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Protein

Methionine aminopeptidase 1

Gene

MAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val.UniRule annotation4 Publications

Miscellaneous

Present with 19600 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Enzyme regulationi

In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug.1 Publication

Kineticsi

Kcat is 1173, 1416 and 507 (Min-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.
  1. KM=2.68 mM for a Met-Ala-Ser peptide2 Publications
  2. KM=6.56 mM for a Met-Gly-Met-Met peptide2 Publications
  3. KM=139 µM for a Met-Ala-Ser-Trp peptide2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei202SubstrateUniRule annotation1
    Metal bindingi219Divalent metal cation 1UniRule annotation1
    Metal bindingi230Divalent metal cation 1UniRule annotation1
    Metal bindingi230Divalent metal cation 2; catalyticUniRule annotation1
    Metal bindingi294Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
    Binding sitei301SubstrateUniRule annotation1
    Metal bindingi327Divalent metal cation 2; catalyticUniRule annotation1
    Metal bindingi358Divalent metal cation 1UniRule annotation1
    Metal bindingi358Divalent metal cation 2; catalyticUniRule annotation1

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • metalloaminopeptidase activity Source: SGD
    • mRNA binding Source: SGD

    GO - Biological processi

    • negative regulation of gene expression Source: SGD
    • protein initiator methionine removal involved in protein maturation Source: SGD

    Keywordsi

    Molecular functionAminopeptidase, Hydrolase, Protease
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YLR244C-MONOMER
    ReactomeiR-SCE-2514859 Inactivation, recovery and regulation of the phototransduction cascade

    Protein family/group databases

    MEROPSiM24.001

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase M 1UniRule annotation
    Gene namesi
    Name:MAP1
    Ordered Locus Names:YLR244C
    ORF Names:L9672.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XII

    Organism-specific databases

    EuPathDBiFungiDB:YLR244C
    SGDiS000004234 MAP1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi22C → S: Changes the ribosome profile distribution of the protein and also increases its occurrence in the cytosolic fraction. 1 Publication1
    Mutagenesisi62H → R: Changes the ribosome profile distribution of the protein. 1 Publication1
    Mutagenesisi219D → N: Reduces activity 1000-fold. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2526

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    PropeptideiPRO_00000185962 – 101 Publication9
    ChainiPRO_000001859711 – 387Methionine aminopeptidase 1Add BLAST377

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ01662
    PaxDbiQ01662
    PRIDEiQ01662

    PTM databases

    iPTMnetiQ01662

    Interactioni

    Subunit structurei

    Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RKM3P382225EBI-2345582,EBI-21417

    Protein-protein interaction databases

    BioGridi3151138 interactors.
    IntActiQ01662 8 interactors.
    MINTiQ01662
    STRINGi4932.YLR244C

    Chemistry databases

    BindingDBiQ01662

    Structurei

    3D structure databases

    ProteinModelPortaliQ01662
    SMRiQ01662
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni22 – 66Zinc finger-like; important for proper ribosome associationAdd BLAST45

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00390000002284
    HOGENOMiHOG000030427
    InParanoidiQ01662
    KOiK01265
    OMAiGDHAYTF
    OrthoDBiEOG092C36SI

    Family and domain databases

    CDDicd01086 MetAP1, 1 hit
    HAMAPiMF_01974 MetAP_1, 1 hit
    InterProiView protein in InterPro
    IPR036005 Creatinase/aminopeptidase-like
    IPR000994 Pept_M24
    IPR001714 Pept_M24_MAP
    IPR002467 Pept_M24A_MAP1
    IPR031615 Zfn-C6H2
    PfamiView protein in Pfam
    PF00557 Peptidase_M24, 1 hit
    PF15801 zf-C6H2, 1 hit
    PRINTSiPR00599 MAPEPTIDASE
    SUPFAMiSSF55920 SSF55920, 1 hit
    TIGRFAMsiTIGR00500 met_pdase_I, 1 hit
    PROSITEiView protein in PROSITE
    PS00680 MAP_1, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q01662-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC
    60 70 80 90 100
    DTSCYENNYK AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV
    110 120 130 140 150
    PEDIPKPDWA ANGLPVSEQR NDRLNNIPIY KKDQIKKIRK ACMLGREVLD
    160 170 180 190 200
    IAAAHVRPGI TTDELDEIVH NETIKRGAYP SPLNYYNFPK SLCTSVNEVI
    210 220 230 240 250
    CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN ISKEALNTTE
    260 270 280 290 300
    TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF
    310 320 330 340 350
    HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD
    360 370 380
    GKLSAQFEHT LLVTEHGVEI LTARNKKSPG GPRQRIK
    Length:387
    Mass (Da):43,373
    Last modified:February 1, 1996 - v2
    Checksum:i4F0A30E9908B8A55
    GO

    Mass spectrometryi

    Molecular mass is 43779 Da from positions 2 - 387. Determined by MALDI. The measured mass is that of a near-native protein after Factor Xa-catalyzed cleavage of a GST fusion, having a remnant Gly-Ile-Pro-Glu-Phe peptide before the native Ser-2.1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77092 mRNA Translation: AAA75193.1
    U20865 Genomic DNA Translation: AAB67398.1
    BK006945 Genomic DNA Translation: DAA09558.1
    PIRiS59390
    RefSeqiNP_013345.1, NM_001182131.1

    Genome annotation databases

    EnsemblFungiiYLR244C; YLR244C; YLR244C
    GeneIDi850945
    KEGGisce:YLR244C

    Similar proteinsi

    Entry informationi

    Entry nameiMAP1_YEAST
    AccessioniPrimary (citable) accession number: Q01662
    Secondary accession number(s): D6VYP2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1996
    Last modified: April 25, 2018
    This is version 159 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome