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O09178

- AMPD3_RAT

UniProt

O09178 - AMPD3_RAT

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Protein

AMP deaminase 3

Gene

Ampd3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi315 – 3151Zinc; catalyticBy similarity
Metal bindingi317 – 3171Zinc; catalyticBy similarity
Binding sitei317 – 3171SubstrateBy similarity
Metal bindingi584 – 5841Zinc; catalyticBy similarity
Binding sitei587 – 5871SubstrateBy similarity
Active sitei606 – 6061Proton acceptorPROSITE-ProRule annotation
Metal bindingi661 – 6611Zinc; catalyticBy similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: RGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. AMP catabolic process Source: RGD
  2. 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

UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 3 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform E
Gene namesi
Name:Ampd3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2111. Ampd3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765AMP deaminase 3PRO_0000194412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO09178.
PRIDEiO09178.

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

GenevestigatoriO09178.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024933.

Structurei

3D structure databases

ProteinModelPortaliO09178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni386 – 3916Substrate bindingBy similarity
Regioni662 – 6654Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiO09178.
KOiK01490.
PhylomeDBiO09178.

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.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced.

Isoform 1 (identifier: O09178-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPKDCPIG
60 70 80 90 100
QKEAKERELQ KELAEQKSVE TAKRKKSFKM IRSQSMSLQM PTQDWKGPPS
110 120 130 140 150
VSPAMSPTTP LVLGAASKPG LAPYDMPEYQ RATISGDYCA GITMEDYEQA
160 170 180 190 200
AKSLAKALMI REKYARLAYH RFPRTTAQYL AHQGESVPLE EGLPDFHPPP
210 220 230 240 250
LPQEDPYCLD DAPPNLGYLV RMQGGVLFVY DNQTMLERQE PHSLPYPDLE
260 270 280 290 300
TYIVDMSHIL ALITDGPTKT YCHRRLNFLE SKFSLHEMLN EMSEFKELKS
310 320 330 340 350
NPHRDFYNVR KVDTHIHAAA CMNQKHLLRF IKYTYQTEPD RTVAEKLGRK
360 370 380 390 400
ITLRQVFDSL HMDPYDLTVD SLDVHAGRQT FHGFDKFNSK YNPVGASELR
410 420 430 440 450
DLYLKTENYL GGEYFARMVK EVARELEDSK YQYSEPRLSI YGRSPKEWSS
460 470 480 490 500
LARWFIQHKV YSPNMRWIIQ VPRIYDIFRS KKLLPSFGKM LENIFLPLFQ
510 520 530 540 550
ATINPQDHRE LHLFLKYVTG FDSVDDESKH SDHMFSDKSP SPDLWTSEQN
560 570 580 590 600
PPYSYYLYYM YANIMVLNNL RRERGLSTFL FRPHCGEAGS ITHLVSAFLT
610 620 630 640 650
ADNISHGLLL KKSPVLQYLY YLAQIPIAMS PLSNNSLFLE YSKNPLREFL
660 670 680 690 700
HKGLHVSLST DDPMQFHYTK EALMEEYAIA AQVWKLSTCD LCEIARNSVL
710 720 730 740 750
QSGLSHQEKQ KFLGQNYYKE GPEGNDIRKT NVAQIRMAFR YETLCNELSF
760
LSDAMKSEEI TALAD
Length:765
Mass (Da):88,483
Last modified:November 1, 1997 - v2
Checksum:iF826FA5966221B09
GO

Sequence cautioni

The sequence AAC53348.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90888 mRNA. Translation: AAC53348.1. Different initiation.
RefSeqiNP_113732.1. NM_031544.1.
UniGeneiRn.11106.

Genome annotation databases

GeneIDi25095.
KEGGirno:25095.
UCSCiRGD:2111. rat. [O09178-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90888 mRNA. Translation: AAC53348.1 . Different initiation.
RefSeqi NP_113732.1. NM_031544.1.
UniGenei Rn.11106.

3D structure databases

ProteinModelPortali O09178.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000024933.

Proteomic databases

PaxDbi O09178.
PRIDEi O09178.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25095.
KEGGi rno:25095.
UCSCi RGD:2111. rat. [O09178-1 ]

Organism-specific databases

CTDi 272.
RGDi 2111. Ampd3.

Phylogenomic databases

eggNOGi COG1816.
HOGENOMi HOG000092200.
HOVERGENi HBG050494.
InParanoidi O09178.
KOi K01490.
PhylomeDBi O09178.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .

Miscellaneous databases

NextBioi 605393.

Gene expression databases

Genevestigatori O09178.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029771. AMPD3.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
PTHR11359:SF2. PTHR11359:SF2. 1 hit.
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type."
    Mahnke-Zizelman D.K., D'Cunha J., Wojnar J.M., Brogley M.A., Sabina R.L.
    Biochem. J. 326:521-529(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiAMPD3_RAT
AccessioniPrimary (citable) accession number: O09178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 98 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3