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UniProtKB - P56658 (ADA_BOVIN)

>sp|P56658|ADA_BOVIN Adenosine deaminase OS=Bos taurus OX=9913 GN=ADA PE=1 SV=3
MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPE
FLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQA
EGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAI
DLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGY
HTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIF
KSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAE
QCL

Entry version 145 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss

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Protein

Adenosine deaminase

Gene

ADA

Organism

Bos taurus (Bovine)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (By similarity).

Plays an important role in purine metabolism and in adenosine homeostasis (By similarity).

Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events (By similarity).

Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity).

Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).

Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (PubMed:23240012).

Enhances CD4+ T-cell differentiation and proliferation (By similarity).

Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity).

Stimulates plasminogen activation (By similarity).

Plays a role in male fertility (By similarity).

Plays a protective role in early postimplantation embryonic development (By similarity).

By similarity1 Publication

Catalytic activityⁱ

adenosine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
inosine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NH₄⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P00813 (ADA_HUMAN)
EC:
3.5.4.4
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P00813 (ADA_HUMAN)
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
adenosine
zoom
+
H⁺
+
H₂O
=
inosine
zoom
+
NH₄⁺
zoom

Cofactorⁱ

Zn²⁺4 PublicationsNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	15	Zinc; catalyticCombined sources9 Publications	1
Metal bindingⁱ	17	Zinc; catalyticCombined sources9 Publications	1
Binding siteⁱ	17	SubstrateCombined sources6 Publications	1
Binding siteⁱ	19	SubstrateCombined sources7 Publications	1
Siteⁱ	58	Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity	1
Siteⁱ	62	Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity	1
Binding siteⁱ	184	Substrate; via amide nitrogen and carbonyl oxygenCombined sources2 Publications	1
Metal bindingⁱ	214	Zinc; catalyticCombined sources9 Publications	1
Active siteⁱ	217	Proton donorBy similarity	1
Siteⁱ	238	Important for catalytic activityBy similarity	1
Metal bindingⁱ	295	Zinc; catalyticCombined sources9 Publications	1
Binding siteⁱ	296	SubstrateCombined sources6 Publications	1

GO - Molecular functionⁱ

adenosine deaminase activity Source: UniProtKB
zinc ion binding Source: UniProtKB

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Cell adhesion, Nucleotide metabolism
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	3.5.4.4, 908

BRENDAⁱ

3.5.4.4, 908

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Adenosine deaminase (EC:3.5.4.4By similarity) Alternative name(s): Adenosine aminohydrolase
Gene namesⁱ	Name:ADA
Organismⁱ	Bos taurus (Bovine)
Taxonomic identifierⁱ	9913 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
Proteomesⁱ	UP000009136 Componentⁱ: Unplaced

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Lysosome, Membrane

Pathology & Biotechⁱ

Pharmaceutical useⁱ

Available under the name Adagen (Enzon). This is a PEG-conjugated form (pegademase). Used to treat patients with severe combined immunodeficiency diseases (SCID).

Chemistry databases

ChEMBLⁱ	CHEMBL2966
DrugCentral More...DrugCentralⁱ	P56658

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity1 Publication
ChainⁱPRO_0000194351	2 – 363	Adenosine deaminaseAdd BLAST		362

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineBy similarity	1
Modified residueⁱ	54	N6-acetyllysineBy similarity	1
Modified residueⁱ	232	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

PaxDbⁱ	P56658
PeptideAtlas More...PeptideAtlasⁱ	P56658
PRIDEⁱ	P56658

Expressionⁱ

Tissue specificityⁱ

Expressed in gastrointestinal tissues (at protein level).1 Publication

Interactionⁱ

Subunit structureⁱ

Interacts with DPP4 (via extracellular domain).

Interacts with PLG (via Kringle 4 domain); the interaction stimulates PLG activation when in complex with DPP4.

By similarity

Binary interactionsⁱ

P56658

With	#Exp.	IntAct
DPP4 [P27487] from Homo sapiens.	5	EBI-7475530,EBI-2871277

Protein-protein interaction databases

IntActⁱ	P56658, 1 interactor
Molecular INTeraction database More...MINTⁱ	P56658
STRINGⁱ	9913.ENSBTAP00000006947

Chemistry databases

BindingDBⁱ

P56658

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	11 – 13	Combined sources	3
Helixⁱ	18 – 20	Combined sources	3
Helixⁱ	24 – 33	Combined sources	10
Helixⁱ	43 – 50	Combined sources	8
Helixⁱ	58 – 72	Combined sources	15
Helixⁱ	76 – 92	Combined sources	17
Beta strandⁱ	95 – 102	Combined sources	8
Helixⁱ	105 – 107	Combined sources	3
Beta strandⁱ	109 – 111	Combined sources	3
Helixⁱ	116 – 118	Combined sources	3
Helixⁱ	126 – 144	Combined sources	19
Beta strandⁱ	147 – 155	Combined sources	9
Helixⁱ	159 – 161	Combined sources	3
Helixⁱ	162 – 171	Combined sources	10
Turnⁱ	174 – 176	Combined sources	3
Beta strandⁱ	177 – 184	Combined sources	8
Helixⁱ	191 – 193	Combined sources	3
Helixⁱ	195 – 207	Combined sources	13
Beta strandⁱ	210 – 219	Combined sources	10
Helixⁱ	221 – 229	Combined sources	9
Beta strandⁱ	234 – 238	Combined sources	5
Helixⁱ	240 – 244	Combined sources	5
Helixⁱ	246 – 254	Combined sources	9
Beta strandⁱ	258 – 261	Combined sources	4
Helixⁱ	263 – 269	Combined sources	7
Beta strandⁱ	270 – 272	Combined sources	3
Helixⁱ	279 – 285	Combined sources	7
Beta strandⁱ	289 – 292	Combined sources	4
Helixⁱ	297 – 300	Combined sources	4
Helixⁱ	304 – 313	Combined sources	10
Helixⁱ	319 – 331	Combined sources	13
Beta strandⁱ	333 – 335	Combined sources	3
Helixⁱ	337 – 351	Combined sources	15

Show more details

3D structure databases

SMRⁱ	P56658
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P56658

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1097, Eukaryota
InParanoidⁱ	P56658
Database of Orthologous Groups More...OrthoDBⁱ	1045809at2759

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01320, ADA, 1 hit
HAMAPⁱ	MF_00540, A_deaminase, 1 hit
InterProⁱ	View protein in InterPro IPR006650, A/AMP_deam_AS IPR028893, A_deaminase IPR001365, A_deaminase_dom IPR006330, Ado/ade_deaminase IPR032466, Metal_Hydrolase
PANTHERⁱ	PTHR11409, PTHR11409, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00962, A_deaminase, 1 hit
SUPFAMⁱ	SSF51556, SSF51556, 1 hit
TIGRFAMsⁱ	TIGR01430, aden_deam, 1 hit
PROSITEⁱ	View protein in PROSITE PS00485, A_DEAMINASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P56658-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAQTPAFNKP KVELHVHLDG AIKPETILYY GRKRGIALPA DTPEELQNII 
        60         70         80         90        100
GMDKPLSLPE FLAKFDYYMP AIAGCREAVK RIAYEFVEMK AKDGVVYVEV 
       110        120        130        140        150
RYSPHLLANS KVEPIPWNQA EGDLTPDEVV SLVNQGLQEG ERDFGVKVRS 
       160        170        180        190        200
ILCCMRHQPS WSSEVVELCK KYREQTVVAI DLAGDETIEG SSLFPGHVKA 
       210        220        230        240        250
YAEAVKSGVH RTVHAGEVGS ANVVKEAVDT LKTERLGHGY HTLEDATLYN 
       260        270        280        290        300
RLRQENMHFE VCPWSSYLTG AWKPDTEHPV VRFKNDQVNY SLNTDDPLIF 
       310        320        330        340        350
KSTLDTDYQM TKNEMGFTEE EFKRLNINAA KSSFLPEDEK KELLDLLYKA 
       360 
YGMPSPASAE QCL

Length:363

Mass (Da):40,919

Last modified:January 23, 2007 - v3

Checksum:ⁱ69F6D25ACFF2A3E5

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	8	N → D AA sequence (PubMed:8877857).Curated	1
Sequence conflictⁱ	32 – 33	RK → KR AA sequence (PubMed:8877857).Curated	2
Sequence conflictⁱ	57	S → T AA sequence (PubMed:8877857).Curated	1
Sequence conflictⁱ	60	E → D AA sequence (PubMed:8877857).Curated	1
Sequence conflictⁱ	77 – 79	EAV → DAI AA sequence (PubMed:8877857).Curated	3
Sequence conflictⁱ	261	V → I AA sequence (PubMed:8877857).Curated	1
Sequence conflictⁱ	279 – 281	PVV → AVI AA sequence (PubMed:8877857).Curated	3
Sequence conflictⁱ	313 – 314	NE → KD AA sequence (PubMed:8877857).Curated	2

Mass spectrometryⁱ

Molecular mass is 40549±16 Da. Determined by ESI. 1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	199	K → Q.	1
Natural variantⁱ	246	A → T.	1
Natural variantⁱ	352	G → R.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF280603 mRNA Translation: AAF91430.1
NCBI Reference Sequences More...RefSeqⁱ	NP_776312.1, NM_173887.2

Genome annotation databases

GeneIDⁱ	280712
KEGGⁱ	bta:280712

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P56658	Adenosine deaminase		BOVIN		443	UniRef90_P56658
Adenosine aminohydrolase		BOSIN		363
Adenosine aminohydrolase		Bison bison bison		363
Adenosine aminohydrolase		BOBOX		363
Adenosine aminohydrolase		BOVIN		363
+1

Protein	Similar proteins		Species	Score	Length	Source
P56658	Adenosine deaminase	)	HUMAN		363	UniRef50_P00813
Adenosine aminohydrolase		CERAT		449
Adenosine deaminase		Ugandan red Colobus		387
Adenosine aminohydrolase		AOTNA		363
Adenosine aminohydrolase		PANTR		363
+196

Cross-referencesⁱ

Web resourcesⁱ

Worthington enzyme manual

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF280603 mRNA Translation: AAF91430.1
RefSeqⁱ	NP_776312.1, NM_173887.2

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1KRM	X-ray	2.50	A	2-357	[»]
	1NDV	X-ray	2.30	A	2-357	[»]
	1NDW	X-ray	2.00	A	2-357	[»]
	1NDY	X-ray	2.00	A	2-357	[»]
	1NDZ	X-ray	2.00	A	2-357	[»]
	1O5R	X-ray	2.35	A	2-357	[»]
	1QXL	X-ray	2.25	A	2-357	[»]
	1UML	X-ray	2.50	A	2-357	[»]
	1V79	X-ray	2.50	A	2-357	[»]
	1V7A	X-ray	2.50	A	2-357	[»]
	1VFL	X-ray	1.80	A	2-357	[»]
	1W1I	X-ray	3.03	E/F/G/H	1-357	[»]
	1WXY	X-ray	2.50	A	2-357	[»]
	1WXZ	X-ray	2.80	A	2-357	[»]
	2BGN	X-ray	3.15	E/F/G/H	2-363	[»]
	2E1W	X-ray	2.50	A	2-357	[»]
	2Z7G	X-ray	2.52	A	2-357	[»]
SMRⁱ	P56658
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P56658, 1 interactor
MINTⁱ	P56658
STRINGⁱ	9913.ENSBTAP00000006947

Chemistry databases

BindingDBⁱ	P56658
ChEMBLⁱ	CHEMBL2966
DrugCentralⁱ	P56658

Proteomic databases

PaxDbⁱ	P56658
PeptideAtlasⁱ	P56658
PRIDEⁱ	P56658

Genome annotation databases

GeneIDⁱ	280712
KEGGⁱ	bta:280712

Organism-specific databases

CTDⁱ	100

CTDⁱ

100

Phylogenomic databases

eggNOGⁱ	KOG1097, Eukaryota
InParanoidⁱ	P56658
OrthoDBⁱ	1045809at2759

Enzyme and pathway databases

BRENDAⁱ	3.5.4.4, 908

BRENDAⁱ

3.5.4.4, 908

Miscellaneous databases

EvolutionaryTraceⁱ	P56658
Protein Ontology More...PROⁱ	PR:P56658

Family and domain databases

CDDⁱ	cd01320, ADA, 1 hit
HAMAPⁱ	MF_00540, A_deaminase, 1 hit
InterProⁱ	View protein in InterPro IPR006650, A/AMP_deam_AS IPR028893, A_deaminase IPR001365, A_deaminase_dom IPR006330, Ado/ade_deaminase IPR032466, Metal_Hydrolase
PANTHERⁱ	PTHR11409, PTHR11409, 1 hit
Pfamⁱ	View protein in Pfam PF00962, A_deaminase, 1 hit
SUPFAMⁱ	SSF51556, SSF51556, 1 hit
TIGRFAMsⁱ	TIGR01430, aden_deam, 1 hit
PROSITEⁱ	View protein in PROSITE PS00485, A_DEAMINASE, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ADA_BOVIN
Accessionⁱ	P56658Primary (citable) accession number: P56658 Secondary accession number(s): Q9MYY1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
	Last sequence update:	January 23, 2007
	Last modified:	February 23, 2022
	This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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Supporting data

UniProtKB - P56658 (ADA_BOVIN)

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Adenosine deaminase

ADA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Plasma membrane

Lysosome

Other locations

Cytosol

Lysosome

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P56658

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