA Ohlmeier S., Kastaniotis A.J., Hiltunen J.K., Bergmann U.;
RT "The yeast mitochondrial proteome, a study of fermentative and respiratory
RT growth.";
RL J. Biol. Chem. 279:3956-3979(2004).
RN [12]
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in the cellular supply of leucine from externally
CC offered leucine-containing dipeptide substrates.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm. Cytoplasm. Mitochondrion.
CC -!- MISCELLANEOUS: Present with 2910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA45403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA81496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA81497.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA81497.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA81999.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA81999.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA82000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z26877; CAA81496.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z26877; CAA81497.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z28157; CAA81999.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z28158; CAA82000.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY558356; AAS56682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X63998; CAA45403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006944; DAA09007.2; -; Genomic_DNA.
DR PIR; S37793; S37793.
DR PIR; S37794; S37794.
DR RefSeq; NP_012765.3; NM_001179723.2.
DR AlphaFoldDB; P32454; -.
DR SMR; P32454; -.
DR BioGRID; 33980; 158.
DR DIP; DIP-4391N; -.
DR IntAct; P32454; 53.
DR MINT; P32454; -.
DR STRING; 4932.YKL157W; -.
DR MEROPS; M01.006; -.
DR iPTMnet; P32454; -.
DR MaxQB; P32454; -.
DR PaxDb; P32454; -.
DR PRIDE; P32454; -.
DR EnsemblFungi; YKL157W_mRNA; YKL157W; YKL157W.
DR GeneID; 853699; -.
DR KEGG; sce:YKL157W; -.
DR SGD; S000001640; APE2.
DR VEuPathDB; FungiDB:YKL157W; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000155246; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; P32454; -.
DR OMA; MMEYVAI; -.
DR BioCyc; YEAST:YKL157W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P32454; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32454; protein.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:SGD.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IDA:SGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Mitochondrion; Periplasm; Protease; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..952
FT /note="Aminopeptidase 2, mitochondrial"
FT /id="PRO_0000095104"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 360..364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 482
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="R -> A (in Ref. 5; CAA45403)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="LL -> FI (in Ref. 5; CAA45403)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> V (in Ref. 5; CAA45403)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="D -> E (in Ref. 5; CAA45403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 952 AA; 107755 MW; 391C068DF4A18C2D CRC64;
MPIVRWLLLK SAVRGSSLIG KAHPCLRSIA AHPRYLSNVY SPPAGVSRSL RINVMWKQSK
LTPPRFVKIM NRRPLFTETS HACAKCQKTS QLLNKTPNRE ILPDNVVPLH YDLTVEPDFK
TFKFEGSVKI ELKINNPAID TVTLNTVDTD IHSAKIGDVT SSEIISEEEQ QVTTFAFPKG
TMSSFKGNAF LDIKFTGILN DNMAGFYRAK YEDKLTGETK YMATTQMEPT DARRAFPCFD
EPNLKASFAI TLVSDPSLTH LSNMDVKNEY VKDGKKVTLF NTTPKMSTYL VAFIVAELKY
VESKNFRIPV RVYATPGNEK HGQFAADLTA KTLAFFEKTF GIQYPLPKMD NVAVHEFSAG
AMENWGLVTY RVVDLLLDKD NSTLDRIQRV AEVVQHELAH QWFGNLVTMD WWEGLWLNEG
FATWMSWYSC NEFQPEWKVW EQYVTDTLQH ALSLDSLRSS HPIEVPVKKA DEINQIFDAI
SYSKGASLLR MISKWLGEET FIKGVSQYLN KFKYGNAKTE DLWDALADAS GKDVRSVMNI
WTKKVGFPVI SVSEDGNGKI TFRQNRYLST ADVKPDEDKT IYPVFLALKT KNGVDSSVVL
SERSKTIELE DPTFFKVNSE QSGIYITSYT DERWAKLGQQ ADLLSVEDRV GLVADVKTLS
ASGYTSTTNF LNLVSKWNNE KSFVVWDQII NSISSMKSTW LFEPKETQDA LDNFTKQLIS
GMTHHLGWEF KSSDSFSTQR LKVTMFGAAC AARDADVEKA ALKMFTDYCS GNKEAIPALI
KPIVFNTVAR VGGAENYEKV YKIYLDPISN DEKLAALRSL GRFKEPKLLE RTLGYLFDGT
VLNQDIYIPM QGMRAHQEGV EALWNWVKKN WDELVKRLPP GLSMLGSVVT LGTSGFTSMQ
KIDEIKKFFA TKSTKGFDQS LAQSLDTITS KAQWVNRDRD VVNKYLKENG YY
