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Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase)

 ADA_HUMAN               Reviewed;         363 AA.
P00813; Q53F92; Q6LA59;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 211.
RecName: Full=Adenosine deaminase;
EC=3.5.4.4 {ECO:0000269|PubMed:16670267, ECO:0000269|PubMed:23193172, ECO:0000269|PubMed:8452534};
AltName: Full=Adenosine aminohydrolase;
Name=ADA; Synonyms=ADA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6090454;
Daddona P.E., Shewach D.S., Kelley W.N., Argos P., Markham A.F.,
Orkin S.H.;
"Human adenosine deaminase. cDNA and complete primary amino acid
sequence.";
J. Biol. Chem. 259:12101-12106(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6546794; DOI=10.1093/nar/12.5.2439;
Wiginton D.A., Adrian G.S., Hutton J.J.;
"Sequence of human adenosine deaminase cDNA including the coding
region and a small intron.";
Nucleic Acids Res. 12:2439-2446(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3839456;
Valerio D., Duyvesteyn M.G.C., Dekker B.M.M., Weeda G., Berkvens T.M.,
van der Voorn L., van Ormondt H., van der Eb A.J.;
"Adenosine deaminase: characterization and expression of a gene with a
remarkable promoter.";
EMBO J. 4:437-443(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3028473; DOI=10.1021/bi00373a017;
Wiginton D.A., Kaplan D.J., States J.C., Akeson A.L., Perme C.M.,
Bilyk I.J., Vaughn A.J., Lattier D.L., Hutton J.J.;
"Complete sequence and structure of the gene for human adenosine
deaminase.";
Biochemistry 25:8234-8244(1986).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (AUG-2004) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 141-363.
PubMed=6688808;
Orkin S.H., Daddona P.E., Shewach D.S., Markham A.F., Bruns G.A.,
Goff S.C., Kelley W.N.;
"Molecular cloning of human adenosine deaminase gene sequences.";
J. Biol. Chem. 258:12753-12756(1983).
[10]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=8452534; DOI=10.1042/bj2900457;
Lindley E.R., Pisoni R.L.;
"Demonstration of adenosine deaminase activity in human fibroblast
lysosomes.";
Biochem. J. 290:457-462(1993).
[11]
INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION.
PubMed=8101391; DOI=10.1126/science.8101391;
Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.;
"Direct association of adenosine deaminase with a T cell activation
antigen, CD26.";
Science 261:466-469(1993).
[12]
INTERACTION WITH DPP4.
PubMed=7907293; DOI=10.1002/eji.1830240311;
De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E.,
Gigase P., Scharpe S.;
"Binding of adenosine deaminase to the lymphocyte surface via CD26.";
Eur. J. Immunol. 24:566-570(1994).
[13]
INTERACTION WITH DPP4.
PubMed=10951221; DOI=10.1046/j.1432-1327.2000.01634.x;
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R.,
Haemers A., Scharpe S., De Meester I.;
"Molecular characterization of dipeptidyl peptidase activity in serum:
soluble CD26/dipeptidyl peptidase IV is responsible for the release of
X-Pro dipeptides.";
Eur. J. Biochem. 267:5608-5613(2000).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11772392; DOI=10.1042/0264-6021:3610203;
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C.,
Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.;
"Regulation of epithelial and lymphocyte cell adhesion by adenosine
deaminase-CD26 interaction.";
Biochem. J. 361:203-209(2002).
[15]
FUNCTION, AND INTERACTION WITH DPP4 AND PLG.
PubMed=15016824; DOI=10.1074/jbc.M401023200;
Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.;
"Cell surface adenosine deaminase binds and stimulates plasminogen
activation on 1-LN human prostate cancer cells.";
J. Biol. Chem. 279:20993-20998(2004).
[16]
INTERACTION WITH DPP4.
PubMed=14691230; DOI=10.1110/ps.03352504;
Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E.,
Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.;
"N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on
enzyme activity, homodimer formation, and adenosine deaminase
binding.";
Protein Sci. 13:145-154(2004).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY HYPOXIA.
PubMed=16670267; DOI=10.1182/blood-2006-02-001016;
Eltzschig H.K., Faigle M., Knapp S., Karhausen J., Ibla J.,
Rosenberger P., Odegard K.C., Laussen P.C., Thompson L.F.,
Colgan S.P.;
"Endothelial catabolism of extracellular adenosine during hypoxia: the
role of surface adenosine deaminase and CD26.";
Blood 108:1602-1610(2006).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20959412; DOI=10.1189/jlb.1009696;
Martinez-Navio J.M., Casanova V., Pacheco R., Naval-Macabuhay I.,
Climent N., Garcia F., Gatell J.M., Mallol J., Gallart T., Lluis C.,
Franco R.;
"Adenosine deaminase potentiates the generation of effector, memory,
and regulatory CD4+ T cells.";
J. Leukoc. Biol. 89:127-136(2011).
[22]
FUNCTION.
