P03958 (ADA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosine deaminase
EC=3.5.4.4

Alternative name(s):
Adenosine aminohydrolase

Gene names

Name:

Ada

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion By similarity.
Catalytic activity	Adenosine + H2O = inosine + NH3.
Cofactor	Binds 1 zinc ion per subunit. Ref.9 Ref.12 Ref.15
Subunit structure	Interacts with DPP4 (extracellular domain) By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Extracellular side By similarity. Cell junction By similarity. Cytoplasmic vesicle lumen. Cytoplasm By similarity. Note: Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion By similarity. Ref.10
Tissue specificity	Detected in brain neurons in the median emninence (at protein level). Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues. Ref.10
Disruption phenotype	Lethal at perinatal stages. Fetuses are viable up to 18 dpc, but after this survival decreases rapidly. Fewer that 10% of mutant pups are born live, and these die within hours after birth. Mutant fetuses display much higher than normal levels of adenosine and dATP, respiratory distress, hepatocellular degeneration and necrosis. Prenatal lethality can be avoided using an ADA expression vector with a trophoblast-specific promoter. Mutant mice die after about three weeks due to immunodeficiency, disturbances in purine metabolism and severe lung inflammation. Ref.7 Ref.8 Ref.11
Sequence similarities	Belongs to the adenosine and AMP deaminases family.
Biophysicochemical properties	Kinetic parameters: KM=20 µM for adenosine Ref.9 Ref.13 pH dependence: Optimum pH is 6-8.5.

Ontologies

Keywords
Biological process	Cell adhesion Nucleotide metabolism
Cellular component	Cell junction Cell membrane Cytoplasm Cytoplasmic vesicle Membrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Peyer's patch development Inferred from mutant phenotype PubMed 10720488. Source: MGI T cell activation Inferred from electronic annotation. Source: Compara adenosine catabolic process Inferred from direct assay Ref.13. Source: UniProtKB aging Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW dATP catabolic process Inferred from direct assay PubMed 7592575. Source: MGI deoxyadenosine catabolic process Inferred from direct assay PubMed 7592575. Source: MGI embryonic digestive tract development Inferred from mutant phenotype Ref.7. Source: MGI germinal center B cell differentiation Inferred from mutant phenotype PubMed 14607964. Source: MGI histamine secretion Inferred from electronic annotation. Source: Compara hypoxanthine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome inosine biosynthetic process Inferred from direct assay Ref.13. Source: UniProtKB liver development Inferred from mutant phenotype Ref.7Ref.8. Source: MGI lung alveolus development Inferred from mutant phenotype Ref.11. Source: MGI negative regulation of adenosine receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of circadian sleep/wake cycle, non-REM sleep Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response Inferred from mutant phenotype Ref.11PubMed 11591798PubMed 15240734PubMed 15630442PubMed 17601796. Source: MGI negative regulation of leukocyte migration Inferred from mutant phenotype PubMed 15240734PubMed 15630442. Source: MGI negative regulation of mature B cell apoptotic process Inferred from mutant phenotype PubMed 14607964. Source: MGI negative regulation of mucus secretion Inferred from mutant phenotype PubMed 15240734PubMed 15630442. Source: MGI negative regulation of penile erection Inferred from mutant phenotype PubMed 18340377. Source: MGI negative regulation of thymocyte apoptotic process Inferred from mutant phenotype PubMed 11067867PubMed 16670300. Source: MGI placenta development Inferred from mutant phenotype PubMed 9272950. Source: MGI positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 14607964. Source: MGI positive regulation of T cell differentiation in thymus Inferred from mutant phenotype PubMed 11067867PubMed 11435465PubMed 12163459PubMed 16670300. Source: MGI positive regulation of T cell receptor signaling pathway Inferred from mutant phenotype PubMed 11435465. Source: MGI positive regulation of alpha-beta T cell differentiation Inferred from mutant phenotype PubMed 11067867PubMed 12163459PubMed 16670300. Source: MGI positive regulation of calcium-mediated signaling Inferred from mutant phenotype PubMed 11435465. Source: MGI positive regulation of germinal center formation Inferred from mutant phenotype PubMed 14607964. Source: MGI positive regulation of heart rate Inferred from mutant phenotype PubMed 16626672. Source: MGI positive regulation of smooth muscle contraction Inferred from mutant phenotype PubMed 18340377. Source: MGI purine nucleotide salvage Inferred from electronic annotation. Source: Compara purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro regulation of cell-cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to morphine Inferred from electronic annotation. Source: Compara trophectodermal cell differentiation Inferred from mutant phenotype PubMed 9272950. Source: MGI xanthine biosynthetic process Inferred from mutant phenotype PubMed 10720488. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic membrane-bounded vesicle lumen Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome dendrite cytoplasm Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular space Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	adenosine deaminase activity Inferred from direct assay Ref.13. Source: UniProtKB purine nucleoside binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 352

