Reviewed, UniProtKB/Swiss-Prot P03958 (ADA_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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)

Catalytic activity	Adenosine + H2O = inosine + NH3.
Tissue specificity	Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	Peyer's patch development Inferred from mutant phenotype. Source: MGI adenosine catabolic process Ref.2 Inferred from direct assay. Source: MGI dATP catabolic process Inferred from direct assay. Source: MGI deoxyadenosine catabolic process Inferred from direct assay. Source: MGI embryonic gut development Inferred from mutant phenotype. Source: MGI germinal center B cell differentiation Inferred from mutant phenotype. Source: MGI hypoxanthine biosynthetic process Inferred from mutant phenotype. Source: MGI inosine biosynthetic process Inferred from direct assay. Source: MGI liver development Inferred from mutant phenotype. Source: MGI lung alveolus development Inferred from mutant phenotype. Source: MGI negative regulation of inflammatory response Inferred from mutant phenotype. Source: MGI negative regulation of leukocyte migration Inferred from genetic interaction. Source: MGI negative regulation of mature B cell apoptosis Inferred from mutant phenotype. Source: MGI negative regulation of mucus secretion Inferred from genetic interaction. Source: MGI negative regulation of penile erection Inferred from mutant phenotype. Source: MGI negative regulation of thymocyte apoptosis Inferred from mutant phenotype. Source: MGI placenta development Inferred from mutant phenotype. Source: MGI positive regulation of B cell proliferation Inferred from mutant phenotype. Source: MGI positive regulation of T cell differentiation in the thymus Inferred from mutant phenotype. Source: MGI positive regulation of T cell receptor signaling pathway Inferred from mutant phenotype. Source: MGI positive regulation of alpha-beta T cell differentiation Inferred from mutant phenotype. Source: MGI positive regulation of calcium-mediated signaling Inferred from mutant phenotype. Source: MGI positive regulation of germinal center formation Inferred from mutant phenotype. Source: MGI positive regulation of heart rate Inferred from mutant phenotype. Source: MGI positive regulation of smooth muscle contraction Inferred from mutant phenotype. Source: MGI purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro trophectodermal cell differentiation Inferred from mutant phenotype. Source: MGI xanthine biosynthetic process Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI
Molecular function	adenosine deaminase activity Ref.2 Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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

Ref.7

Active site

238

1

Ref.7

Active site

295

1

Ref.7

Metal binding

15

1

Zinc

Metal binding

17

1

Zinc

Metal binding

214

1

Zinc

Metal binding

295

1

Zinc

Binding site

19

1

Substrate

Binding site

184

1

Substrate; via amide nitrogen

Binding site

296

1

Substrate

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

Sequence conflict

141

1

E → R in AAB07142. Ref.2

Secondary structure

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352

Helix Strand Turn

Details...

Beta strand

11 – 17

7

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

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

269 – 272

4

Helix

279 – 285

7

Beta strand

290 – 292

3

Turn

297 – 301

5

Helix

304 – 313

10

Turn

314 – 316

3

Helix

319 – 331

13

Helix

337 – 350

14

Sequences

	Sequence		Length	Mass (Da)
	P03958-1 [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: 2410423] [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: 2387582] [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: 11471062] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[7]	"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: 1925539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), ACTIVE SITES GLU-217; HIS-238 AND ASP-295, SUBSTRATE-BINDING SITES ASP-19; GLY-184 AND ASP-296, ZINC-BINDING SITES HIS-15; HIS-17; HIS-214 AND ASP-295.
[8]	"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: 8942668] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[9]	"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: 9622483] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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_031424.1.

UniGene

Mm.388

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P03958.

PTM databases

PhosphoSite

P03958.

2-D gel databases

REPRODUCTION-2DPAGE

P03958.

Proteomic databases

PRIDE

P03958.

Genome annotation databases

Ensembl

ENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697; Mus musculus. [Genome view]

GeneID

11486.

KEGG

mmu:11486.

UCSC

uc008ntl.1. mouse.

Organism-specific databases

CTD

11486.

MGI

MGI:87916. Ada.

Phylogenomic databases

HOGENOM

P03958.

HOVERGEN

P03958.

OMA

CLLRHLP.

Enzyme and pathway databases

BRENDA

3.5.4.4. 244.

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.
IPR006330. A_deaminase.
[Graphical view]

PANTHER

PTHR11409. A/AMP_deaminase. 1 hit.

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 Resources

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:	November 3, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)