PubMed=21919946; DOI=10.1111/j.1439-0272.2011.01231.x;
Rostampour F., Biglari M., Vaisi-Raygani A., Salimi S., Tavilani H.;
"Adenosine deaminase activity in fertile and infertile men.";
Andrologia 44:586-589(2012).
[23]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF LEU-58; ASP-60; PHE-61; LEU-62; LYS-64; PHE-65; ASP-66;
MET-69; ILE-115; ASN-118; MET-155; HIS-157; GLY-184; ASP-185 AND
LEU-194.
PubMed=23193172; DOI=10.1096/fj.12-212621;
Gracia E., Farre D., Cortes A., Ferrer-Costa C., Orozco M., Mallol J.,
Lluis C., Canela E.I., McCormick P.J., Franco R., Fanelli F.,
Casado V.;
"The catalytic site structural gate of adenosine deaminase
allosterically modulates ligand binding to adenosine receptors.";
FASEB J. 27:1048-1061(2013).
[24]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 5-363 IN COMPLEX WITH NICKEL
IONS AND 2-DEAOXYADENOSINE, AND COFACTOR.
Structural genomics consortium (SGC);
"The crystal structure of human adenosine deaminase.";
Submitted (AUG-2009) to the PDB data bank.
[25]
VARIANTS ADASCID TRP-76; PRO-107; GLN-149; CYS-211; THR-215 AND
LEU-274.
PubMed=2166947; DOI=10.1073/pnas.87.16.6171;
Hirschhorn R., Tzall S., Ellenbogen A.;
"Hot spot mutations in adenosine deaminase deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 87:6171-6175(1990).
[26]
VARIANT ADA*2 ASN-8.
PubMed=8031011; DOI=10.1111/j.1469-1809.1994.tb00720.x;
Hirschhorn R., Yang D.R., Israni A.;
"An Asp8Asn substitution results in the adenosine deaminase (ADA)
genetic polymorphism (ADA 2 allozyme): occurrence on different
chromosomal backgrounds and apparent intragenic crossover.";
Ann. Hum. Genet. 58:1-9(1994).
[27]
VARIANTS ADASCID.
PubMed=6208479; DOI=10.1128/MCB.4.9.1712;
Adrian G.S., Wiginton D.A., Hutton J.;
"Structure of adenosine deaminase mRNAs from normal and adenosine
deaminase-deficient human cell lines.";
Mol. Cell. Biol. 4:1712-1717(1984).
[28]
VARIANT ADASCID GLN-101.
PubMed=3839802; DOI=10.1172/JCI112050;
Bonthron D.T., Markham A.F., Ginsburg D., Orkin S.H.;
"Identification of a point mutation in the adenosine deaminase gene
responsible for immunodeficiency.";
J. Clin. Invest. 76:894-897(1985).
[29]
VARIANTS ADASCID TRP-101; HIS-211 AND VAL-329.
PubMed=3182793;
Akeson A.L., Wiginton D.A., Dusing M.R., States J.C., Hutton J.J.;
"Mutant human adenosine deaminase alleles and their expression by
transfection into fibroblasts.";
J. Biol. Chem. 263:16291-16296(1988).
[30]
VARIANT ADASCID GLN-297.
PubMed=2783588; DOI=10.1172/JCI113909;
Hirschhorn R., Tzall S., Ellenbogen A., Orkin S.H.;
"Identification of a point mutation resulting in a heat-labile
adenosine deaminase (ADA) in two unrelated children with partial ADA
deficiency.";
J. Clin. Invest. 83:497-501(1989).
[31]
VARIANTS ADASCID CYS-156 AND LEU-291.
PubMed=1284479; DOI=10.1002/humu.1380010214;
Hirschhorn R.;
"Identification of two new missense mutations (R156C and S291L) in two
ADA-SCID patients unusual for response to therapy with partial
exchange transfusions.";
Hum. Mutat. 1:166-168(1992).
[32]
VARIANTS ADASCID LEU-101; HIS-156; MET-177; ARG-216 AND LEU-291.
PubMed=8227344; DOI=10.1172/JCI116833;
Santisteban I., Arredondo-Vega F.X., Kelly S., Mary A., Fischer A.,
Hummell D.S., Lawton A., Sorensen R.U., Stiehm E.R., Uribe L.,
Weinberg K., Hershfield M.S.;
"Novel splicing, missense, and deletion mutations in seven adenosine
deaminase-deficient patients with late/delayed onset of combined
immunodeficiency disease. Contribution of genotype to phenotype.";
J. Clin. Invest. 92:2291-2302(1993).
[33]
VARIANT ADASCID ARG-20.
PubMed=8299233; DOI=10.1006/clin.1994.1026;
Yang D.R., Huie M.L., Hirschhorn R.;
"Homozygosity for a missense mutation (G20R) associated with neonatal
onset adenosine deaminase-deficient severe combined immunodeficiency
(ADA-SCID).";
Clin. Immunol. Immunopathol. 70:171-175(1994).
[34]
VARIANTS ARG-80 AND GLN-142.
