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O08739 (AMPD3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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 3
EC=3.5.4.6
Alternative name(s):
AMP deaminase H-type
AMP deaminase isoform E
Heart-type AMPD
Gene names
Name:Ampd3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length766 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

Found in heart, lung brain, spleen, kidney and to a lesser extent in liver.

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 – 766766AMP deaminase 3
PRO_0000194411

Regions

Region387 – 3926Substrate binding By similarity
Region663 – 6664Substrate binding By similarity

Sites

Active site6071Proton acceptor By similarity
Metal binding3161Zinc; catalytic By similarity
Metal binding3181Zinc; catalytic By similarity
Metal binding5851Zinc; catalytic By similarity
Metal binding6621Zinc; catalytic By similarity
Binding site3181Substrate By similarity
Binding site5881Substrate By similarity

Amino acid modifications

Modified residue1071Phosphoserine By similarity

Experimental info

Sequence conflict2511E → K in BAA19933. Ref.1
Sequence conflict6451N → K in BAA19933. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08739 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 94991133B18B8AA5

FASTA76688,652
        10         20         30         40         50         60 
MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPEDCPIG QKEAKERELQ 

        70         80         90        100        110        120 
KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PTQQDWKGPP TASPAMSPAT PLVPGATSKP 

       130        140        150        160        170        180 
GPAPYAMPEY QRVTISGDYC AGITVEDYEQ AAKSLAKALM IREKYARLAY HRFPRTTAQY 

       190        200        210        220        230        240 
LAHQGESVPL EEGLPDFHPP PLPQEDPYCL DDAPPNLGYL VRMHGGVLFV YDNQTMLERQ 

       250        260        270        280        290        300 
EPHSLPYPDL ETYIVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML NEMSEFKELK 

       310        320        330        340        350        360 
SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKLGR KITLRQVFDS 

       370        380        390        400        410        420 
LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL RDLYLKTENY LGGEYFARMV 

       430        440        450        460        470        480 
KEVARELEDS KYQYSEPRLS IYGRSPKEWS SLARWFIQHK VYSPNMRWII QVPRIYDIFR 

       490        500        510        520        530        540 
SKKLLPNFGK MLENIFLPLF KATINPQDHR ELHLFLKYVT GFDSVDDESK HSDHMFSDKS 

       550        560        570        580        590        600 
PSPDLWTSEQ NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG SITHLVSAFL 

       610        620        630        640        650        660 
TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF LHKGLHVSLS 

       670        680        690        700        710        720 
TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV LQSGLSHQEK QKFLGQNYYK 

       730        740        750        760 
EGPEGNDIRK TNVAQIRMAF RYETLCNELS FLSDAMKSEE ITALTK

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of cDNA encoding heart-type isoform of AMP deaminase."
Wang X., Morisaki H., Sermsuvitayawong K., Mineo I., Toyama K., Ogasawara N., Mukai T., Morisaki T.
Gene 188:285-290(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Genomic organization of Ampd3, heart-type AMPD gene, located in mouse chromosome 7."
Sermsuvitayawong K., Wang X., Nagabukuro A., Matsuda Y., Morisaki H., Toyama K., Mukai T., Morisaki T.
Mamm. Genome 8:767-769(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Ovary and Uterus.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Strain: C57BL/6.
Tissue: Brain and Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D85596 mRNA. Translation: BAA19933.1.
D88994 Genomic DNA. Translation: BAA32548.1. Sequence problems.
AK133465 mRNA. Translation: BAE21671.1.
CH466531 Genomic DNA. Translation: EDL16988.1.
CH466531 Genomic DNA. Translation: EDL16989.1.
CH466531 Genomic DNA. Translation: EDL16990.1.
BC040366 mRNA. Translation: AAH40366.1.
BC056380 mRNA. Translation: AAH56380.1.
IPIIPI00275398.
RefSeqNP_001263230.1. NM_001276301.1.
NP_033797.2. NM_009667.3.
UniGeneMm.3238.

3D structure databases

ProteinModelPortalO08739.
SMRO08739. Positions 143-761.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000123052.

PTM databases

PhosphoSiteO08739.

Proteomic databases

PaxDbO08739.
PRIDEO08739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005829; ENSMUSP00000005829; ENSMUSG00000005686.
ENSMUST00000170374; ENSMUSP00000130495; ENSMUSG00000005686.
GeneID11717.
KEGGmmu:11717.

Organism-specific databases

CTD272.
MGIMGI:1096344. Ampd3.

Phylogenomic databases

eggNOGCOG1816.
GeneTreeENSGT00390000008190.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidQ8CFR4.
KOK01490.
OMAFSLHEML.
OrthoDBEOG4J9MZC.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Gene expression databases

ArrayExpressO08739.
BgeeO08739.
CleanExMM_AMPD3.
GenevestigatorO08739.
GermOnlineENSMUSG00000005686. Mus musculus.

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

NextBio279393.
SOURCESearch...

Entry information

Entry nameAMPD3_MOUSE
AccessionPrimary (citable) accession number: O08739
Secondary accession number(s): O88692, Q8CFR4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents