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P10759

- AMPD1_RAT

UniProt

P10759 - AMPD1_RAT

Protein

AMP deaminase 1

Gene

Ampd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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 bindingi303 – 3031Zinc; catalyticBy similarity
    Metal bindingi305 – 3051Zinc; catalyticBy similarity
    Binding sitei305 – 3051SubstrateBy similarity
    Metal bindingi572 – 5721Zinc; catalyticBy similarity
    Binding sitei575 – 5751SubstrateBy similarity
    Active sitei594 – 5941Proton acceptorPROSITE-ProRule annotation
    Metal bindingi649 – 6491Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. myosin heavy chain binding Source: RGD

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_221255. Purine salvage.
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi2109. Ampd1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747AMP deaminase 1PRO_0000194405Add
    BLAST

    Proteomic databases

    PaxDbiP10759.
    PRIDEiP10759.

    Expressioni

    Tissue specificityi

    Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.

    Gene expression databases

    GenevestigatoriP10759.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP10759.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni374 – 3796Substrate bindingBy similarity
    Regioni650 – 6534Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00390000008190.
    HOGENOMiHOG000092200.
    HOVERGENiHBG050494.
    InParanoidiP10759.
    KOiK01490.
    OMAiNMTWMIQ.
    OrthoDBiEOG70ZZMQ.
    PhylomeDBiP10759.
    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.

    P10759-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS    50
    LREMQAHIFH MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE 100
    EFISSSPTYE SVPDFQRVQI TGDYASGVTV EDFEVVCKGL YRALCIREKY 150
    MQKSFQRFPK TPSKYLRNID GEALVAIESF YPVFTPPPKK GEDPFRREDL 200
    PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF LDDMNFLLAL 250
    IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV 300
    DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM 350
    HPYDLTVDSL DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING 400
    EYFATIIKEV GADLVDAKYQ HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC 450
    PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE NIFLPVFEAT INPQTHPDLS 500
    VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS YTYYAYYMYA 550
    NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK 600
    SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD 650
    PMQFHFTKEP LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF 700
    LGNNYLEEGP VGNDIRRTNV AQIRMAYRYE TWCYELNLIA EGLKSTE 747
    Length:747
    Mass (Da):86,432
    Last modified:July 1, 1989 - v1
    Checksum:iC8928B67F2DD9478
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02811 mRNA. Translation: AAB54086.1.
    M58688 mRNA. Translation: AAA40726.1.
    PIRiA27366.
    RefSeqiNP_620231.1. NM_138876.1.
    UniGeneiRn.9794.

    Genome annotation databases

    EnsembliENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656.
    GeneIDi25028.
    KEGGirno:25028.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02811 mRNA. Translation: AAB54086.1 .
    M58688 mRNA. Translation: AAA40726.1 .
    PIRi A27366.
    RefSeqi NP_620231.1. NM_138876.1.
    UniGenei Rn.9794.

    3D structure databases

    ProteinModelPortali P10759.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P10759.
    PRIDEi P10759.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025248 ; ENSRNOP00000025248 ; ENSRNOG00000018656 .
    GeneIDi 25028.
    KEGGi rno:25028.

    Organism-specific databases

    CTDi 270.
    RGDi 2109. Ampd1.

    Phylogenomic databases

    eggNOGi COG1816.
    GeneTreei ENSGT00390000008190.
    HOGENOMi HOG000092200.
    HOVERGENi HBG050494.
    InParanoidi P10759.
    KOi K01490.
    OMAi NMTWMIQ.
    OrthoDBi EOG70ZZMQ.
    PhylomeDBi P10759.
    TreeFami TF300439.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .
    Reactomei REACT_221255. Purine salvage.

    Miscellaneous databases

    NextBioi 605167.
    PROi P10759.

    Gene expression databases

    Genevestigatori P10759.

    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. "Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation."
      Sabina R.L., Marquetant R., Desai N.M., Kaletha K., Holmes E.W.
      J. Biol. Chem. 262:12397-12400(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 536-548.
      Tissue: Muscle.
    2. "A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1."
      Mineo I., Clarke P.R., Sabina R.L., Holmes E.W.
      Mol. Cell. Biol. 10:5271-5278(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.

    Entry informationi

    Entry nameiAMPD1_RAT
    AccessioniPrimary (citable) accession number: P10759
    Secondary accession number(s): P78501, Q6LDJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 102 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, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3