PubMed=8589684; DOI=10.1093/hmg/4.11.2081;
Santisteban I., Arredondo-Vega F.X., Kelly S., Loubser M., Meydan N.,
Roifman C., Howell P.L., Bowen T., Weinberg K.I., Schroeder M.L.,
Hershfield M.S.;
"Three new adenosine deaminase mutations that define a splicing
enhancer and cause severe and partial phenotypes: implications for
evolution of a CpG hotspot and expression of a transduced ADA cDNA.";
Hum. Mol. Genet. 4:2081-2087(1995).
[35]
VARIANTS ADASCID ASP-15; ASP-83 AND ASP-179.
PubMed=7599635; DOI=10.1002/humu.1380050309;
Santisteban I., Arredondo-Vega F.X., Kelly S., Debre M., Fisher A.,
Perignon J.L., Hilman B., Eldahr J., Dreyfus D.H., Gelfand E.W.,
Howell P.L., Hershfield M.S.;
"Four new adenosine deaminase mutations, altering a zinc-binding
histidine, two conserved alanines, and a 5' splice site.";
Hum. Mutat. 5:243-250(1995).
[36]
VARIANTS MET-152 AND ILE-233.
PubMed=9225964; DOI=10.1007/s004390050460;
Hirschhorn R., Borkowsky W., Jiang C.-K., Yang D.R., Jenkins T.;
"Two newly identified mutations (Thr233Ile and Leu152Met) in partially
adenosine deaminase-deficient (ADA-) individuals that result in
differing biochemical and metabolic phenotypes.";
Hum. Genet. 100:22-29(1997).
[37]
VARIANTS ADASCID CYS-97 AND VAL-106, CHARACTERIZATION OF VARIANTS
ADASCID CYS-97; VAL-106; CYS-211 AND THR-215, AND CHARACTERIZATION OF
VARIANT ILE-233.
PubMed=9361033; DOI=10.1093/hmg/6.13.2271;
Jiang C., Hong R., Horowitz S.D., Kong X., Hirschhorn R.;
"An adenosine deaminase (ADA) allele contains two newly identified
deleterious mutations (Y97C and L106V) that interact to abolish enzyme
activity.";
Hum. Mol. Genet. 6:2271-2278(1997).
[38]
VARIANTS ADASCID CYS-74; MET-129; GLU-140; TRP-149 AND PRO-199.
PubMed=10200056;
DOI=10.1002/(SICI)1098-1004(1998)11:6<482::AID-HUMU14>3.3.CO;2-8;
Arrendondo-Vega F.X., Santisteban I., Notarangelo L.D., El Dahr J.,
Buckley R., Roifman C., Conley M.E., Hershfield M.S.;
"Seven novel mutations in the adenosine deaminase (ADA) gene in
patients with severe and delayed onset combined immunodeficiency:
G74C, V129M, G140E, R149W, Q199P, 462delG, and E337del.";
Hum. Mutat. 11:482-482(1998).
[39]
EFFECT OF VARIANT ADA*2 ASN-8 ON SLEEP.
PubMed=16221767; DOI=10.1073/pnas.0505414102;
Retey J.V., Adam M., Honegger E., Khatami R., Luhmann U.F.O.,
Jung H.H., Berger W., Landolt H.-P.;
"A functional genetic variation of adenosine deaminase affects the
duration and intensity of deep sleep in humans.";
Proc. Natl. Acad. Sci. U.S.A. 102:15676-15681(2005).
[40]
VARIANT [LARGE SCALE ANALYSIS] GLN-142.
PubMed=18772397; DOI=10.1126/science.1164368;
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B.,
Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
"Core signaling pathways in human pancreatic cancers revealed by
global genomic analyses.";
Science 321:1801-1806(2008).
[41]
VARIANT ADA*2 ASN-8, AND CHARACTERIZATION OF VARIANT ASN-8.
PubMed=21734253; DOI=10.1093/cercor/bhr173;
Bachmann V., Klaus F., Bodenmann S., Schaefer N., Brugger P.,
Huber S., Berger W., Landolt H.P.;
"Functional ADA polymorphism increases sleep depth and reduces
vigilant attention in humans.";
Cereb. Cortex 22:962-970(2012).
[42]
VARIANT ADA*2 ASN-8, CHARACTERIZATION OF VARIANT ASN-8, AND FUNCTION.
PubMed=26166670; DOI=10.1016/j.urology.2015.06.034;
Fattahi A., Khodadadi I., Amiri I., Latifi Z., Ghorbani M.,
Tavilani H.;
"The Role of G22 A Adenosine Deaminase 1 Gene Polymorphism and the
Activities of ADA Isoenzymes in Fertile and Infertile Men.";
Urology 86:730-734(2015).
-!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
deoxyadenosine (PubMed:8452534, PubMed:16670267). 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
(PubMed:20959412). Its interaction with DPP4 regulates lymphocyte-
epithelial cell adhesion (PubMed:11772392). Enhances dendritic
cell immunogenicity by affecting dendritic cell costimulatory
molecule expression and cytokines and chemokines secretion (By
similarity). Enhances CD4+ T-cell differentiation and
proliferation (PubMed:20959412). Acts as a positive modulator of
adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand
affinity via conformational change (PubMed:23193172). Stimulates
plasminogen activation (PubMed:15016824). Plays a role in male
fertility (PubMed:21919946, PubMed:26166670). Plays a protective
role in early postimplantation embryonic development (By
similarity). {ECO:0000250|UniProtKB:P03958,
ECO:0000250|UniProtKB:P56658, ECO:0000269|PubMed:11772392,
ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:16670267,
ECO:0000269|PubMed:20959412, ECO:0000269|PubMed:21919946,
ECO:0000269|PubMed:23193172, ECO:0000269|PubMed:26166670,
ECO:0000269|PubMed:8452534}.
-!- CATALYTIC ACTIVITY: Adenosine + H(2)O = inosine + NH(3).
{ECO:0000269|PubMed:16670267, ECO:0000269|PubMed:23193172,
ECO:0000269|PubMed:8452534}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000305|Ref.24};
Note=Binds 1 zinc ion per subunit. {ECO:0000305|Ref.24};
-!- ENZYME REGULATION: Inhibited by Cu(2+) and Hg(2+), coformycin,
deoxycoformycin (dCF), 2-deoxyadenosine, 6-methylaminopurine
riboside, 2-3-iso-propylidene-adenosine and erythro-9-(2-hydroxy-
3-nonyl)adenine. {ECO:0000269|PubMed:16670267,
ECO:0000269|PubMed:8452534}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=37 uM for adenosine (at 25 degrees Celsius and pH 5.5)
{ECO:0000269|PubMed:8452534};
Vmax=41 umol/min/mg enzyme {ECO:0000269|PubMed:23193172};
-!- SUBUNIT: Interacts with DPP4 (via extracellular domain)
(PubMed:10951221, PubMed:14691230, PubMed:7907293, PubMed:8101391,
PubMed:15016824). Interacts with PLG (via Kringle 4 domain); the
interaction stimulates PLG activation when in complex with DPP4
(PubMed:15016824). {ECO:0000269|PubMed:10951221,
ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:15016824,
ECO:0000269|PubMed:7907293, ECO:0000269|PubMed:8101391}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11772392,
ECO:0000269|PubMed:8101391}; Peripheral membrane protein;
Extracellular side. Cell junction {ECO:0000269|PubMed:11772392}.
Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}.
Cytoplasm {ECO:0000250}. Lysosome {ECO:0000269|PubMed:8452534}.
Note=Colocalized with DPP4 at the cell surface.
{ECO:0000269|PubMed:11772392}.
-!- TISSUE SPECIFICITY: Found in all tissues, occurs in large amounts
in T-lymphocytes (PubMed:20959412). Expressed at the time of
weaning in gastrointestinal tissues.
{ECO:0000269|PubMed:20959412}.
-!- INDUCTION: Up-regulated by hypoxia. {ECO:0000269|PubMed:16670267}.
-!- POLYMORPHISM: There is a common allele, ADA*2, also known as the
ADA 2 allozyme. It is associated with the reduced metabolism of
adenosine to inosine. It specifically enhances deep sleep and
slow-wave activity (SWA) during sleep.
{ECO:0000269|PubMed:16221767}.
-!- DISEASE: Severe combined immunodeficiency autosomal recessive T-
cell-negative/B-cell-negative/NK-cell-negative due to adenosine
deaminase deficiency (ADASCID) [MIM:102700]: An autosomal
recessive disorder accounting for about 50% of non-X-linked SCIDs.
SCID refers to a genetically and clinically heterogeneous group of
rare congenital disorders characterized by impairment of both
humoral and cell-mediated immunity, leukopenia, and low or absent
antibody levels. Patients with SCID present in infancy with
recurrent, persistent infections by opportunistic organisms. The
common characteristic of all types of SCID is absence of T-cell-
mediated cellular immunity due to a defect in T-cell development.
ADA deficiency has been diagnosed in chronically ill teenagers and
adults (late or adult onset). Population and newborn screening
programs have also identified several healthy individuals with
normal immunity who have partial ADA deficiency.
{ECO:0000269|PubMed:10200056, ECO:0000269|PubMed:1284479,
ECO:0000269|PubMed:2166947, ECO:0000269|PubMed:2783588,
ECO:0000269|PubMed:3182793, ECO:0000269|PubMed:3839802,
ECO:0000269|PubMed:6208479, ECO:0000269|PubMed:7599635,
ECO:0000269|PubMed:8227344, ECO:0000269|PubMed:8299233,
ECO:0000269|PubMed:9361033}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Adenosine and AMP deaminases family. {ECO:0000305}.
-!- WEB RESOURCE: Name=ADAbase; Note=ADA mutation db;
URL="http://structure.bmc.lu.se/idbase/ADAbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Adenosine deaminase entry;
URL="https://en.wikipedia.org/wiki/Adenosine_deaminase";
-!- WEB RESOURCE: Name=Mendelian genes adenosine deaminase (ADA);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/ADA";
-----------------------------------------------------------------------
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EMBL; X02994; CAA26734.1; -; mRNA.
EMBL; X02189; CAA26130.1; ALT_SEQ; Genomic_DNA.
EMBL; X02190; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02191; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02192; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02193; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02194; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02195; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02196; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02197; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02198; CAA26130.1; JOINED; Genomic_DNA.
EMBL; X02199; CAA26130.1; JOINED; Genomic_DNA.
EMBL; M13792; AAA78791.1; -; Genomic_DNA.
EMBL; AL139352; CAH73885.1; -; Genomic_DNA.
EMBL; Z97053; CAH73885.1; JOINED; Genomic_DNA.
EMBL; Z97053; CAB09782.2; -; Genomic_DNA.
EMBL; AL139352; CAB09782.2; JOINED; Genomic_DNA.
EMBL; AK223397; BAD97117.1; -; mRNA.
EMBL; BC007678; AAH07678.1; -; mRNA.
EMBL; BC040226; AAH40226.1; -; mRNA.
CCDS; CCDS13335.1; -.
PIR; A91032; DUHUA.
RefSeq; NP_000013.2; NM_000022.3.
UniGene; Hs.654536; -.
PDB; 1M7M; Model; -; A=1-363.
PDB; 3IAR; X-ray; 1.52 A; A=5-363.
PDBsum; 1M7M; -.
PDBsum; 3IAR; -.
ProteinModelPortal; P00813; -.
SMR; P00813; -.
BioGrid; 106614; 22.
CORUM; P00813; -.
DIP; DIP-371N; -.
IntAct; P00813; 5.
MINT; MINT-5000852; -.
STRING; 9606.ENSP00000361965; -.
BindingDB; P00813; -.
ChEMBL; CHEMBL1910; -.
DrugBank; DB07783; 1-((1R)-1-(HYDROXYMETHYL)-3-{6-[(3-PHENYLPROPANOYL)AMINO]-1H-INDOL-1-YL}PROPYL)-1H-IMIDAZOLE-4-CARBOXAMIDE.
DrugBank; DB04218; 1-Deaza-Adenosine.
DrugBank; DB00640; Adenosine.
DrugBank; DB00975; Dipyridamole.
DrugBank; DB00974; Edetic Acid.
DrugBank; DB05057; Erdosteine.
DrugBank; DB02616; FR117016.
DrugBank; DB02096; FR221647.
DrugBank; DB03572; FR230513.
DrugBank; DB03220; FR233623.
DrugBank; DB02830; FR236913.
DrugBank; DB03370; FR239087.
DrugBank; DB01280; Nelarabine.
DrugBank; DB00552; Pentostatin.
DrugBank; DB04440; Purine Riboside.
DrugBank; DB00277; Theophylline.
DrugBank; DB00194; Vidarabine.
GuidetoPHARMACOLOGY; 1230; -.
iPTMnet; P00813; -.
PhosphoSitePlus; P00813; -.
SwissPalm; P00813; -.
BioMuta; ADA; -.
DMDM; 113339; -.
EPD; P00813; -.
MaxQB; P00813; -.
PaxDb; P00813; -.
PeptideAtlas; P00813; -.
PRIDE; P00813; -.
TopDownProteomics; P00813; -.
DNASU; 100; -.
Ensembl; ENST00000372874; ENSP00000361965; ENSG00000196839.
GeneID; 100; -.
KEGG; hsa:100; -.
UCSC; uc002xmj.4; human.
CTD; 100; -.
DisGeNET; 100; -.
EuPathDB; HostDB:ENSG00000196839.12; -.
GeneCards; ADA; -.
GeneReviews; ADA; -.
HGNC; HGNC:186; ADA.
HPA; CAB004307; -.
HPA; HPA001399; -.
HPA; HPA023884; -.
MalaCards; ADA; -.
MIM; 102700; phenotype.
MIM; 608958; gene.
neXtProt; NX_P00813; -.
OpenTargets; ENSG00000196839; -.
Orphanet; 39041; Omenn syndrome.
Orphanet; 277; Severe combined immunodeficiency due to adenosine deaminase deficiency.
PharmGKB; PA24503; -.
eggNOG; KOG1097; Eukaryota.
eggNOG; COG1816; LUCA.
GeneTree; ENSGT00730000111151; -.
HOGENOM; HOG000218816; -.
HOVERGEN; HBG001718; -.
InParanoid; P00813; -.
KO; K01488; -.
OMA; HHVGSAS; -.
OrthoDB; EOG091G0NL8; -.
PhylomeDB; P00813; -.
TreeFam; TF314270; -.
BioCyc; MetaCyc:HS02191-MONOMER; -.
BRENDA; 3.5.4.4; 2681.
Reactome; R-HSA-74217; Purine salvage.
SABIO-RK; P00813; -.
SignaLink; P00813; -.
ChiTaRS; ADA; human.
EvolutionaryTrace; P00813; -.
GeneWiki; Adenosine_deaminase; -.
GenomeRNAi; 100; -.
PRO; PR:P00813; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000196839; -.
CleanEx; HS_ADA; -.
ExpressionAtlas; P00813; baseline and differential.
Genevisible; P00813; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0004000; F:adenosine deaminase activity; IDA:UniProtKB.
