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Reviewed, UniProtKB/Swiss-Prot P10759 (AMPD1_RAT)

Last modified November 3, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    AMP deaminase 1
    EC=3.5.4.6
Alternative name(s):
    Myoadenylate deaminase
    AMP deaminase isoform M
Gene names
Name: Ampd1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism.

Catalytic activity

AMP + H2O = IMP + NH3.

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

Sites

Active site3631 Potential
Active site5731 Potential
Active site6491 Potential
Active site6501 Potential

Sequences

Sequence LengthMass (Da)Tools
P10759-1 [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: 3624265] [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: 2398891] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
+Additional computationally mapped references.

Cross-references

Sequence databases

J02811 mRNA. Translation: AAB54086.1.
M58688 mRNA. Translation: AAA40726.1.
IPIIPI00193319.
PIRA27366.
RefSeqNP_620231.1.
UniGeneRn.9794

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP10759.

Proteomic databases

PRIDEP10759.

Genome annotation databases

EnsemblENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656; Rattus norvegicus. [Genome view]
GeneID25028.
KEGGrno:25028.
UCSCNM_138876. rat.

Organism-specific databases

CTD25028.
RGD2109. Ampd1.

Phylogenomic databases

HOVERGENP10759.
OMAFAKLKMH.

Enzyme and pathway databases

BRENDA3.5.4.6. 248.

Gene expression databases

ArrayExpressP10759.
GenevestigatorP10759.
GermOnlineENSRNOG00000018656. Rattus norvegicus.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase.
IPR006329. AMP_deaminase.
IPR016297. AMP_deaminase_met.
[Graphical view]
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 Resources

NextBio605167.

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: November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents