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O09178 (AMPD3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP deaminase 3

EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform E
Gene names
Name:Ampd3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length765 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.

Tissue specificity

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.

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Sequence caution

The sequence AAC53348.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processAMP catabolic process

Traceable author statement Ref.1. Source: RGD

IMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionAMP deaminase activity

Inferred from direct assay Ref.1. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: O09178-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 765765AMP deaminase 3
PRO_0000194412

Regions

Region386 – 3916Substrate binding By similarity
Region662 – 6654Substrate binding By similarity

Sites

Active site6061Proton acceptor By similarity
Metal binding3151Zinc; catalytic By similarity
Metal binding3171Zinc; catalytic By similarity
Metal binding5841Zinc; catalytic By similarity
Metal binding6611Zinc; catalytic By similarity
Binding site3171Substrate By similarity
Binding site5871Substrate By similarity

Amino acid modifications

Modified residue1061Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F826FA5966221B09

FASTA76588,483
        10         20         30         40         50         60 
MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPKDCPIG QKEAKERELQ 

        70         80         90        100        110        120 
KELAEQKSVE TAKRKKSFKM IRSQSMSLQM PTQDWKGPPS VSPAMSPTTP LVLGAASKPG 

       130        140        150        160        170        180 
LAPYDMPEYQ RATISGDYCA GITMEDYEQA AKSLAKALMI REKYARLAYH RFPRTTAQYL 

       190        200        210        220        230        240 
AHQGESVPLE EGLPDFHPPP LPQEDPYCLD DAPPNLGYLV RMQGGVLFVY DNQTMLERQE 

       250        260        270        280        290        300 
PHSLPYPDLE TYIVDMSHIL ALITDGPTKT YCHRRLNFLE SKFSLHEMLN EMSEFKELKS 

       310        320        330        340        350        360 
NPHRDFYNVR KVDTHIHAAA CMNQKHLLRF IKYTYQTEPD RTVAEKLGRK ITLRQVFDSL 

       370        380        390        400        410        420 
HMDPYDLTVD SLDVHAGRQT FHGFDKFNSK YNPVGASELR DLYLKTENYL GGEYFARMVK 

       430        440        450        460        470        480 
EVARELEDSK YQYSEPRLSI YGRSPKEWSS LARWFIQHKV YSPNMRWIIQ VPRIYDIFRS 

       490        500        510        520        530        540 
KKLLPSFGKM LENIFLPLFQ ATINPQDHRE LHLFLKYVTG FDSVDDESKH SDHMFSDKSP 

       550        560        570        580        590        600 
SPDLWTSEQN PPYSYYLYYM YANIMVLNNL RRERGLSTFL FRPHCGEAGS ITHLVSAFLT 

       610        620        630        640        650        660 
ADNISHGLLL KKSPVLQYLY YLAQIPIAMS PLSNNSLFLE YSKNPLREFL HKGLHVSLST 

       670        680        690        700        710        720 
DDPMQFHYTK EALMEEYAIA AQVWKLSTCD LCEIARNSVL QSGLSHQEKQ KFLGQNYYKE 

       730        740        750        760 
GPEGNDIRKT NVAQIRMAFR YETLCNELSF LSDAMKSEEI TALAD 

« Hide

References

[1]"Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type."
Mahnke-Zizelman D.K., D'Cunha J., Wojnar J.M., Brogley M.A., Sabina R.L.
Biochem. J. 326:521-529(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90888 mRNA. Translation: AAC53348.1. Different initiation.
RefSeqNP_113732.1. NM_031544.1.
UniGeneRn.11106.

3D structure databases

ProteinModelPortalO09178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000024933.

Proteomic databases

PaxDbO09178.
PRIDEO09178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25095.
KEGGrno:25095.
UCSCRGD:2111. rat. [O09178-1]

Organism-specific databases

CTD272.
RGD2111. Ampd3.

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidO09178.
KOK01490.
PhylomeDBO09178.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Gene expression databases

GenevestigatorO09178.

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

NextBio605393.

Entry information

Entry nameAMPD3_RAT
AccessionPrimary (citable) accession number: O09178
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 94 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