AAP1_YEAST
ID AAP1_YEAST Reviewed; 856 AA.
AC P37898; D3DKZ5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Alanine/arginine aminopeptidase;
DE EC=3.4.11.-;
GN Name=AAP1; OrderedLocusNames=YHR047C;
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] OF 107-652.
RX PubMed=8100228; DOI=10.1016/s0021-9258(19)85242-0;
RA Caprioglio D.R., Padilla C., Werner-Washburne M.;
RT "Isolation and characterization of AAP1. A gene encoding an
RT alanine/arginine aminopeptidase in yeast.";
RL J. Biol. Chem. 268:14310-14315(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
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).
CC -!- FUNCTION: Positive effector of glycogen accumulation. May be involved
CC in nutrient-sensing.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- MISCELLANEOUS: Present with 77000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; L12542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00062; AAB68919.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06739.1; -; Genomic_DNA.
DR PIR; S46750; S46750.
DR RefSeq; NP_011913.1; NM_001179177.1.
DR AlphaFoldDB; P37898; -.
DR SMR; P37898; -.
DR BioGRID; 36479; 51.
DR DIP; DIP-6698N; -.
DR IntAct; P37898; 130.
DR MINT; P37898; -.
DR STRING; 4932.YHR047C; -.
DR MEROPS; M01.007; -.
DR iPTMnet; P37898; -.
DR MaxQB; P37898; -.
DR PaxDb; P37898; -.
DR PRIDE; P37898; -.
DR EnsemblFungi; YHR047C_mRNA; YHR047C; YHR047C.
DR GeneID; 856443; -.
DR KEGG; sce:YHR047C; -.
DR SGD; S000001089; AAP1.
DR VEuPathDB; FungiDB:YHR047C; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000155246; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; P37898; -.
DR OMA; FIPCVDH; -.
DR BioCyc; YEAST:G3O-31102-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:P37898; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P37898; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:SGD.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
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; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..856
FT /note="Alanine/arginine aminopeptidase"
FT /id="PRO_0000095105"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264..268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 386
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 550..569
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="V -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 97663 MW; 0209F9E0298DF9DB CRC64;
MSREVLPNNV TPLHYDITLE PNFRAFTFEG SLKIDLQIND HSINSVQINY LEIDFHSARI
EGVNAIEVNK NENQQKATLV FPNGTFENLG PSAKLEIIFS GILNDQMAGF YRAKYTDKVT
GETKYMATTQ MEATDARRAF PCFDEPNLKA TFAVTLVSES FLTHLSNMDV RNETIKEGKK
YTTFNTTPKM STYLVAFIVA DLRYVESNNF RIPVRVYSTP GDEKFGQFAA NLAARTLRFF
EDTFNIEYPL PKMDMVAVHE FSAGAMENWG LVTYRVIDLL LDIENSSLDR IQRVAEVIQH
ELAHQWFGNL VTMDWWEGLW LNEGFATWMS WYSCNKFQPE WKVWEQYVTD NLQRALNLDS
LRSSHPIEVP VNNADEINQI FDAISYSKGS SLLRMISKWL GEETFIKGVS QYLNKFKYGN
AKTGDLWDAL ADASGKDVCS VMNIWTKRVG FPVLSVKEHK NKITLTQHRY LSTGDVKEEE
DTTIYPILLA LKDSTGIDNT LVLNEKSATF ELKNEEFFKI NGDQSGIFIT SYSDERWAKL
SKQANLLSVE DRVGLVADAK ALSASGYTST TNFLNLISNW KNEDSFVVWE QIINSLSALK
STWVFEPEDI LNALDKFTLD LVLNKLSELG WNIGEDDSFA IQRLKVTLFS AACTSGNEKM
QSIAVEMFEE YANGNKQAIP ALFKAVVFNT VARLGGENNY EKIFNIYQNP VSSEEKIIAL
RALGRFEDKE LLERTLSYLL DGTVLNQDFY IPMQGIRVHK KGIERLWAWM QEHWDEIAKR
LQPGSPVLGG VLTLGLTNFT SFEALEKISA FYSRKVTKGF DQTLAQALDT IRSKAQWVSR
DREIVATYLR EHEYDQ
