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Protein

AMP deaminase 3

Gene

Ampd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

Pathway:iIMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. AMP deaminase 1 (Ampd1), AMP deaminase 3 (Ampd3), AMP deaminase 2 (Ampd2)
This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from AMP, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi316 – 3161Zinc; catalyticBy similarity
Metal bindingi318 – 3181Zinc; catalyticBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Metal bindingi585 – 5851Zinc; catalyticBy similarity
Binding sitei588 – 5881SubstrateBy similarity
Active sitei607 – 6071Proton acceptorPROSITE-ProRule annotation
Metal bindingi662 – 6621Zinc; catalyticBy similarity

GO - Molecular functioni

  • AMP deaminase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • ADP metabolic process Source: CACAO
  • AMP metabolic process Source: CACAO
  • ATP metabolic process Source: CACAO
  • energy homeostasis Source: MGI
  • erythrocyte homeostasis Source: CACAO
  • GTP metabolic process Source: CACAO
  • IMP biosynthetic process Source: MGI
  • IMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_345398. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 3 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase H-type
AMP deaminase isoform E
Heart-type AMPD
Gene namesi
Name:Ampd3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1096344. Ampd3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766AMP deaminase 3PRO_0000194411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO08739.
PaxDbiO08739.
PRIDEiO08739.

PTM databases

PhosphoSiteiO08739.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO08739.
CleanExiMM_AMPD3.
ExpressionAtlasiO08739. baseline and differential.
GenevisibleiO08739. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiO08739. 1 interaction.
MINTiMINT-4115626.
STRINGi10090.ENSMUSP00000005829.

Structurei

3D structure databases

ProteinModelPortaliO08739.
SMRiO08739. Positions 143-761.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni387 – 3926Substrate bindingBy similarity
Regioni663 – 6664Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiO08739.
KOiK01490.
OMAiMMELNEP.
OrthoDBiEOG70ZZMQ.
PhylomeDBiO08739.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029771. AMPD3.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF2. PTHR11359:SF2. 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.

O08739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPEDCPIG
60 70 80 90 100
QKEAKERELQ KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PTQQDWKGPP
110 120 130 140 150
TASPAMSPAT PLVPGATSKP GPAPYAMPEY QRVTISGDYC AGITVEDYEQ
160 170 180 190 200
AAKSLAKALM IREKYARLAY HRFPRTTAQY LAHQGESVPL EEGLPDFHPP
210 220 230 240 250
PLPQEDPYCL DDAPPNLGYL VRMHGGVLFV YDNQTMLERQ EPHSLPYPDL
260 270 280 290 300
ETYIVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML NEMSEFKELK
310 320 330 340 350
SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKLGR
360 370 380 390 400
KITLRQVFDS LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL
410 420 430 440 450
RDLYLKTENY LGGEYFARMV KEVARELEDS KYQYSEPRLS IYGRSPKEWS
460 470 480 490 500
SLARWFIQHK VYSPNMRWII QVPRIYDIFR SKKLLPNFGK MLENIFLPLF
510 520 530 540 550
KATINPQDHR ELHLFLKYVT GFDSVDDESK HSDHMFSDKS PSPDLWTSEQ
560 570 580 590 600
NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG SITHLVSAFL
610 620 630 640 650
TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF
660 670 680 690 700
LHKGLHVSLS TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV
710 720 730 740 750
LQSGLSHQEK QKFLGQNYYK EGPEGNDIRK TNVAQIRMAF RYETLCNELS
760
FLSDAMKSEE ITALTK
Length:766
Mass (Da):88,652
Last modified:July 27, 2011 - v2
Checksum:i94991133B18B8AA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511E → K in BAA19933 (PubMed:9133604).Curated
Sequence conflicti645 – 6451N → K in BAA19933 (PubMed:9133604).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21747.1.
RefSeqiNP_001263230.1. NM_001276301.1.
NP_033797.2. NM_009667.3.
XP_006507285.1. XM_006507222.2.
UniGeneiMm.3238.

Genome annotation databases

EnsembliENSMUST00000005829; ENSMUSP00000005829; ENSMUSG00000005686.
ENSMUST00000170374; ENSMUSP00000130495; ENSMUSG00000005686.
GeneIDi11717.
KEGGimmu:11717.
UCSCiuc009jfl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21747.1.
RefSeqiNP_001263230.1. NM_001276301.1.
NP_033797.2. NM_009667.3.
XP_006507285.1. XM_006507222.2.
UniGeneiMm.3238.

3D structure databases

ProteinModelPortaliO08739.
SMRiO08739. Positions 143-761.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08739. 1 interaction.
MINTiMINT-4115626.
STRINGi10090.ENSMUSP00000005829.

PTM databases

PhosphoSiteiO08739.

Proteomic databases

MaxQBiO08739.
PaxDbiO08739.
PRIDEiO08739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005829; ENSMUSP00000005829; ENSMUSG00000005686.
ENSMUST00000170374; ENSMUSP00000130495; ENSMUSG00000005686.
GeneIDi11717.
KEGGimmu:11717.
UCSCiuc009jfl.2. mouse.

Organism-specific databases

CTDi272.
MGIiMGI:1096344. Ampd3.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiO08739.
KOiK01490.
OMAiMMELNEP.
OrthoDBiEOG70ZZMQ.
PhylomeDBiO08739.
TreeFamiTF300439.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_345398. Purine salvage.

Miscellaneous databases

NextBioi279393.
PROiO08739.
SOURCEiSearch...

Gene expression databases

BgeeiO08739.
CleanExiMM_AMPD3.
ExpressionAtlasiO08739. baseline and differential.
GenevisibleiO08739. MM.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029771. AMPD3.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF2. PTHR11359:SF2. 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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAMPD3_MOUSE
AccessioniPrimary (citable) accession number: O08739
Secondary accession number(s): O88692, Q8CFR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.