GO; GO:0001883; F:purine nucleoside binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
GO; GO:0006154; P:adenosine catabolic process; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0046061; P:dATP catabolic process; IEA:Ensembl.
GO; GO:0006157; P:deoxyadenosine catabolic process; IEA:Ensembl.
GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
GO; GO:0002314; P:germinal center B cell differentiation; IEA:Ensembl.
GO; GO:0001821; P:histamine secretion; IEA:Ensembl.
GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
GO; GO:0046103; P:inosine biosynthetic process; IDA:MGI.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042323; P:negative regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
GO; GO:0070256; P:negative regulation of mucus secretion; IEA:Ensembl.
GO; GO:0060407; P:negative regulation of penile erection; IEA:Ensembl.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0002636; P:positive regulation of germinal center formation; IEA:Ensembl.
GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0032261; P:purine nucleotide salvage; IMP:UniProtKB.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
GO; GO:0046111; P:xanthine biosynthetic process; IEA:Ensembl.
CDD; cd01320; ADA; 1.
HAMAP; MF_00540; A_deaminase; 1.
InterPro; IPR006650; A/AMP_deam_AS.
InterPro; IPR001365; A/AMP_deaminase_dom.
InterPro; IPR028893; A_deaminase.
InterPro; IPR006330; Ado/ade_deaminase.
InterPro; IPR032466; Metal_Hydrolase.
Pfam; PF00962; A_deaminase; 1.
SUPFAM; SSF51556; SSF51556; 1.
TIGRFAMs; TIGR01430; aden_deam; 1.
PROSITE; PS00485; A_DEAMINASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Disease mutation;
Hereditary hemolytic anemia; Hydrolase; Lysosome; Membrane;
Metal-binding; Nucleotide metabolism; Polymorphism;
Reference proteome; SCID; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 363 Adenosine deaminase.
/FTId=PRO_0000194352.
REGION 126 143 Required for binding to DDP4.
{ECO:0000269|PubMed:15016824}.
ACT_SITE 217 217 Proton donor.
{ECO:0000250|UniProtKB:P03958}.
METAL 15 15 Zinc; catalytic. {ECO:0000305|Ref.24}.
METAL 17 17 Zinc; catalytic. {ECO:0000305|Ref.24}.
METAL 214 214 Zinc; catalytic. {ECO:0000305|Ref.24}.
METAL 295 295 Zinc; catalytic. {ECO:0000305|Ref.24}.
BINDING 17 17 Substrate. {ECO:0000244|PDB:3IAR,
ECO:0000269|Ref.24}.
BINDING 19 19 Substrate. {ECO:0000244|PDB:3IAR,
ECO:0000269|Ref.24}.
BINDING 184 184 Substrate; via amide nitrogen.
{ECO:0000244|PDB:3IAR,
ECO:0000269|Ref.24}.
BINDING 296 296 Substrate. {ECO:0000244|PDB:3IAR,
ECO:0000269|Ref.24}.
SITE 58 58 Important for interaction with adenosine
receptors and increasing their affinity
for agonists.
{ECO:0000269|PubMed:23193172}.
SITE 62 62 Important for interaction with adenosine
receptors and increasing their affinity
for agonists.
{ECO:0000269|PubMed:23193172}.
SITE 238 238 Important for catalytic activity.
{ECO:0000250|UniProtKB:P03958}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8}.
MOD_RES 54 54 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 8 8 D -> N (polymorphism; allele ADA*2; found
in about 10% of the population; affects
duration and intensity of deep sleep;
enhances negative effects of sleep loss
during sleep deprivation; may have a
protective role against male infertility;
20% to 30% decrease in activity;
dbSNP:rs73598374).
{ECO:0000269|PubMed:16221767,
ECO:0000269|PubMed:21734253,
ECO:0000269|PubMed:26166670,
ECO:0000269|PubMed:8031011}.
/FTId=VAR_002209.
VARIANT 15 15 H -> D (in ADASCID; loss of activity;
dbSNP:rs121908725).
{ECO:0000269|PubMed:7599635}.
/FTId=VAR_002210.
VARIANT 20 20 G -> R (in ADASCID; loss of activity;
dbSNP:rs121908724).
{ECO:0000269|PubMed:8299233}.
/FTId=VAR_002211.
VARIANT 74 74 G -> C (in ADASCID; delayed-onset;
dbSNP:rs121908730).
{ECO:0000269|PubMed:10200056}.
/FTId=VAR_002212.
VARIANT 76 76 R -> W (in ADASCID; dbSNP:rs121908736).
{ECO:0000269|PubMed:2166947}.
/FTId=VAR_002213.
VARIANT 80 80 K -> R (in dbSNP:rs11555566).
{ECO:0000269|PubMed:8589684}.
/FTId=VAR_002214.
VARIANT 83 83 A -> D (in ADASCID; loss of activity;
dbSNP:rs121908726).
{ECO:0000269|PubMed:7599635}.
/FTId=VAR_002215.
