Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3V1D3

- AMPD1_MOUSE

UniProt

Q3V1D3 - AMPD1_MOUSE

Protein

AMP deaminase 1

Gene

Ampd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 2 (18 Sep 2013)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    AMP deaminase plays a critical role in energy metabolism.

    Catalytic activityi

    AMP + H2O = IMP + NH3.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi301 – 3011Zinc; catalyticBy similarity
    Metal bindingi303 – 3031Zinc; catalyticBy similarity
    Binding sitei303 – 3031SubstrateBy similarity
    Metal bindingi570 – 5701Zinc; catalyticBy similarity
    Binding sitei573 – 5731SubstrateBy similarity
    Active sitei592 – 5921Proton acceptorPROSITE-ProRule annotation
    Metal bindingi647 – 6471Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP salvage Source: UniProtKB-UniPathway
    2. response to organic substance Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase 1 (EC:3.5.4.6)
    Alternative name(s):
    AMP deaminase isoform M
    Myoadenylate deaminase
    Gene namesi
    Name:Ampd1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:88015. Ampd1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745AMP deaminase 1PRO_0000269718Add
    BLAST

    Proteomic databases

    MaxQBiQ3V1D3.
    PaxDbiQ3V1D3.
    PRIDEiQ3V1D3.

    PTM databases

    PhosphoSiteiQ3V1D3.

    Expressioni

    Gene expression databases

    CleanExiMM_AMPD1.
    GenevestigatoriQ3V1D3.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiQ3V1D3. 1 interaction.
    STRINGi10090.ENSMUSP00000088217.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3V1D3.
    SMRiQ3V1D3. Positions 565-652.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni372 – 3776Substrate bindingBy similarity
    Regioni648 – 6514Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00390000008190.
    HOGENOMiHOG000092200.
    HOVERGENiHBG050494.
    InParanoidiQ3V1D3.
    KOiK01490.
    OMAiNMTWMIQ.
    OrthoDBiEOG70ZZMQ.
    TreeFamiTF300439.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 1 hit.
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3V1D3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS    50
    LHEMQAHIFH MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF 100
    ISSSPTYESV PDFQRVQITG DYASGVTVED FEVVCKGLYR ALCIREKYMQ 150
    KSFQRFPKTP SKYLRNIDGE ALVGNESFYP VFTPPPKKGE DPFRTEDLPA 200
    NLGYHLKMKA GVIYIYPDEA AANRDEPKPY PYPNLDDFLD DMNFLLALIA 250
    QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT 300
    HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP 350
    YDLTVDSLDV HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY 400
    FATIIKEVGA DLVEAKYQHA EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN 450
    MTWMIQVPRI YDVFRSKNFL PHFGKMLENI FLPVFEATIN PQAHPDLSVF 500
    LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMENNPSYT YYAYYMYANI 550
    TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP 600
    VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM 650
    QFHFTKEPLM EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG 700
    NNYLEEGPVG NDIRRTNVAQ IRMAYRYETW CYELNLIAEG LKATE 745
    Length:745
    Mass (Da):86,105
    Last modified:September 18, 2013 - v2
    Checksum:i4595A57908A13239
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261E → D in BAE21218. (PubMed:16141072)Curated
    Sequence conflicti534 – 5341E → G in BAE21218. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132524 mRNA. Translation: BAE21218.1.
    AC150894 Genomic DNA. No translation available.
    AC163297 Genomic DNA. No translation available.
    CCDSiCCDS38571.1.
    RefSeqiNP_001028475.2. NM_001033303.2.
    UniGeneiMm.331272.

    Genome annotation databases

    EnsembliENSMUST00000090715; ENSMUSP00000088217; ENSMUSG00000070385.
    GeneIDi229665.
    KEGGimmu:229665.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132524 mRNA. Translation: BAE21218.1 .
    AC150894 Genomic DNA. No translation available.
    AC163297 Genomic DNA. No translation available.
    CCDSi CCDS38571.1.
    RefSeqi NP_001028475.2. NM_001033303.2.
    UniGenei Mm.331272.

    3D structure databases

    ProteinModelPortali Q3V1D3.
    SMRi Q3V1D3. Positions 565-652.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3V1D3. 1 interaction.
    STRINGi 10090.ENSMUSP00000088217.

    PTM databases

    PhosphoSitei Q3V1D3.

    Proteomic databases

    MaxQBi Q3V1D3.
    PaxDbi Q3V1D3.
    PRIDEi Q3V1D3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090715 ; ENSMUSP00000088217 ; ENSMUSG00000070385 .
    GeneIDi 229665.
    KEGGi mmu:229665.

    Organism-specific databases

    CTDi 270.
    MGIi MGI:88015. Ampd1.

    Phylogenomic databases

    eggNOGi COG1816.
    GeneTreei ENSGT00390000008190.
    HOGENOMi HOG000092200.
    HOVERGENi HBG050494.
    InParanoidi Q3V1D3.
    KOi K01490.
    OMAi NMTWMIQ.
    OrthoDBi EOG70ZZMQ.
    TreeFami TF300439.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .

    Miscellaneous databases

    NextBioi 379583.
    PROi Q3V1D3.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_AMPD1.
    Genevestigatori Q3V1D3.

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 1 hit.
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
    TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J.
      Tissue: Skin.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiAMPD1_MOUSE
    AccessioniPrimary (citable) accession number: Q3V1D3
    Secondary accession number(s): F8VPY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: September 18, 2013
    Last modified: October 1, 2014
    This is version 71 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3