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P10759 (AMPD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747AMP deaminase 1
PRO_0000194405

Regions

Region374 – 3796Substrate binding By similarity
Region650 – 6534Substrate binding By similarity

Sites

Active site5941Proton acceptor By similarity
Metal binding3031Zinc; catalytic By similarity
Metal binding3051Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity
Metal binding6491Zinc; catalytic By similarity
Binding site3051Substrate By similarity
Binding site5751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P10759 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: C8928B67F2DD9478

FASTA74786,432
        10         20         30         40         50         60 
MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LREMQAHIFH 

        70         80         90        100        110        120 
MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE EFISSSPTYE SVPDFQRVQI 

       130        140        150        160        170        180 
TGDYASGVTV EDFEVVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEALVAIESF 

       190        200        210        220        230        240 
YPVFTPPPKK GEDPFRREDL PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF 

       250        260        270        280        290        300 
LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV 

       310        320        330        340        350        360 
DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM HPYDLTVDSL 

       370        380        390        400        410        420 
DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVDAKYQ 

       430        440        450        460        470        480 
HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE 

       490        500        510        520        530        540 
NIFLPVFEAT INPQTHPDLS VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS 

       550        560        570        580        590        600 
YTYYAYYMYA NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK 

       610        620        630        640        650        660 
SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP 

       670        680        690        700        710        720 
LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF LGNNYLEEGP VGNDIRRTNV 

       730        740 
AQIRMAYRYE TWCYELNLIA EGLKSTE 

« Hide

References

[1]"Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation."
Sabina R.L., Marquetant R., Desai N.M., Kaletha K., Holmes E.W.
J. Biol. Chem. 262:12397-12400(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 536-548.
Tissue: Muscle.
[2]"A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1."
Mineo I., Clarke P.R., Sabina R.L., Holmes E.W.
Mol. Cell. Biol. 10:5271-5278(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02811 mRNA. Translation: AAB54086.1.
M58688 mRNA. Translation: AAA40726.1.
PIRA27366.
RefSeqNP_620231.1. NM_138876.1.
UniGeneRn.9794.

3D structure databases

ProteinModelPortalP10759.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP10759.
PRIDEP10759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656.
GeneID25028.
KEGGrno:25028.

Organism-specific databases

CTD270.
RGD2109. Ampd1.

Phylogenomic databases

eggNOGCOG1816.
GeneTreeENSGT00390000008190.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidP10759.
KOK01490.
OMANMTWMIQ.
OrthoDBEOG70ZZMQ.
PhylomeDBP10759.
TreeFamTF300439.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Gene expression databases

GenevestigatorP10759.

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

NextBio605167.
PROP10759.

Entry information

Entry nameAMPD1_RAT
AccessionPrimary (citable) accession number: P10759
Secondary accession number(s): P78501, Q6LDJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 100 of the entry and version 1 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