VARIANT 97 97 Y -> C (in ADASCID; unknown pathological
significance; loss of activity on its
own; total loss of activity; when
associated with V-106;
dbSNP:rs267606634).
{ECO:0000269|PubMed:9361033}.
/FTId=VAR_076954.
VARIANT 101 101 R -> L (in ADASCID; dbSNP:rs121908714).
{ECO:0000269|PubMed:8227344}.
/FTId=VAR_002216.
VARIANT 101 101 R -> Q (in ADASCID; loss of activity;
dbSNP:rs121908714).
{ECO:0000269|PubMed:3839802}.
/FTId=VAR_002218.
VARIANT 101 101 R -> W (in ADASCID; dbSNP:rs121908717).
{ECO:0000269|PubMed:3182793}.
/FTId=VAR_002217.
VARIANT 106 106 L -> V (in ADASCID; unknown pathological
significance; 30% of activity; total loss
of activity; when associated with C-97;
dbSNP:rs267606635).
{ECO:0000269|PubMed:9361033}.
/FTId=VAR_076955.
VARIANT 107 107 L -> P (in ADASCID; dbSNP:rs121908739).
{ECO:0000269|PubMed:2166947}.
/FTId=VAR_002219.
VARIANT 129 129 V -> M (in ADASCID; delayed-onset;
dbSNP:rs121908731).
{ECO:0000269|PubMed:10200056}.
/FTId=VAR_002220.
VARIANT 140 140 G -> E (in ADASCID; dbSNP:rs121908732).
{ECO:0000269|PubMed:10200056}.
/FTId=VAR_002221.
VARIANT 142 142 R -> Q (in a pancreatic ductal
adenocarcinoma sample; somatic mutation;
dbSNP:rs61732239).
{ECO:0000269|PubMed:18772397,
ECO:0000269|PubMed:8589684}.
/FTId=VAR_002222.
VARIANT 149 149 R -> Q (in ADASCID; dbSNP:rs121908737).
{ECO:0000269|PubMed:2166947}.
/FTId=VAR_002223.
VARIANT 149 149 R -> W (in ADASCID; dbSNP:rs121908733).
{ECO:0000269|PubMed:10200056}.
/FTId=VAR_002224.
VARIANT 152 152 L -> M (in an individual with partial ADA
deficiency but no immunodeficiency; 1,5%
of activity; dbSNP:rs121908728).
{ECO:0000269|PubMed:9225964}.
/FTId=VAR_002225.
VARIANT 156 156 R -> C (in ADASCID; dbSNP:rs121908735).
{ECO:0000269|PubMed:1284479}.
/FTId=VAR_002226.
VARIANT 156 156 R -> H (in ADASCID; loss of activity;
dbSNP:rs121908722).
{ECO:0000269|PubMed:8227344}.
/FTId=VAR_002227.
VARIANT 177 177 V -> M (in ADASCID; loss of activity;
dbSNP:rs121908719).
{ECO:0000269|PubMed:8227344}.
/FTId=VAR_002228.
VARIANT 179 179 A -> D (in ADASCID; loss of activity;
dbSNP:rs121908727).
{ECO:0000269|PubMed:7599635}.
/FTId=VAR_002229.
VARIANT 199 199 Q -> P (in ADASCID; delayed-onset;
dbSNP:rs121908734).
{ECO:0000269|PubMed:10200056}.
/FTId=VAR_002230.
VARIANT 211 211 R -> C (in ADASCID; late onset; 4% of
activity; dbSNP:rs121908740).
{ECO:0000269|PubMed:2166947,
ECO:0000269|PubMed:9361033}.
/FTId=VAR_002231.
VARIANT 211 211 R -> H (in ADASCID; dbSNP:rs121908716).
{ECO:0000269|PubMed:3182793}.
/FTId=VAR_002232.
VARIANT 215 215 A -> T (in ADASCID; 8% of activity;
dbSNP:rs114025668).
{ECO:0000269|PubMed:2166947,
ECO:0000269|PubMed:9361033}.
/FTId=VAR_002233.
VARIANT 216 216 G -> R (in ADASCID; severe;
dbSNP:rs121908723).
{ECO:0000269|PubMed:8227344}.
/FTId=VAR_002234.
VARIANT 233 233 T -> I (in an individual with partial ADA
deficiency but no immunodeficiency; 20%
of activity; dbSNP:rs121908729).
{ECO:0000269|PubMed:9225964,
ECO:0000269|PubMed:9361033}.
/FTId=VAR_002235.
VARIANT 274 274 P -> L (in ADASCID; dbSNP:rs121908738).
{ECO:0000269|PubMed:2166947}.
/FTId=VAR_002236.
VARIANT 291 291 S -> L (in ADASCID; dbSNP:rs121908721).
{ECO:0000269|PubMed:1284479,
ECO:0000269|PubMed:8227344}.
/FTId=VAR_002237.
VARIANT 297 297 P -> Q (in ADASCID; dbSNP:rs121908718).
{ECO:0000269|PubMed:2783588}.
/FTId=VAR_002238.
VARIANT 304 304 L -> R (in ADASCID; loss of activity;
dbSNP:rs199422327).
