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Q3V1D3 (AMPD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP deaminase 1

EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene names
Name:Ampd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism.

Catalytic activity

AMP + H2O = IMP + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processIMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionAMP deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745AMP deaminase 1
PRO_0000269718

Regions

Region372 – 3776Substrate binding By similarity
Region648 – 6514Substrate binding By similarity

Sites

Active site5921Proton acceptor By similarity
Metal binding3011Zinc; catalytic By similarity
Metal binding3031Zinc; catalytic By similarity
Metal binding5701Zinc; catalytic By similarity
Metal binding6471Zinc; catalytic By similarity
Binding site3031Substrate By similarity
Binding site5731Substrate By similarity

Experimental info

Sequence conflict2261E → D in BAE21218. Ref.1
Sequence conflict5341E → G in BAE21218. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3V1D3 [UniParc].

Last modified September 18, 2013. Version 2.
Checksum: 4595A57908A13239

FASTA74586,105
        10         20         30         40         50         60 
MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LHEMQAHIFH 

        70         80         90        100        110        120 
MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF ISSSPTYESV PDFQRVQITG 

       130        140        150        160        170        180 
DYASGVTVED FEVVCKGLYR ALCIREKYMQ KSFQRFPKTP SKYLRNIDGE ALVGNESFYP 

       190        200        210        220        230        240 
VFTPPPKKGE DPFRTEDLPA NLGYHLKMKA GVIYIYPDEA AANRDEPKPY PYPNLDDFLD 

       250        260        270        280        290        300 
DMNFLLALIA QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT 

       310        320        330        340        350        360 
HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP YDLTVDSLDV 

       370        380        390        400        410        420 
HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY FATIIKEVGA DLVEAKYQHA 

       430        440        450        460        470        480 
EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN MTWMIQVPRI YDVFRSKNFL PHFGKMLENI 

       490        500        510        520        530        540 
FLPVFEATIN PQAHPDLSVF LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMENNPSYT 

       550        560        570        580        590        600 
YYAYYMYANI TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP 

       610        620        630        640        650        660 
VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM QFHFTKEPLM 

       670        680        690        700        710        720 
EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG NNYLEEGPVG NDIRRTNVAQ 

       730        740 
IRMAYRYETW CYELNLIAEG LKATE 

« Hide

References

[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK132524 mRNA. Translation: BAE21218.1.
AC150894 Genomic DNA. No translation available.
AC163297 Genomic DNA. No translation available.
RefSeqNP_001028475.2. NM_001033303.2.
UniGeneMm.331272.

3D structure databases

ProteinModelPortalQ3V1D3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3V1D3. 1 interaction.
STRING10090.ENSMUSP00000088217.

PTM databases

PhosphoSiteQ3V1D3.

Proteomic databases

PaxDbQ3V1D3.
PRIDEQ3V1D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090715; ENSMUSP00000088217; ENSMUSG00000070385.
GeneID229665.
KEGGmmu:229665.

Organism-specific databases

CTD270.
MGIMGI:88015. Ampd1.

Phylogenomic databases

eggNOGCOG1816.
GeneTreeENSGT00390000008190.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidQ3V1D3.
KOK01490.
OMANMTWMIQ.
OrthoDBEOG70ZZMQ.
TreeFamTF300439.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Gene expression databases

CleanExMM_AMPD1.
GenevestigatorQ3V1D3.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
PANTHERPTHR11359. PTHR11359. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsTIGR01429. AMP_deaminase. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379583.
PROQ3V1D3.
SOURCESearch...

Entry information

Entry nameAMPD1_MOUSE
AccessionPrimary (citable) accession number: Q3V1D3
Secondary accession number(s): F8VPY9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 18, 2013
Last modified: April 16, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot