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Protein

Adenosine deaminase

Gene

ADA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 + H2O = inosine + NH3.By similarity

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi15Zinc; catalyticCombined sources9 Publications1
Metal bindingi17Zinc; catalyticCombined sources9 Publications1
Binding sitei17SubstrateCombined sources6 Publications1
Binding sitei19SubstrateCombined sources7 Publications1
Sitei58Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity1
Sitei62Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity1
Binding sitei184Substrate; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
Metal bindingi214Zinc; catalyticCombined sources9 Publications1
Active sitei217Proton donorBy similarity1
Sitei238Important for catalytic activityBy similarity1
Metal bindingi295Zinc; catalyticCombined sources9 Publications1
Binding sitei296SubstrateCombined sources6 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell adhesion, Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.4. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminase (EC:3.5.4.4By similarity)
Alternative name(s):
Adenosine aminohydrolase
Gene namesi
Name:ADA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
  • Cell junction By similarity
  • Cytoplasmic vesicle lumen By similarity
  • Cytoplasm By similarity
  • Lysosome By similarity

  • Note: Colocalized with DPP4 at the cell surface.By similarity

GO - Cellular componenti

Complete GO annotation...

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

ChEMBLiCHEMBL2966.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00001943512 – 363Adenosine deaminaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei54N6-acetyllysineBy similarity1
Modified residuei232N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP56658.
PeptideAtlasiP56658.
PRIDEiP56658.

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

WithEntry#Exp.IntActNotes
DPP4P274875EBI-7475530,EBI-2871277From a different organism.

Protein-protein interaction databases

IntActiP56658. 1 interactor.
STRINGi9913.ENSBTAP00000006947.

Chemistry databases

BindingDBiP56658.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi18 – 20Combined sources3
Helixi24 – 33Combined sources10
Helixi43 – 50Combined sources8
Helixi58 – 72Combined sources15
Helixi76 – 92Combined sources17
Beta strandi95 – 102Combined sources8
Helixi105 – 107Combined sources3
Beta strandi109 – 111Combined sources3
Helixi116 – 118Combined sources3
Helixi126 – 144Combined sources19
Beta strandi147 – 155Combined sources9
Helixi159 – 161Combined sources3
Helixi162 – 171Combined sources10
Turni174 – 176Combined sources3
Beta strandi177 – 184Combined sources8
Helixi191 – 193Combined sources3
Helixi195 – 207Combined sources13
Beta strandi210 – 219Combined sources10
Helixi221 – 229Combined sources9
Beta strandi234 – 238Combined sources5
Helixi240 – 244Combined sources5
Helixi246 – 254Combined sources9
Beta strandi258 – 261Combined sources4
Helixi263 – 269Combined sources7
Beta strandi270 – 272Combined sources3
Helixi279 – 285Combined sources7
Beta strandi289 – 292Combined sources4
Helixi297 – 300Combined sources4
Helixi304 – 313Combined sources10
Helixi319 – 331Combined sources13
Beta strandi333 – 335Combined sources3
Helixi337 – 351Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KRMX-ray2.50A2-357[»]
1NDVX-ray2.30A2-357[»]
1NDWX-ray2.00A2-357[»]
1NDYX-ray2.00A2-357[»]
1NDZX-ray2.00A2-357[»]
1O5RX-ray2.35A2-357[»]
1QXLX-ray2.25A2-357[»]
1UMLX-ray2.50A2-357[»]
1V79X-ray2.50A2-357[»]
1V7AX-ray2.50A2-357[»]
1VFLX-ray1.80A2-357[»]
1W1IX-ray3.03E/F/G/H1-357[»]
1WXYX-ray2.50A2-357[»]
1WXZX-ray2.80A2-357[»]
2BGNX-ray3.15E/F/G/H2-363[»]
2E1WX-ray2.50A2-357[»]
2Z7GX-ray2.52A2-357[»]
ProteinModelPortaliP56658.
SMRiP56658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56658.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
HOGENOMiHOG000218816.
HOVERGENiHBG001718.
InParanoidiP56658.
KOiK01488.

Family and domain databases

CDDicd01320. ADA. 1 hit.
HAMAPiMF_00540. A_deaminase. 1 hit.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56658-1 [UniParc]FASTAAdd 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
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8N → D AA sequence (PubMed:8877857).Curated1
Sequence conflicti32 – 33RK → KR AA sequence (PubMed:8877857).Curated2
Sequence conflicti57S → T AA sequence (PubMed:8877857).Curated1
Sequence conflicti60E → D AA sequence (PubMed:8877857).Curated1
Sequence conflicti77 – 79EAV → DAI AA sequence (PubMed:8877857).Curated3
Sequence conflicti261V → I AA sequence (PubMed:8877857).Curated1
Sequence conflicti279 – 281PVV → AVI AA sequence (PubMed:8877857).Curated3
Sequence conflicti313 – 314NE → KD AA sequence (PubMed:8877857).Curated2

Mass spectrometryi

Molecular mass is 40549±16 Da from positions 2 - 363. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti199K → Q.1
Natural varianti246A → T.1
Natural varianti352G → R.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF280603 mRNA. Translation: AAF91430.1.
RefSeqiNP_776312.1. NM_173887.2.
UniGeneiBt.4303.

Genome annotation databases

GeneIDi280712.
KEGGibta:280712.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF280603 mRNA. Translation: AAF91430.1.
RefSeqiNP_776312.1. NM_173887.2.
UniGeneiBt.4303.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KRMX-ray2.50A2-357[»]
1NDVX-ray2.30A2-357[»]
1NDWX-ray2.00A2-357[»]
1NDYX-ray2.00A2-357[»]
1NDZX-ray2.00A2-357[»]
1O5RX-ray2.35A2-357[»]
1QXLX-ray2.25A2-357[»]
1UMLX-ray2.50A2-357[»]
1V79X-ray2.50A2-357[»]
1V7AX-ray2.50A2-357[»]
1VFLX-ray1.80A2-357[»]
1W1IX-ray3.03E/F/G/H1-357[»]
1WXYX-ray2.50A2-357[»]
1WXZX-ray2.80A2-357[»]
2BGNX-ray3.15E/F/G/H2-363[»]
2E1WX-ray2.50A2-357[»]
2Z7GX-ray2.52A2-357[»]
ProteinModelPortaliP56658.
SMRiP56658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP56658. 1 interactor.
STRINGi9913.ENSBTAP00000006947.

Chemistry databases

BindingDBiP56658.
ChEMBLiCHEMBL2966.

Proteomic databases

PaxDbiP56658.
PeptideAtlasiP56658.
PRIDEiP56658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280712.
KEGGibta:280712.

Organism-specific databases

CTDi100.

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
HOGENOMiHOG000218816.
HOVERGENiHBG001718.
InParanoidiP56658.
KOiK01488.

Enzyme and pathway databases

BRENDAi3.5.4.4. 908.

Miscellaneous databases

EvolutionaryTraceiP56658.
PROiP56658.

Family and domain databases

CDDicd01320. ADA. 1 hit.
HAMAPiMF_00540. A_deaminase. 1 hit.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADA_BOVIN
AccessioniPrimary (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: November 30, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.