351

Adenosine deaminase

PRO_0000194353

Sites

Active site

217

1

Proton donor Probable

Metal binding

15

1

Zinc; catalytic

Metal binding

17

1

Zinc; catalytic

Metal binding

214

1

Zinc; catalytic

Metal binding

295

1

Zinc; catalytic

Binding site

17

1

Substrate

Binding site

19

1

Substrate

Binding site

184

1

Substrate; via amide nitrogen and carbonyl oxygen

Binding site

296

1

Substrate

Site

238

1

Important for catalytic activity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

54

1

N6-acetyllysine By similarity

Modified residue

232

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

217

1

E → D: Reduces catalytic activity 700-fold. No effect on affinity for adenosine. Ref.9

Mutagenesis

217

1

E → G: Reduces catalytic activity 3200-fold. No effect on affinity for adenosine. Ref.9

Mutagenesis

217

1

E → Q: Reduces catalytic activity 4800-fold, and slighly increases affinity for substrate. Ref.9

Mutagenesis

217

1

E → S: Loss of activity. Ref.9

Mutagenesis

238

1

H → A: Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold. Ref.14

Mutagenesis

238

1

H → E: Nearly abolishes enzyme activity. Ref.14

Mutagenesis

238

1

H → R: Reduces enzyme activity 1500-fold. No effect on affinity for adenosine. Ref.14

Mutagenesis

295

1

D → E: No effect on affinity for adenosine. Reduces enzyme activity 2750-fold. Ref.13

