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O08739

- AMPD3_MOUSE

UniProt

O08739 - AMPD3_MOUSE

Protein

AMP deaminase 3

Gene

Ampd3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 bindingi316 – 3161Zinc; catalyticBy similarity
    Metal bindingi318 – 3181Zinc; catalyticBy similarity
    Binding sitei318 – 3181SubstrateBy similarity
    Metal bindingi585 – 5851Zinc; catalyticBy similarity
    Binding sitei588 – 5881SubstrateBy similarity
    Active sitei607 – 6071Proton acceptorPROSITE-ProRule annotation
    Metal bindingi662 – 6621Zinc; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. ADP metabolic process Source: MGI
    2. AMP metabolic process Source: MGI
    3. ATP metabolic process Source: MGI
    4. energy homeostasis Source: MGI
    5. IMP biosynthetic process Source: MGI
    6. IMP salvage Source: UniProtKB-UniPathway

    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 3 (EC:3.5.4.6)
    Alternative name(s):
    AMP deaminase H-type
    AMP deaminase isoform E
    Heart-type AMPD
    Gene namesi
    Name:Ampd3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1096344. Ampd3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 766766AMP deaminase 3PRO_0000194411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei107 – 1071PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO08739.
    PaxDbiO08739.
    PRIDEiO08739.

    PTM databases

    PhosphoSiteiO08739.

    Expressioni

    Tissue specificityi

    Found in heart, lung brain, spleen, kidney and to a lesser extent in liver.

    Gene expression databases

    ArrayExpressiO08739.
    BgeeiO08739.
    CleanExiMM_AMPD3.
    GenevestigatoriO08739.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiO08739. 1 interaction.
    MINTiMINT-4115626.
    STRINGi10090.ENSMUSP00000123052.

    Structurei

    3D structure databases

    ProteinModelPortaliO08739.
    SMRiO08739. Positions 143-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni387 – 3926Substrate bindingBy similarity
    Regioni663 – 6664Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    GeneTreeiENSGT00390000008190.
    HOGENOMiHOG000092200.
    HOVERGENiHBG050494.
    InParanoidiQ8CFR4.
    KOiK01490.
    OMAiFSLHEML.
    OrthoDBiEOG70ZZMQ.
    PhylomeDBiO08739.
    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.

    O08739-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPEDCPIG    50
    QKEAKERELQ KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PTQQDWKGPP 100
    TASPAMSPAT PLVPGATSKP GPAPYAMPEY QRVTISGDYC AGITVEDYEQ 150
    AAKSLAKALM IREKYARLAY HRFPRTTAQY LAHQGESVPL EEGLPDFHPP 200
    PLPQEDPYCL DDAPPNLGYL VRMHGGVLFV YDNQTMLERQ EPHSLPYPDL 250
    ETYIVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML NEMSEFKELK 300
    SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKLGR 350
    KITLRQVFDS LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL 400
    RDLYLKTENY LGGEYFARMV KEVARELEDS KYQYSEPRLS IYGRSPKEWS 450
    SLARWFIQHK VYSPNMRWII QVPRIYDIFR SKKLLPNFGK MLENIFLPLF 500
    KATINPQDHR ELHLFLKYVT GFDSVDDESK HSDHMFSDKS PSPDLWTSEQ 550
    NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG SITHLVSAFL 600
    TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF 650
    LHKGLHVSLS TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV 700
    LQSGLSHQEK QKFLGQNYYK EGPEGNDIRK TNVAQIRMAF RYETLCNELS 750
    FLSDAMKSEE ITALTK 766
    Length:766
    Mass (Da):88,652
    Last modified:July 27, 2011 - v2
    Checksum:i94991133B18B8AA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511E → K in BAA19933. (PubMed:9133604)Curated
    Sequence conflicti645 – 6451N → K in BAA19933. (PubMed:9133604)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85596 mRNA. Translation: BAA19933.1.
    D88994 Genomic DNA. Translation: BAA32548.1. Sequence problems.
    AK133465 mRNA. Translation: BAE21671.1.
    CH466531 Genomic DNA. Translation: EDL16988.1.
    CH466531 Genomic DNA. Translation: EDL16989.1.
    CH466531 Genomic DNA. Translation: EDL16990.1.
    BC040366 mRNA. Translation: AAH40366.1.
    BC056380 mRNA. Translation: AAH56380.1.
    CCDSiCCDS21747.1.
    RefSeqiNP_001263230.1. NM_001276301.1.
    NP_033797.2. NM_009667.3.
    XP_006507285.1. XM_006507222.1.
    UniGeneiMm.3238.

