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Q9SLN5

- MAP1A_ARATH

UniProt

Q9SLN5 - MAP1A_ARATH

Protein

Methionine aminopeptidase 1A

Gene

MAP1A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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).UniRule annotation

    Catalytic activityi

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

    Cofactori

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei214 – 2141SubstrateUniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
    Metal bindingi242 – 2421Divalent metal cation 1UniRule annotation
    Metal bindingi242 – 2421Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi305 – 3051Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei312 – 3121SubstrateUniRule annotation
    Metal bindingi338 – 3381Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi369 – 3691Divalent metal cation 1UniRule annotation
    Metal bindingi369 – 3691Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. N-terminal protein amino acid modification Source: TAIR
    2. protein initiator methionine removal Source: UniProtKB-HAMAP
    3. protein processing Source: TAIR

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT2G45240-MONOMER.

    Protein family/group databases

    MEROPSiM24.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1AUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1AUniRule annotation
    Short name:
    MetAP 1AUniRule annotation
    Alternative name(s):
    Peptidase M 1AUniRule annotation
    Gene namesi
    Name:MAP1A
    Ordered Locus Names:At2g45240
    ORF Names:F4L23.25
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G45240.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. cytosol Source: TAIR
    3. cytosolic ribosome Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 398397Methionine aminopeptidase 1APRO_0000148969Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9SLN5.
    PRIDEiQ9SLN5.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevestigatoriQ9SLN5.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    MINTiMINT-8069122.
    STRINGi3702.AT2G45240.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SLN5.
    SMRiQ9SLN5. Positions 95-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 5844Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    InParanoidiQ9SLN5.
    KOiK01265.
    OMAiCFKRNWS.
    PhylomeDBiQ9SLN5.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    IPR002893. Znf_MYND.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9SLN5-1 [UniParc]FASTAAdd to Basket

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    MASESDASSI ATLSCARCEK PAHLQCPKCI DLKLPREQAS FCTQECFKAA    50
    WSSHKSVHVK AQLSSIGDQN SDLISQGWLY CVKKGQARTP KLPHFDWTGP 100
    LKQYPISTKR VVPAEIEKPD WAIDGTPKVE PNSDLQHVVE IKTPEQIQRM 150
    RETCKIAREV LDAAARVIHP GVTTDEIDRV VHEATIAAGG YPSPLNYYFF 200
    PKSCCTSVNE VICHGIPDAR KLEDGDIVNV DVTVCYKGCH GDLNETYFVG 250
    NVDEASRQLV KCTYECLEKA IAIVKPGVRF REIGEIVNRH ATMSGLSVVR 300
    SYCGHGIGDL FHCAPNIPHY ARNKAVGVMK AGQTFTIEPM INAGGWRDRT 350
    WPDGWTAVTA DGKRSAQFEH TLLVTETGVE VLTARLPSSP DVYPWLTK 398
    Length:398
    Mass (Da):43,992
    Last modified:May 1, 2000 - v1
    Checksum:i4B9D23A90C5FA780
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311D → H in AAM65219. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250960 mRNA. Translation: AAG33974.1.
    AC002387 Genomic DNA. Translation: AAB82638.1.
    CP002685 Genomic DNA. Translation: AEC10528.1.
    AY099542 mRNA. Translation: AAM20394.1.
    BT008490 mRNA. Translation: AAP37849.1.
    AY087682 mRNA. Translation: AAM65219.1.
    PIRiB84888.
    RefSeqiNP_182049.1. NM_130087.3.
    UniGeneiAt.12298.

    Genome annotation databases

    EnsemblPlantsiAT2G45240.1; AT2G45240.1; AT2G45240.
    GeneIDi819132.
    KEGGiath:AT2G45240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250960 mRNA. Translation: AAG33974.1 .
    AC002387 Genomic DNA. Translation: AAB82638.1 .
    CP002685 Genomic DNA. Translation: AEC10528.1 .
    AY099542 mRNA. Translation: AAM20394.1 .
    BT008490 mRNA. Translation: AAP37849.1 .
    AY087682 mRNA. Translation: AAM65219.1 .
    PIRi B84888.
    RefSeqi NP_182049.1. NM_130087.3.
    UniGenei At.12298.

    3D structure databases

    ProteinModelPortali Q9SLN5.
    SMRi Q9SLN5. Positions 95-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-8069122.
    STRINGi 3702.AT2G45240.1-P.

    Protein family/group databases

    MEROPSi M24.017.

    Proteomic databases

    PaxDbi Q9SLN5.
    PRIDEi Q9SLN5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G45240.1 ; AT2G45240.1 ; AT2G45240 .
    GeneIDi 819132.
    KEGGi ath:AT2G45240.

    Organism-specific databases

    GeneFarmi 1939. 184.
    TAIRi AT2G45240.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    InParanoidi Q9SLN5.
    KOi K01265.
    OMAi CFKRNWS.
    PhylomeDBi Q9SLN5.

    Enzyme and pathway databases

    BioCyci ARA:AT2G45240-MONOMER.

    Miscellaneous databases

    PROi Q9SLN5.

    Gene expression databases

    Genevestigatori Q9SLN5.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    IPR002893. Znf_MYND.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
      Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
      EMBO J. 19:5916-5929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAP1A_ARATH
    AccessioniPrimary (citable) accession number: Q9SLN5
    Secondary accession number(s): Q548T6, Q8LAQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3