/FTId=VAR_002239.
VARIANT 329 329 A -> V (in ADASCID; dbSNP:rs121908715).
{ECO:0000269|PubMed:3182793}.
/FTId=VAR_002240.
VARIANT 337 337 Missing (in ADASCID).
/FTId=VAR_002241.
MUTAGEN 58 58 L->A: Decreases enzyme activity by
reducing substrate affinity and maximum
velocity; abolishes ADORA1 and ADORA2A
modulator function.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 60 60 D->A: Moderately reduces enzyme activity;
reduces ADORA1 and ADORA2A modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 61 61 F->A: Decreases enzyme activity by
reducing maximum velocity; reduces ADORA1
modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 62 62 L->A: Decreases enzyme activity by
reducing substrate affinity and maximum
velocity; abolishes ADORA1 and ADORA2A
modulator function.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 64 64 K->A: Moderately reduces enzyme activity;
no change in ADORA1 and ADORA2A
modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 65 65 F->A: Decreases enzyme activity by
reducing substrate affinity and maximum
velocity; reduces ADORA1 and ADORA2A
modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 66 66 D->A: No change in enzyme activity; no
change in ADORA1 and ADORA2A modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 69 69 M->A: Decreases enzyme activity by
reducing maximum velocity; reduces
ADORA2A modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 115 115 I->A: No change in enzyme activity; no
change in ADORA1 and ADORA2A modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 118 118 N->A: Moderately reduces enzyme activity;
no change in ADORA1 and ADORA2A
modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 155 155 M->A: Decreases enzyme activity by
reducing substrate affinity and maximum
velocity. {ECO:0000269|PubMed:23193172}.
MUTAGEN 157 157 H->A: Moderately reduces enzyme activity;
no change in ADORA1 and ADORA2A
modulation.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 184 184 G->Q: Moderately reduces enzyme activity.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 185 185 D->A: Moderately reduces enzyme activity.
{ECO:0000269|PubMed:23193172}.
MUTAGEN 194 194 L->A: No change in enzyme activity.
{ECO:0000269|PubMed:23193172}.
CONFLICT 340 340 K -> R (in Ref. 5; BAD97117).
{ECO:0000305}.
STRAND 11 13 {ECO:0000244|PDB:3IAR}.
HELIX 18 20 {ECO:0000244|PDB:3IAR}.
HELIX 24 34 {ECO:0000244|PDB:3IAR}.
HELIX 43 50 {ECO:0000244|PDB:3IAR}.
HELIX 58 62 {ECO:0000244|PDB:3IAR}.
HELIX 63 67 {ECO:0000244|PDB:3IAR}.
HELIX 69 72 {ECO:0000244|PDB:3IAR}.
HELIX 76 91 {ECO:0000244|PDB:3IAR}.
TURN 92 94 {ECO:0000244|PDB:3IAR}.
STRAND 95 102 {ECO:0000244|PDB:3IAR}.
HELIX 104 107 {ECO:0000244|PDB:3IAR}.
STRAND 109 111 {ECO:0000244|PDB:3IAR}.
HELIX 116 118 {ECO:0000244|PDB:3IAR}.
HELIX 126 144 {ECO:0000244|PDB:3IAR}.
STRAND 147 155 {ECO:0000244|PDB:3IAR}.
HELIX 159 161 {ECO:0000244|PDB:3IAR}.
HELIX 162 171 {ECO:0000244|PDB:3IAR}.
TURN 172 176 {ECO:0000244|PDB:3IAR}.
STRAND 177 184 {ECO:0000244|PDB:3IAR}.
HELIX 191 193 {ECO:0000244|PDB:3IAR}.
HELIX 195 207 {ECO:0000244|PDB:3IAR}.
STRAND 210 219 {ECO:0000244|PDB:3IAR}.
HELIX 221 229 {ECO:0000244|PDB:3IAR}.
STRAND 234 238 {ECO:0000244|PDB:3IAR}.
HELIX 240 244 {ECO:0000244|PDB:3IAR}.
HELIX 246 254 {ECO:0000244|PDB:3IAR}.
STRAND 258 261 {ECO:0000244|PDB:3IAR}.
HELIX 263 268 {ECO:0000244|PDB:3IAR}.
STRAND 270 272 {ECO:0000244|PDB:3IAR}.
HELIX 279 285 {ECO:0000244|PDB:3IAR}.
STRAND 290 292 {ECO:0000244|PDB:3IAR}.
HELIX 297 300 {ECO:0000244|PDB:3IAR}.
HELIX 304 315 {ECO:0000244|PDB:3IAR}.
HELIX 319 331 {ECO:0000244|PDB:3IAR}.
STRAND 333 335 {ECO:0000244|PDB:3IAR}.
HELIX 337 351 {ECO:0000244|PDB:3IAR}.
HELIX 355 362 {ECO:0000244|PDB:3IAR}.
SEQUENCE 363 AA; 40764 MW; 786BC5085CA9AFCB CRC64;
MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD
FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA
EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI
DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY
HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF
KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG
QNL


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