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Q9FV51

- MAP1C_ARATH

UniProt

Q9FV51 - MAP1C_ARATH

Protein

Methionine aminopeptidase 1C, chloroplastic/mitochondrial

Gene

MAP1C

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    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 sitei172 – 1721SubstrateUniRule annotation
    Metal bindingi189 – 1891Divalent metal cation 1UniRule annotation
    Metal bindingi200 – 2001Divalent metal cation 1UniRule annotation
    Metal bindingi200 – 2001Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi262 – 2621Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei269 – 2691SubstrateUniRule annotation
    Metal bindingi296 – 2961Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi327 – 3271Divalent metal cation 1UniRule annotation
    Metal bindingi327 – 3271Divalent 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

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G25740-MONOMER.

    Protein family/group databases

    MEROPSiM24.A07.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1C, chloroplastic/mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1CUniRule annotation
    Short name:
    MetAP 1CUniRule annotation
    Alternative name(s):
    Peptidase M 1CUniRule annotation
    Gene namesi
    Name:MAP1C
    Ordered Locus Names:At3g25740
    ORF Names:K13N2.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G25740.

    Subcellular locationi

    Plastidchloroplast 1 PublicationUniRule annotation. Mitochondrion 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Mitochondrion, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 344Methionine aminopeptidase 1C, chloroplastic/mitochondrialPRO_0000045806
    Transit peptidei1 – ?Chloroplast and mitochondrionUniRule annotation

    Proteomic databases

    PaxDbiQ9FV51.
    PRIDEiQ9FV51.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevestigatoriQ9FV51.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV51.
    SMRiQ9FV51. Positions 67-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    InParanoidiQ9FV51.
    OMAiMERFIGH.
    PhylomeDBiQ9FV51.

    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.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9FV51-1 [UniParc]FASTAAdd to Basket

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    MLQKISQSIS LCNGDQFKPL IYLAGAPTNF ISSPLSGKKK SSSLRIKRIQ    50
    QLQSTLEDRI NPPLVCGTVS PRLSVPDHIL KPLYVESSKV PEISSELQIP 100
    DSIGIVKMKK ACELAARVLD YAGTLVRPFV TTDEIDKAVH QMVIEFGAYP 150
    SPLGYGGFPK SVCTSVNECM FHGIPDSRPL QNGDIINIDV AVYLDGYHGD 200
    TSKTFLCGDV NGSLKQLVKV TEECLEKGIS VCKDGASFKQ IGKIISEHAA 250
    KYGYNMERFI GHGVGTVLHS EPLIYLHSNY DYELEYMIEG QTFTLEPILT 300
    IGTTEFVTWP DKWTIVTADG GPAAQFEHTI LITTTGAEIL TISS 344
    Length:344
    Mass (Da):37,679
    Last modified:January 24, 2006 - v2
    Checksum:iABD84A7FF64D70BA
    GO

    Sequence cautioni

    The sequence BAA95761.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 2641V → L in AAG33976. (PubMed:11060042)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250962 mRNA. Translation: AAG33976.1.
    AB028607 Genomic DNA. Translation: BAA95761.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE77063.1.
    RefSeqiNP_189202.1. NM_113473.2.
    UniGeneiAt.16911.

    Genome annotation databases

    EnsemblPlantsiAT3G25740.1; AT3G25740.1; AT3G25740.
    GeneIDi822165.
    KEGGiath:AT3G25740.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250962 mRNA. Translation: AAG33976.1 .
    AB028607 Genomic DNA. Translation: BAA95761.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE77063.1 .
    RefSeqi NP_189202.1. NM_113473.2.
    UniGenei At.16911.

    3D structure databases

    ProteinModelPortali Q9FV51.
    SMRi Q9FV51. Positions 67-341.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M24.A07.

    Proteomic databases

    PaxDbi Q9FV51.
    PRIDEi Q9FV51.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G25740.1 ; AT3G25740.1 ; AT3G25740 .
    GeneIDi 822165.
    KEGGi ath:AT3G25740.

    Organism-specific databases

    GeneFarmi 2287. 184.
    TAIRi AT3G25740.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    InParanoidi Q9FV51.
    OMAi MERFIGH.
    PhylomeDBi Q9FV51.

    Enzyme and pathway databases

    BioCyci ARA:AT3G25740-MONOMER.

    Gene expression databases

    Genevestigatori Q9FV51.

    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.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    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. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      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.

    Entry informationi

    Entry nameiMAP1C_ARATH
    AccessioniPrimary (citable) accession number: Q9FV51
    Secondary accession number(s): Q9LS05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 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