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Q02356 (AMPD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
AMP deaminase 2
EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform L
Gene names
Name:Ampd2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length824 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.

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionAMP deaminase activity

Inferred from electronic annotation. Source: 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 – 824824AMP deaminase 2
PRO_0000194409

Regions

Region435 – 4406Substrate binding By similarity
Region711 – 7144Substrate binding By similarity

Sites

Active site6551Proton acceptor By similarity
Metal binding3641Zinc; catalytic By similarity
Metal binding3661Zinc; catalytic By similarity
Metal binding6331Zinc; catalytic By similarity
Metal binding7101Zinc; catalytic By similarity
Binding site3661Substrate By similarity
Binding site6361Substrate By similarity

Amino acid modifications

Modified residue211Phosphoserine By similarity
Modified residue631Phosphoserine By similarity
Modified residue901Phosphotyrosine By similarity
Modified residue961Phosphoserine By similarity
Modified residue1131Phosphoserine By similarity
Modified residue1331Phosphothreonine By similarity
Modified residue1351Phosphoserine By similarity
Modified residue1371Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02356 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 3076B550E17AF95C

FASTA82494,787
        10         20         30         40         50         60 
MASYPGPGKS KAKYPFKKRA SLQASAAAPE ARSGLGASPL QSARSLPGTA PCLKHFPLDL 

        70         80         90        100        110        120 
RTSMDGKCKE IAEELFSRSL AESELRSAPY EFPEESPIEQ LEERRQRLER QISQDVKLEP 

       130        140        150        160        170        180 
DILLRAKQDF LKTDSDSDLQ LYKEQGEGQG DRGLWERDVV LEREFQRVII SGEEKCGVPF 

       190        200        210        220        230        240 
TDLLDAAKSV VRALFIREKY MALSLQSFCP TTRRYLQQLA EKPLETRTYE QSPDTPVSAD 

       250        260        270        280        290        300 
APVHPPALEQ HPYEHCEPST MPGDLGLGLR MVRGVVHVYT RRDPDEHCPE VELPYPDLQE 

       310        320        330        340        350        360 
FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV PHRDFYNIRK 

       370        380        390        400        410        420 
VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ TLREVFESMN LTAYDLSVDT 

       430        440        450        460        470        480 
LDVHADRNTF HRFDKFNAKY NPIGESVLRE IFIKTDNKIS GKYFAHIIKE VMSDLEESKY 

       490        500        510        520        530        540 
QNAELRLSIY GRSRDEWDKL ARWAVNHRVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML 

       550        560        570        580        590        600 
ENIFLPLFEA TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP 

       610        620        630        640        650        660 
PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA ENISHGLLLR 

       670        680        690        700        710        720 
KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS RGLMVSLSTD DPLQFHFTKE 

       730        740        750        760        770        780 
PLMEEYSIAT QVWKLSSCDM CELARNSVLM SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN 

       790        800        810        820 
VPDIRVGYRY ETLCQELALI TQAVQSEMLE TIPEEVGIVM SPGP

« Hide

References

« Hide 'large scale' references
[1]"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: Lung.
[2]"Adenylate deaminase. A multigene family in humans and rats."
Morisaki T., Sabina R.L., Holmes E.W.
J. Biol. Chem. 265:11482-11486(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 632-719.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC166402 mRNA. Translation: AAI66402.1.
M38126 Genomic DNA. Translation: AAA40728.1.
IPIIPI00554244.
PIRA37056.
RefSeqNP_001095151.1. NM_001101681.2.
UniGeneRn.104557.

3D structure databases

ProteinModelPortalQ02356.
SMRQ02356. Positions 160-807.
ModBaseSearch...

PTM databases

PhosphoSiteQ02356.

Proteomic databases

PaxDbQ02356.
PRIDEQ02356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026051; ENSRNOP00000026051; ENSRNOG00000019240.
GeneID362015.
KEGGrno:362015.
UCSCRGD:2110. rat.

Organism-specific databases

CTD271.
RGD2110. Ampd2.

Phylogenomic databases

eggNOGCOG1816.
GeneTreeENSGT00390000008190.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidQ02356.
KOK01490.
OrthoDBEOG41JZBP.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Gene expression databases

ArrayExpressQ02356.
GenevestigatorQ02356.
GermOnlineENSRNOG00000019240. Rattus norvegicus.

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

NextBio678390.

Entry information

Entry nameAMPD2_RAT
AccessionPrimary (citable) accession number: Q02356
Secondary accession number(s): B2GUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: March 24, 2009
Last modified: April 3, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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