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Q9CPW9

- MAP12_MOUSE

UniProt

Q9CPW9 - MAP12_MOUSE

Protein

Methionine aminopeptidase 1D, mitochondrial

Gene

Metap1d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.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 sitei161 – 1611SubstrateUniRule annotation
    Metal bindingi178 – 1781Divalent metal cation 1UniRule annotation
    Metal bindingi189 – 1891Divalent metal cation 1UniRule annotation
    Metal bindingi189 – 1891Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi252 – 2521Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi284 – 2841Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi315 – 3151Divalent metal cation 1UniRule annotation
    Metal bindingi315 – 3151Divalent 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. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Protein family/group databases

    MEROPSiM24.028.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1D, mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1DUniRule annotation
    Short name:
    MetAP 1DUniRule annotation
    Alternative name(s):
    Methionyl aminopeptidase type 1D, mitochondrial
    Peptidase M 1DUniRule annotation
    Gene namesi
    Name:Metap1d
    Synonyms:Map1d, Metapl1, Mnpepl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1913809. Metap1d.

    Subcellular locationi

    Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1919MitochondrionUniRule annotationAdd
    BLAST
    Chaini20 – 335316Methionine aminopeptidase 1D, mitochondrialPRO_0000314127Add
    BLAST

    Proteomic databases

    PaxDbiQ9CPW9.
    PRIDEiQ9CPW9.

    PTM databases

    PhosphoSiteiQ9CPW9.

    Expressioni

    Gene expression databases

    BgeeiQ9CPW9.
    CleanExiMM_METAPL1.
    GenevestigatoriQ9CPW9.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9CPW9. 1 interaction.
    MINTiMINT-4124719.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CPW9.
    SMRiQ9CPW9. Positions 60-330.
    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.
    GeneTreeiENSGT00390000002284.
    HOGENOMiHOG000030427.
    HOVERGENiHBG067178.
    InParanoidiQ9CPW9.
    KOiK01265.
    OMAiLNHIYLH.
    OrthoDBiEOG786H38.
    PhylomeDBiQ9CPW9.
    TreeFamiTF325318.

    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.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9CPW9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAPIGVPLL VRGGCQRILS SPLNHIYLHK RSGSQQRRHF FFWRQRDISH    50
    SVVSPAAVSP AHPVPKRIKK PDYVTTGIVP DWGDSIEVKD EDQIQGLREA 100
    CRLARHVLLL AGKSLKVDMT TEEIDALVHW EIIRHDAYPS PLGYGRFPKS 150
    VCTSVNNVLC HGIPDSRPLQ DGDIINIDVT VYYNGYHGDT SETFLVGNVD 200
    ESGKKLVEVA RRCRDEAIAA CRAGAPFSVI GNTISRITHQ NGLQVCPHFV 250
    GHGIGSYFHG HPEIWHHAND NDLPMEEGMA FTIEPIITEG SPEFKVLEDA 300
    WTVVSLDNQR SAQFEHTVLI TPRGVEILTK LPQEA 335
    Length:335
    Mass (Da):37,262
    Last modified:June 1, 2001 - v1
    Checksum:iEF270DDD1826E802
    GO
    Isoform 2 (identifier: Q9CPW9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.

    Show »
    Length:217
    Mass (Da):24,058
    Checksum:i0EE940FF76A74279
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321N → T in CAC88860. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 2. 2 PublicationsVSP_030210Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ414378 mRNA. Translation: CAC88860.1.
    AK005241 mRNA. Translation: BAB23899.1.
    AK010067 mRNA. Translation: BAB26680.1.
    AL928931 Genomic DNA. Translation: CAM23833.1.
    BC051534 mRNA. Translation: AAH51534.1.
    CCDSiCCDS16115.1. [Q9CPW9-1]
    RefSeqiNP_079909.1. NM_025633.3. [Q9CPW9-1]
    XP_006500073.1. XM_006500010.1. [Q9CPW9-2]
    UniGeneiMm.152796.
    Mm.443051.

    Genome annotation databases

    EnsembliENSMUST00000037210; ENSMUSP00000048190; ENSMUSG00000041921. [Q9CPW9-1]
    GeneIDi66559.
    KEGGimmu:66559.
    UCSCiuc008kas.1. mouse. [Q9CPW9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ414378 mRNA. Translation: CAC88860.1 .
    AK005241 mRNA. Translation: BAB23899.1 .
    AK010067 mRNA. Translation: BAB26680.1 .
    AL928931 Genomic DNA. Translation: CAM23833.1 .
    BC051534 mRNA. Translation: AAH51534.1 .
    CCDSi CCDS16115.1. [Q9CPW9-1 ]
    RefSeqi NP_079909.1. NM_025633.3. [Q9CPW9-1 ]
    XP_006500073.1. XM_006500010.1. [Q9CPW9-2 ]
    UniGenei Mm.152796.
    Mm.443051.

    3D structure databases

    ProteinModelPortali Q9CPW9.
    SMRi Q9CPW9. Positions 60-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9CPW9. 1 interaction.
    MINTi MINT-4124719.

    Protein family/group databases

    MEROPSi M24.028.

    PTM databases

    PhosphoSitei Q9CPW9.

    Proteomic databases

    PaxDbi Q9CPW9.
    PRIDEi Q9CPW9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037210 ; ENSMUSP00000048190 ; ENSMUSG00000041921 . [Q9CPW9-1 ]
    GeneIDi 66559.
    KEGGi mmu:66559.
    UCSCi uc008kas.1. mouse. [Q9CPW9-1 ]

    Organism-specific databases

    CTDi 254042.
    MGIi MGI:1913809. Metap1d.

    Phylogenomic databases

    eggNOGi COG0024.
    GeneTreei ENSGT00390000002284.
    HOGENOMi HOG000030427.
    HOVERGENi HBG067178.
    InParanoidi Q9CPW9.
    KOi K01265.
    OMAi LNHIYLH.
    OrthoDBi EOG786H38.
    PhylomeDBi Q9CPW9.
    TreeFami TF325318.

    Miscellaneous databases

    NextBioi 322010.
    PROi Q9CPW9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CPW9.
    CleanExi MM_METAPL1.
    Genevestigatori Q9CPW9.

    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.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of mouse MNPEPL peptidase, a novel member of peptidase family M24."
      Dando P.M., Fortunato M., Rawlings N.D., Barrett A.J.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Spleen.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Tongue.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiMAP12_MOUSE
    AccessioniPrimary (citable) accession number: Q9CPW9
    Secondary accession number(s): Q80WB3, Q91YD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3