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Protein

AMP deaminase 1

Gene

Ampd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi303 – 3031Zinc; catalyticBy similarity
Metal bindingi305 – 3051Zinc; catalyticBy similarity
Binding sitei305 – 3051SubstrateBy similarity
Metal bindingi572 – 5721Zinc; catalyticBy similarity
Binding sitei575 – 5751SubstrateBy similarity
Active sitei594 – 5941Proton acceptorPROSITE-ProRule annotation
Metal bindingi649 – 6491Zinc; catalyticBy similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. myosin heavy chain binding Source: RGD

GO - Biological processi

  1. IMP salvage Source: UniProtKB-UniPathway
  2. response to organic substance Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_221255. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 1 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene namesi
Name:Ampd1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2109. Ampd1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747AMP deaminase 1PRO_0000194405Add
BLAST

Proteomic databases

PaxDbiP10759.
PRIDEiP10759.

Expressioni

Tissue specificityi

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.

Gene expression databases

GenevestigatoriP10759.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP10759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 3796Substrate bindingBy similarity
Regioni650 – 6534Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiP10759.
KOiK01490.
OMAiNMTWMIQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiP10759.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10759-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS
60 70 80 90 100
LREMQAHIFH MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE
110 120 130 140 150
EFISSSPTYE SVPDFQRVQI TGDYASGVTV EDFEVVCKGL YRALCIREKY
160 170 180 190 200
MQKSFQRFPK TPSKYLRNID GEALVAIESF YPVFTPPPKK GEDPFRREDL
210 220 230 240 250
PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF LDDMNFLLAL
260 270 280 290 300
IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV
310 320 330 340 350
DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM
360 370 380 390 400
HPYDLTVDSL DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING
410 420 430 440 450
EYFATIIKEV GADLVDAKYQ HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC
460 470 480 490 500
PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE NIFLPVFEAT INPQTHPDLS
510 520 530 540 550
VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS YTYYAYYMYA
560 570 580 590 600
NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK
610 620 630 640 650
SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD
660 670 680 690 700
PMQFHFTKEP LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF
710 720 730 740
LGNNYLEEGP VGNDIRRTNV AQIRMAYRYE TWCYELNLIA EGLKSTE
Length:747
Mass (Da):86,432
Last modified:July 1, 1989 - v1
Checksum:iC8928B67F2DD9478
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02811 mRNA. Translation: AAB54086.1.
M58688 mRNA. Translation: AAA40726.1.
PIRiA27366.
RefSeqiNP_620231.1. NM_138876.1.
UniGeneiRn.9794.

Genome annotation databases

EnsembliENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656.
GeneIDi25028.
KEGGirno:25028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02811 mRNA. Translation: AAB54086.1.
M58688 mRNA. Translation: AAA40726.1.
PIRiA27366.
RefSeqiNP_620231.1. NM_138876.1.
UniGeneiRn.9794.

3D structure databases

ProteinModelPortaliP10759.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP10759.
PRIDEiP10759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656.
GeneIDi25028.
KEGGirno:25028.

Organism-specific databases

CTDi270.
RGDi2109. Ampd1.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiP10759.
KOiK01490.
OMAiNMTWMIQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiP10759.
TreeFamiTF300439.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_221255. Purine salvage.

Miscellaneous databases

NextBioi605167.
PROiP10759.

Gene expression databases

GenevestigatoriP10759.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiAMPD1_RAT
AccessioniPrimary (citable) accession number: P10759
Secondary accession number(s): P78501, Q6LDJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.