MAP1_YEAST
ID MAP1_YEAST Reviewed; 387 AA.
AC Q01662; D6VYP2;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MAP 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MetAP 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03174};
DE AltName: Full=Peptidase M 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE Flags: Precursor;
GN Name=MAP1; OrderedLocusNames=YLR244C; ORFNames=L9672.12;
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 [MRNA], AND PROTEIN SEQUENCE OF 11-24.
RX PubMed=1569059; DOI=10.1016/s0021-9258(18)42400-3;
RA Chang Y.-H., Teichert U., Smith J.A.;
RT "Molecular cloning, sequencing, deletion, and overexpression of a
RT methionine aminopeptidase gene from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:8007-8011(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION, ZINC-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7862096; DOI=10.1007/bf00294688;
RA Zuo S., Guo Q., Ling C., Chang Y.H.;
RT "Evidence that two zinc fingers in the methionine aminopeptidase from
RT Saccharomyces cerevisiae are important for normal growth.";
RL Mol. Gen. Genet. 246:247-253(1995).
RN [5]
RP MUTAGENESIS OF ASP-219.
RX PubMed=9367524; DOI=10.1006/abbi.1997.0345;
RA Klinkenberg M., Ling C., Chang Y.H.;
RT "A dominant negative mutation in Saccharomyces cerevisiae methionine
RT aminopeptidase-1 affects catalysis and interferes with the function of
RT methionine aminopeptidase-2.";
RL Arch. Biochem. Biophys. 347:193-200(1997).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=9177176; DOI=10.1073/pnas.94.12.6099;
RA Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., Crews C.M.;
RT "The anti-angiogenic agent fumagillin covalently binds and inhibits the
RT methionine aminopeptidase, MetAP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6099-6103(1997).
RN [7]
RP COFACTOR.
RX PubMed=9865965; DOI=10.1002/pro.5560071224;
RA Walker K.W., Bradshaw R.A.;
RT "Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a
RT cofactor: a case of mistaken identity?";
RL Protein Sci. 7:2684-2687(1998).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10075912;
RA Walker K.W., Yi E., Bradshaw R.A.;
RT "Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid
RT purification and improved activity assay.";
RL Biotechnol. Appl. Biochem. 29:157-163(1999).
RN [9]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=11811952; DOI=10.1006/abbi.2001.2675;
RA Chen S., Vetro J.A., Chang Y.H.;
RT "The specificity in vivo of two distinct methionine aminopeptidases in
RT Saccharomyces cerevisiae.";
RL Arch. Biochem. Biophys. 398:87-93(2002).
RN [10]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-22 AND HIS-62.
RX PubMed=11968008; DOI=10.1002/jcb.10161;
RA Vetro J.A., Chang Y.H.;
RT "Yeast methionine aminopeptidase type 1 is ribosome-associated and requires
RT its N-terminal zinc finger domain for normal function in vivo.";
RL J. Cell. Biochem. 85:678-688(2002).
RN [11]
RP FUNCTION.
RX PubMed=12874831; DOI=10.1002/jcb.10566;
RA Dummitt B., Micka W.S., Chang Y.H.;
RT "N-terminal methionine removal and methionine metabolism in Saccharomyces
RT cerevisiae.";
RL J. Cell. Biochem. 89:964-974(2003).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when the
CC second residue in the primary sequence is small and uncharged (Met-
CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-
CC terminal methionine removal. Less efficient when the second residue is
CC Val. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11811952,
CC ECO:0000269|PubMed:11968008, ECO:0000269|PubMed:12874831,
CC ECO:0000269|PubMed:7862096}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- ACTIVITY REGULATION: In contract to the MetAP 2 isoform, is not
CC inhibited by the fungal metabolite fumagillin, an antiangiogenic drug.
CC {ECO:0000269|PubMed:9177176}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.68 mM for a Met-Ala-Ser peptide {ECO:0000269|PubMed:10075912,
CC ECO:0000269|PubMed:7862096};
CC KM=6.56 mM for a Met-Gly-Met-Met peptide
CC {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096};
CC KM=139 uM for a Met-Ala-Ser-Trp peptide {ECO:0000269|PubMed:10075912,
CC ECO:0000269|PubMed:7862096};
CC Note=kcat is 1173, 1416 and 507 min(-1) with a Met-Ala-Ser, a Met-
CC Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.;
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S
CC translational complex. {ECO:0000255|HAMAP-Rule:MF_03174,
CC ECO:0000269|PubMed:11968008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 19600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03174}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77092; AAA75193.1; -; mRNA.
DR EMBL; U20865; AAB67398.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09558.1; -; Genomic_DNA.
DR PIR; S59390; S59390.
DR RefSeq; NP_013345.1; NM_001182131.1.
DR AlphaFoldDB; Q01662; -.
DR SMR; Q01662; -.
DR BioGRID; 31511; 49.
DR DIP; DIP-8076N; -.
DR IntAct; Q01662; 2.
DR MINT; Q01662; -.
DR STRING; 4932.YLR244C; -.
DR BindingDB; Q01662; -.
DR ChEMBL; CHEMBL2526; -.
DR MEROPS; M24.017; -.
DR iPTMnet; Q01662; -.
DR MaxQB; Q01662; -.
DR PaxDb; Q01662; -.
DR PRIDE; Q01662; -.
DR EnsemblFungi; YLR244C_mRNA; YLR244C; YLR244C.
DR GeneID; 850945; -.
DR KEGG; sce:YLR244C; -.
DR SGD; S000004234; MAP1.
DR VEuPathDB; FungiDB:YLR244C; -.
DR eggNOG; KOG2738; Eukaryota.
DR GeneTree; ENSGT00940000158205; -.
DR HOGENOM; CLU_015857_2_1_1; -.
DR InParanoid; Q01662; -.
DR OMA; GDHAYTF; -.
DR BioCyc; YEAST:YLR244C-MON; -.
DR Reactome; R-SCE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:Q01662; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q01662; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IMP:SGD.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR InterPro; IPR031615; Zfn-C6H2.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF15801; zf-C6H2; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT PROPEP 2..10
FT /evidence="ECO:0000269|PubMed:1569059"
FT /id="PRO_0000018596"
FT CHAIN 11..387
FT /note="Methionine aminopeptidase 1"
FT /id="PRO_0000018597"
FT REGION 22..66
FT /note="Zinc finger-like; important for proper ribosome
FT association"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 327
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 358
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 358
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 22
FT /note="C->S: Changes the ribosome profile distribution of
FT the protein and also increases its occurrence in the
FT cytosolic fraction."
FT /evidence="ECO:0000269|PubMed:11968008"
FT MUTAGEN 62
FT /note="H->R: Changes the ribosome profile distribution of
FT the protein."
FT /evidence="ECO:0000269|PubMed:11968008"
FT MUTAGEN 219
FT /note="D->N: Reduces activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:9367524"
SQ SEQUENCE 387 AA; 43373 MW; 4F0A30E9908B8A55 CRC64;
MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC DTSCYENNYK
AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV PEDIPKPDWA ANGLPVSEQR
NDRLNNIPIY KKDQIKKIRK ACMLGREVLD IAAAHVRPGI TTDELDEIVH NETIKRGAYP
SPLNYYNFPK SLCTSVNEVI CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN
ISKEALNTTE TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF
HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD GKLSAQFEHT
LLVTEHGVEI LTARNKKSPG GPRQRIK
