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Protein

AMP deaminase 2

Gene

Ampd2

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

Functioni

AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle (By similarity).By similarity

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 bindingi364 – 3641Zinc; catalyticBy similarity
Metal bindingi366 – 3661Zinc; catalyticBy similarity
Binding sitei366 – 3661SubstrateBy similarity
Metal bindingi633 – 6331Zinc; catalyticBy similarity
Binding sitei636 – 6361SubstrateBy similarity
Active sitei655 – 6551Proton acceptorPROSITE-ProRule annotation
Metal bindingi710 – 7101Zinc; catalyticBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cyclic purine nucleotide metabolic process Source: UniProtKB
  2. energy homeostasis Source: Ensembl
  3. 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_221255. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 2 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform L
Gene namesi
Name:Ampd2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2110. Ampd2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 824824AMP deaminase 2PRO_0000194409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei63 – 631PhosphoserineBy similarity
Modified residuei90 – 901PhosphotyrosineBy similarity
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei133 – 1331PhosphothreonineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ02356.
PRIDEiQ02356.

PTM databases

PhosphoSiteiQ02356.

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

GenevestigatoriQ02356.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliQ02356.
SMRiQ02356. Positions 160-807.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni435 – 4406Substrate bindingBy similarity
Regioni711 – 7144Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ02356.
KOiK01490.
OMAiRYETLCQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiQ02356.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 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.

Q02356-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASYPGPGKS KAKYPFKKRA SLQASAAAPE ARSGLGASPL QSARSLPGTA
60 70 80 90 100
PCLKHFPLDL RTSMDGKCKE IAEELFSRSL AESELRSAPY EFPEESPIEQ
110 120 130 140 150
LEERRQRLER QISQDVKLEP DILLRAKQDF LKTDSDSDLQ LYKEQGEGQG
160 170 180 190 200
DRGLWERDVV LEREFQRVII SGEEKCGVPF TDLLDAAKSV VRALFIREKY
210 220 230 240 250
MALSLQSFCP TTRRYLQQLA EKPLETRTYE QSPDTPVSAD APVHPPALEQ
260 270 280 290 300
HPYEHCEPST MPGDLGLGLR MVRGVVHVYT RRDPDEHCPE VELPYPDLQE
310 320 330 340 350
FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV
360 370 380 390 400
PHRDFYNIRK VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ
410 420 430 440 450
TLREVFESMN LTAYDLSVDT LDVHADRNTF HRFDKFNAKY NPIGESVLRE
460 470 480 490 500
IFIKTDNKIS GKYFAHIIKE VMSDLEESKY QNAELRLSIY GRSRDEWDKL
510 520 530 540 550
ARWAVNHRVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML ENIFLPLFEA
560 570 580 590 600
TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP
610 620 630 640 650
PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA
660 670 680 690 700
ENISHGLLLR KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS
710 720 730 740 750
RGLMVSLSTD DPLQFHFTKE PLMEEYSIAT QVWKLSSCDM CELARNSVLM
760 770 780 790 800
SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN VPDIRVGYRY ETLCQELALI
810 820
TQAVQSEMLE TIPEEVGIVM SPGP
Length:824
Mass (Da):94,787
Last modified:March 24, 2009 - v2
Checksum:i3076B550E17AF95C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166402 mRNA. Translation: AAI66402.1.
M38126 Genomic DNA. Translation: AAA40728.1.
PIRiA37056.
RefSeqiNP_001095151.1. NM_001101681.2.
UniGeneiRn.104557.

Genome annotation databases

EnsembliENSRNOT00000026051; ENSRNOP00000026051; ENSRNOG00000019240.
GeneIDi362015.
KEGGirno:362015.
UCSCiRGD:2110. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166402 mRNA. Translation: AAI66402.1.
M38126 Genomic DNA. Translation: AAA40728.1.
PIRiA37056.
RefSeqiNP_001095151.1. NM_001101681.2.
UniGeneiRn.104557.

3D structure databases

ProteinModelPortaliQ02356.
SMRiQ02356. Positions 160-807.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ02356.

Proteomic databases

PaxDbiQ02356.
PRIDEiQ02356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026051; ENSRNOP00000026051; ENSRNOG00000019240.
GeneIDi362015.
KEGGirno:362015.
UCSCiRGD:2110. rat.

Organism-specific databases

CTDi271.
RGDi2110. Ampd2.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ02356.
KOiK01490.
OMAiRYETLCQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiQ02356.
TreeFamiTF300439.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_221255. Purine salvage.

Miscellaneous databases

NextBioi678390.

Gene expression databases

GenevestigatoriQ02356.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 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. "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].
    Tissue: Lung.
  2. "Adenylate deaminase. A multigene family in humans and rats."
    Morisaki T., Sabina R.L., Holmes E.W.
    J. Biol. Chem. 265:11482-11486(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 632-719.
    Tissue: Brain.

Entry informationi

Entry nameiAMPD2_RAT
AccessioniPrimary (citable) accession number: Q02356
Secondary accession number(s): B2GUT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: March 24, 2009
Last modified: January 7, 2015
This is version 100 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

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.