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UniProtKB/Swiss-Prot entry P03958


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADA_MOUSE
Primary accession number P03958
Secondary accession numbers None
Integrated into Swiss-Prot on October 23, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 91)
Name and origin of the protein
Protein name Adenosine deaminase
Synonyms EC 3.5.4.4
Adenosine aminohydrolase
Gene name
Name: Ada
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2410423 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli.";
J. Biol. Chem. 260:10299-10307(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(90)90189-2; PubMed=2387582 [NCBI, ExPASy, EBI, Israel, Japan]
Al-Ubaidi M.R., Ramamurthy V., Maa M.C., Ingolia D.E., Chinsky J.M., Martin B.D., Kellems R.E.;
"Structural and functional analysis of the murine adenosine deaminase gene.";
Genomics 7:476-485(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Xu P., Winston J.W., Lu J., Muzny D.M., Gibbs R.A., Kellems R.E.;
"The comparative sequence analysis of murine and human ADA genes.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ILS, and ISS;
DOI=10.1007/s00335-001-1001-x; PubMed=11471062 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"High-throughput sequence identification of gene coding variants within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
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, AND ZINC-BINDING SITES HIS-15; HIS-17; HIS-214 AND ASP-295.
PubMed=1925539 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson D.K., Rudolph F.B., Quiocho F.A.;
"Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.";
Science 252:1278-1284(1991).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi961427e; PubMed=8942668 [NCBI, ExPASy, EBI, Israel, Japan]
Sideraki V., Wilson D.K., Kurz L.C., Quiocho F.A., Rudolph F.B.;
"Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation.";
Biochemistry 35:15019-15028(1996).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1021/bi980324o; PubMed=9622483 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Z., Quiocho F.A.;
"Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity.";
Biochemistry 37:8314-8324(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M10319; AAA37173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34251; AAB07142.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34242; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34243; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34244; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34246; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34247; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34248; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34249; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34250; AAB07142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73107; AAC08442.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF483480; AAL90754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF483481; AAL90755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075899; BAC36039.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002075; AAH02075.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01010; DUMSA.
RefSeq NP_031424.1; -.
UniGene Mm.388
3D structure databases
PDB
1A4L; X-ray; 2.60 A; A/B/C/D=4-352.[ExPASy / RCSB / EBI]
1A4M; X-ray; 1.95 A; A/B/C/D=4-352.[ExPASy / RCSB / EBI]
1ADD; X-ray; 2.40 A; A=4-352.[ExPASy / RCSB / EBI]
1FKW; X-ray; 2.40 A; A=4-352.[ExPASy / RCSB / EBI]
1FKX; X-ray; 2.40 A; A=4-352.[ExPASy / RCSB / EBI]
1UIO; X-ray; 2.40 A; A=4-352.[ExPASy / RCSB / EBI]
1UIP; X-ray; 2.40 A; A=4-352.[ExPASy / RCSB / EBI]
2ADA; X-ray; 2.40 A; A=1-352.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A4L; -.
1A4M; -.
1ADD; -.
1FKW; -.
1FKX; -.
1UIO; -.
1UIP; -.
2ADA; -.
ModBase P03958.
2D gel databases
REPRODUCTION-2DPAGE P03958; -.
Organism-specific databases
MGI MGI:87916; Ada.
Gene expression databases
ArrayExpress P03958; -.
CleanEx MM_ADA; -.
GermOnline ENSMUSG00000017697; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0004000; Molecular function: adenosine deaminase activity (inferred from direct assay from MGI).
GO:0006154; Biological process: adenosine catabolic process (inferred from direct assay from MGI).
GO:0046061; Biological process: dATP catabolic process (inferred from direct assay from MGI).
GO:0006157; Biological process: deoxyadenosine catabolic process (inferred from direct assay from MGI).
GO:0048566; Biological process: embryonic gut development (inferred from mutant phenotype from MGI).
GO:0046103; Biological process: inosine biosynthetic process (inferred from direct assay from MGI).
GO:0001889; Biological process: liver development (inferred from mutant phenotype from MGI).
GO:0030324; Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from MGI).
GO:0001890; Biological process: placenta development (inferred from mutant phenotype from MGI).
GO:0045582; Biological process: positive regulation of T cell differentiation (inferred from mutant phenotype from MGI).
GO:0001829; Biological process: trophectodermal cell differentiation (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR006650; A/AMP_deam_AS.
IPR001365; A/AMP_deaminase.
IPR006330; A_deaminase.
Graphical view of domain structure.
PANTHER PTHR11409; A/AMP_deaminase; 1.
Pfam PF00962; A_deaminase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01430; aden_deam; 1.
PROSITE PS00485; A_DEAMINASE; 1.
BLOCKS P03958.
ProtoNet P03958.
Other
SWISS-3DIMAGE P03958.
Genome annotation databases
Ensembl ENSMUSG00000017697; Mus musculus. [Contig view]
GeneID 11486; -.
KEGG mmu:11486; -.
Phylogenomic databases
HOGENOM P03958; -.
HOVERGEN P03958; -.
Other
LinkHub P03958; -.
NextBio 278844; -.
SOURCE Ada; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Hydrolase; Metal-binding; Nucleotide metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   352  351     Adenosine deaminase. PRO_0000194353
ACT_SITE   217   217         
ACT_SITE   238   238         
ACT_SITE   295   295         
METAL   15    15        Zinc. 
METAL   17    17        Zinc. 
METAL   214   214        Zinc. 
METAL   295   295        Zinc. 
BINDING   19    19        Substrate. 
BINDING   184   184        Substrate; via amide nitrogen. 
BINDING   296   296        Substrate. 
MOD_RES   2     2        N-acetylalanine (By similarity). 
CONFLICT   141   141        E -> R (in Ref. 2; AAB07142). 
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      
STRAND   95   102  8      
HELIX   105   107  3      
HELIX   116   118  3      
HELIX   126   144  19      
STRAND   147   155  9      
HELIX   159   161  3      
HELIX   162   171  10      
TURN   174   176  3      
STRAND   177   184  8      
HELIX   191   193  3      
HELIX   195   207  13      
STRAND   210   219  10      
HELIX   221   229  9      
STRAND   234   238  5      
HELIX   240   244  5      
HELIX   246   254  9      
STRAND   258   261  4      
HELIX   263   268  6      
STRAND   269   272  4      
HELIX   279   285  7      
STRAND   290   292  3      
TURN   297   301  5      
HELIX   304   313  10      
TURN   314   316  3      
HELIX   319   331  13      
HELIX   337   350  14      
Sequence information
Length: 352 AA [This is the length of the unprocessed precursor] Molecular weight: 39992 Da [This is the MW of the unprocessed precursor] CRC64: E53A8A1FABA148CD [This is a checksum on the sequence]
        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 

P03958 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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