    Genome annotation databases

    EnsembliENSMUST00000005829; ENSMUSP00000005829; ENSMUSG00000005686.
    ENSMUST00000170374; ENSMUSP00000130495; ENSMUSG00000005686.
    GeneIDi11717.
    KEGGimmu:11717.
    UCSCiuc009jfl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85596 mRNA. Translation: BAA19933.1 .
    D88994 Genomic DNA. Translation: BAA32548.1 . Sequence problems.
    AK133465 mRNA. Translation: BAE21671.1 .
    CH466531 Genomic DNA. Translation: EDL16988.1 .
    CH466531 Genomic DNA. Translation: EDL16989.1 .
    CH466531 Genomic DNA. Translation: EDL16990.1 .
    BC040366 mRNA. Translation: AAH40366.1 .
    BC056380 mRNA. Translation: AAH56380.1 .
    CCDSi CCDS21747.1.
    RefSeqi NP_001263230.1. NM_001276301.1.
    NP_033797.2. NM_009667.3.
    XP_006507285.1. XM_006507222.1.
    UniGenei Mm.3238.

    3D structure databases

    ProteinModelPortali O08739.
    SMRi O08739. Positions 143-761.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O08739. 1 interaction.
    MINTi MINT-4115626.
    STRINGi 10090.ENSMUSP00000123052.

    PTM databases

    PhosphoSitei O08739.

    Proteomic databases

    MaxQBi O08739.
    PaxDbi O08739.
    PRIDEi O08739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005829 ; ENSMUSP00000005829 ; ENSMUSG00000005686 .
    ENSMUST00000170374 ; ENSMUSP00000130495 ; ENSMUSG00000005686 .
    GeneIDi 11717.
    KEGGi mmu:11717.
    UCSCi uc009jfl.1. mouse.

    Organism-specific databases

    CTDi 272.
    MGIi MGI:1096344. Ampd3.

    Phylogenomic databases

    eggNOGi COG1816.
    GeneTreei ENSGT00390000008190.
    HOGENOMi HOG000092200.
    HOVERGENi HBG050494.
    InParanoidi Q8CFR4.
    KOi K01490.
    OMAi FSLHEML.
    OrthoDBi EOG70ZZMQ.
    PhylomeDBi O08739.
    TreeFami TF300439.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .

    Miscellaneous databases

    NextBioi 279393.
    PROi O08739.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08739.
    Bgeei O08739.
    CleanExi MM_AMPD3.
    Genevestigatori O08739.

    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 expression of cDNA encoding heart-type isoform of AMP deaminase."
      Wang X., Morisaki H., Sermsuvitayawong K., Mineo I., Toyama K., Ogasawara N., Mukai T., Morisaki T.
      Gene 188:285-290(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Genomic organization of Ampd3, heart-type AMPD gene, located in mouse chromosome 7."
      Sermsuvitayawong K., Wang X., Nagabukuro A., Matsuda Y., Morisaki H., Toyama K., Mukai T., Morisaki T.
      Mamm. Genome 8:767-769(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    3. "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: Ovary and Uterus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Strain: C57BL/6.
      Tissue: Brain and Eye.

    Entry informationi

    Entry nameiAMPD3_MOUSE
    AccessioniPrimary (citable) accession number: O08739
    Secondary accession number(s): O88692, Q8CFR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 102 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