Mutagenesis

296

1

D → A: Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold. Ref.13

Mutagenesis

296

1

D → N: Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold. Ref.13

Sequence conflict

141

1

E → R in AAB07142. Ref.2

Secondary structure

1

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352

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Helix

18 – 20

3

Helix

24 – 34

11

Helix

43 – 50

8

Helix

58 – 62

5

Helix

65 – 72

8

Helix

76 – 92

17

Beta strand

95 – 102

8

Helix

105 – 107

3

Beta strand

109 – 111

3

Helix

116 – 118

3

Helix

126 – 144

19

Beta strand

147 – 155

9

Helix

159 – 161

3

Helix

162 – 171

10

Turn

174 – 176

3

Beta strand

177 – 184

8

Helix

191 – 193

3

Helix

195 – 207

13

Beta strand

210 – 219

10

Helix

221 – 229

9

Beta strand

234 – 238

5

Helix

240 – 244

5

Helix

246 – 254

9

Beta strand

258 – 261

4

Helix

263 – 268

6

Beta strand

270 – 272

3

Helix

279 – 285

7

Beta strand

289 – 292

4

Helix

297 – 300

4

Helix

304 – 315

12

Helix

319 – 332

14

Beta strand

333 – 335

3

Helix

337 – 350

14

Sequences

	Sequence		Length	Mass (Da)
	P03958 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E53A8A1FABA148CD	FASTA	352	39,992
	10 20 30 40 50 60 MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII GMDKPLSLPG 70 80 90 100 110 120 FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVDPMPWNQT 130 140 150 160 170 180 EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS ILCCMRHQPS WSLEVLELCK KYNQKTVVAM 190 200 210 220 230 240 DLAGDETIEG SSLFPGHVEA YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY 250 260 270 280 290 300 HTIEDEALYN RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF 310 320 330 340 350 KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE YQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli." Yeung C.-Y., Ingolia D.E., Roth D.B., Shoemaker C., Al-Ubaidi M.R., Yen J.-Y., Ching C., Bobonis C., Kaufman R.J., Kellems R.E. J. Biol. Chem. 260:10299-10307(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural and functional analysis of the murine adenosine deaminase gene." Al-Ubaidi M.R., Ramamurthy V., Maa M.C., Ingolia D.E., Chinsky J.M., Martin B.D., Kellems R.E. Genomics 7:476-485(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The comparative sequence analysis of murine and human ADA genes." Xu P., Winston J.W., Lu J., Muzny D.M., Gibbs R.A., Kellems R.E. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[5]	"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: Tongue.
[6]	"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: Mammary tumor.
[7]	"Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death." Migchielsen A.A., Breuer M.L., van Roon M.A., te Riele H., Zurcher C., Ossendorp F., Toutain S., Hershfield M.S., Berns A., Valerio D. Nat. Genet. 10:279-287(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[8]	"Disruption of the adenosine deaminase gene causes hepatocellular impairment and perinatal lethality in mice." Wakamiya M., Blackburn M.R., Jurecic R., McArthur M.J., Geske R.S., Cartwright J. Jr., Mitani K., Vaishnav S., Belmont J.W., Kellems R.E., Finegold M.J., Montgomery C.A. Jr., Bradley A., Caskey C.T. Proc. Natl. Acad. Sci. U.S.A. 92:3673-3677(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[9]	"Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase." Mohamedali K.A., Kurz L.C., Rudolph F.B. Biochemistry 35:1672-1680(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLU-217, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE, PROPOSED ENZYME MECHANISM.
[10]	"Adenosine deaminase in rodent median eminence: detection by antibody to the mouse enzyme and co-localization with adenosine deaminase-complexing protein (CD26)." Nagy J.I., Yamamoto T., Uemura H., Schrader W.P. Neuroscience 73:459-471(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]	"Metabolic consequences of adenosine deaminase deficiency in mice are associated with defects in alveogenesis, pulmonary inflammation, and airway obstruction." Blackburn M.R., Volmer J.B., Thrasher J.L., Zhong H., Crosby J.R., Lee J.J., Kellems R.E. J. Exp. Med. 192:159-170(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[12]	"Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations." Wilson D.K., Rudolph F.B., Quiocho F.A. Science 252:1278-1284(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TRANSITION STATE ANALOG 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE, COFACTOR, PROPOSED ENZYME MECHANISM.
[13]	"Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase." Sideraki V., Mohamedali K.A., Wilson D.K., Chang Z., Kellems R.E., Quiocho F.A., Rudolph F.B. Biochemistry 35:7862-7872(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-352 OF MUTANTS GLU-295 AND ALA-296 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-295 AND ASP-296.
[14]	"Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation." Sideraki V., Wilson D.K., Kurz L.C., Quiocho F.A., Rudolph F.B. Biochemistry 35:15019-15028(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS ALA-238 AND GLU-238 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, MUTAGENESIS OF HIS-238.
[15]	"Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity." Wang Z., Quiocho F.A. Biochemistry 37:8314-8324(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND INHIBITOR, COFACTOR, ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M10319 mRNA. Translation: AAA37173.1.
M34251 , M34242, M34243, M34244, M34246, M34247, M34248, M34249, M34250 Genomic DNA. Translation: AAB07142.1.
U73107 Genomic DNA. Translation: AAC08442.1.
AF483480 mRNA. Translation: AAL90754.1.
AF483481 mRNA. Translation: AAL90755.1.
AK075899 mRNA. Translation: BAC36039.1.
BC002075 mRNA. Translation: AAH02075.1.

IPI

IPI00261467.

PIR

DUMSA. A01010.

RefSeq

NP_001258981.1. NM_001272052.1.
NP_031424.1. NM_007398.4.

UniGene

Mm.388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4L	X-ray	2.60	A/B/C/D	4-352	[»]
1A4M	X-ray	1.95	A/B/C/D	4-352	[»]
1ADD	X-ray	2.40	A	4-352	[»]
1FKW	X-ray	2.40	A	4-352	[»]
1FKX	X-ray	2.40	A	4-352	[»]
1UIO	X-ray	2.40	A	4-352	[»]
1UIP	X-ray	2.40	A	4-352	[»]
2ADA	X-ray	2.40	A	1-352	[»]
3KM8	X-ray	2.00	A/B	1-352	[»]
3MVI	X-ray	1.60	A/B	4-352	[»]
3MVT	X-ray	2.20	A/C	4-352	[»]
3T1G	X-ray	2.35	A	4-352	[»]

ProteinModelPortal

P03958.

SMR

P03958. Positions 4-352.

ModBase

Search...

PTM databases

PhosphoSite

P03958.

2D gel databases

REPRODUCTION-2DPAGE

P03958.

Proteomic databases

PaxDb

P03958.

PRIDE

P03958.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697.

GeneID

11486.

KEGG

mmu:11486.

Organism-specific databases

CTD

100.

MGI

MGI:87916. Ada.

Phylogenomic databases

eggNOG

COG1816.

HOGENOM

HOG000218816.

HOVERGEN

HBG001718.

InParanoid

P03958.

KO

K01488.

OMA

MPAIAGC.

OrthoDB

EOG40K808.

Gene expression databases

ArrayExpress

P03958.

Bgee

P03958.

CleanEx

MM_ADA.

Genevestigator

P03958.

GermOnline

ENSMUSG00000017697. Mus musculus.

Family and domain databases

InterPro

IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006330. Ado/ade_deaminase.
[Graphical view]

Pfam

PF00962. A_deaminase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01430. aden_deam. 1 hit.

PROSITE

PS00485. A_DEAMINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P03958.

ChEMBL

CHEMBL3206.

ChiTaRS

ADA. mouse.

EvolutionaryTrace

P03958.

NextBio

278844.

SOURCE

Search...

Entry information

Entry name

ADA_MOUSE

Accession

Primary (citable) accession number: P03958

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program