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Protein

Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase

Gene

Adprm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress.1 Publication

Catalytic activityi

CDP-choline + H2O = CMP + phosphocholine.
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.
CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate.

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=39 µM for ADP-ribose1 Publication
  2. KM=28.5 µM for CDP-choline1 Publication
  3. KM=41.3 µM for CDP-ethanolamine1 Publication
  4. KM=28.1 µM for CDP-glycerol1 Publication
  5. KM=201 µM for ADP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi25 – 251Zinc 1By similarity
    Metal bindingi27 – 271Zinc 1By similarity
    Metal bindingi74 – 741Zinc 1By similarity
    Metal bindingi74 – 741Zinc 2By similarity
    Metal bindingi110 – 1101Zinc 2By similarity
    Metal bindingi241 – 2411Zinc 2By similarity
    Metal bindingi278 – 2781Zinc 2By similarity
    Metal bindingi280 – 2801Zinc 1By similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.6.1.53. 5301.
    ReactomeiR-RNO-2393930. Phosphate bond hydrolysis by NUDT proteins.
    SABIO-RKQ5M886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC:3.6.1.13, EC:3.6.1.16, EC:3.6.1.53)
    Alternative name(s):
    ADPRibase-Mn
    CDP-choline phosphohydrolase
    Gene namesi
    Name:Adprm
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 10

    Organism-specific databases

    RGDi1309906. Adprm.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Manganese-dependent ADP-ribose/CDP-alcohol diphosphatasePRO_0000286569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ5M886.

    Expressioni

    Tissue specificityi

    Preferentially expressed in immune cells.1 Publication

    Gene expression databases

    GenevisibleiQ5M886. RN.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000004560.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5M886.
    SMRiQ5M886. Positions 15-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ADPRibase-Mn family.Curated

    Phylogenomic databases

    eggNOGiENOG410IJ2N. Eukaryota.
    COG1409. LUCA.
    GeneTreeiENSGT00390000014667.
    HOGENOMiHOG000154875.
    HOVERGENiHBG100432.
    InParanoidiQ5M886.
    KOiK01517.
    OMAiHECVVCF.
    OrthoDBiEOG757CXK.
    PhylomeDBiQ5M886.
    TreeFamiTF331229.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5M886-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MADKPDPSSP ADGPEPLFSF GVIADIQYAD LEDGYNFQRS RRRYYRHSLV
    60 70 80 90 100
    HLQGAIEDWN KESSMPCCVL QLGDIIDGYN AQYKVSEKSL ELVMNTFQML
    110 120 130 140 150
    KVPVHHTWGN HEFYNFSRDY LANSKLNSKF LEDQIPQHPE TTPSENYYAY
    160 170 180 190 200
    HFVPFPKFRF ILLDSYDLSV LGIDQFSPKY EQCMKILREH NPNVELNSPQ
    210 220 230 240 250
    GLSEPQYVQF NGGFSQEQLN WLNEVLTFSD ANQEKVVIVS HLPIYPEASD
    260 270 280 290 300
    SVCLAWNYVD ALSIIWSHQC VVCFLAGHTH DGGYSEDPFG VHHVNLEGVI
    310 320 330
    ETAPDSQAFG TVHVYPDKML LKGRGRVPDR IMNYKRE
    Length:337
    Mass (Da):38,712
    Last modified:February 1, 2005 - v1
    Checksum:iB34FFB3351FD9727
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441Y → C in ABW03224 (PubMed:18352857).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU037900 mRNA. Translation: ABW03224.1.
    BC088174 mRNA. Translation: AAH88174.1.
    RefSeqiNP_001009246.1. NM_001009246.1.
    XP_006246665.1. XM_006246603.2.
    UniGeneiRn.163104.

    Genome annotation databases

    EnsembliENSRNOT00000004560; ENSRNOP00000004560; ENSRNOG00000003397.
    GeneIDi287406.
    KEGGirno:287406.
    UCSCiRGD:1309906. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU037900 mRNA. Translation: ABW03224.1.
    BC088174 mRNA. Translation: AAH88174.1.
    RefSeqiNP_001009246.1. NM_001009246.1.
    XP_006246665.1. XM_006246603.2.
    UniGeneiRn.163104.

    3D structure databases

    ProteinModelPortaliQ5M886.
    SMRiQ5M886. Positions 15-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000004560.

    Proteomic databases

    PaxDbiQ5M886.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000004560; ENSRNOP00000004560; ENSRNOG00000003397.
    GeneIDi287406.
    KEGGirno:287406.
    UCSCiRGD:1309906. rat.

    Organism-specific databases

    CTDi56985.
    RGDi1309906. Adprm.

    Phylogenomic databases

    eggNOGiENOG410IJ2N. Eukaryota.
    COG1409. LUCA.
    GeneTreeiENSGT00390000014667.
    HOGENOMiHOG000154875.
    HOVERGENiHBG100432.
    InParanoidiQ5M886.
    KOiK01517.
    OMAiHECVVCF.
    OrthoDBiEOG757CXK.
    PhylomeDBiQ5M886.
    TreeFamiTF331229.

    Enzyme and pathway databases

    BRENDAi3.6.1.53. 5301.
    ReactomeiR-RNO-2393930. Phosphate bond hydrolysis by NUDT proteins.
    SABIO-RKQ5M886.

    Miscellaneous databases

    NextBioi626034.
    PROiQ5M886.

    Gene expression databases

    GenevisibleiQ5M886. RN.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells."
      Canales J., Fernandez A., Ribeiro J.M., Cabezas A., Rodrigues J.R., Cameselle J.C., Costas M.J.
      Biochem. J. 413:103-113(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    2. "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].
      Tissue: Liver.

    Entry informationi

    Entry nameiADPRM_RAT
    AccessioniPrimary (citable) accession number: Q5M886
    Secondary accession number(s): A9Y0H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: February 1, 2005
    Last modified: December 9, 2015
    This is version 80 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. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.