ID Q4FK28_MOUSE Unreviewed; 352 AA. AC Q4FK28; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 145. DE RecName: Full=Adenosine deaminase {ECO:0000256|ARBA:ARBA00018099}; DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784}; DE AltName: Full=Adenosine aminohydrolase {ECO:0000256|ARBA:ARBA00031852}; GN Name=Ada {ECO:0000313|MGI:MGI:87916}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:CAJ18432.1}; RN [1] {ECO:0000313|EMBL:CAJ18432.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); CC Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; CC Evidence={ECO:0000256|ARBA:ARBA00034443}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; CC Evidence={ECO:0000256|ARBA:ARBA00034443}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+); CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; CC Evidence={ECO:0000256|ARBA:ARBA00001600}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; CC Evidence={ECO:0000256|ARBA:ARBA00001600}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}. CC Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane CC protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side CC {ECO:0000256|ARBA:ARBA00004296}. Cytoplasmic vesicle lumen CC {ECO:0000256|ARBA:ARBA00004321}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT010224; CAJ18432.1; -; mRNA. DR RefSeq; NP_001258981.1; NM_001272052.1. DR RefSeq; NP_031424.1; NM_007398.4. DR AlphaFoldDB; Q4FK28; -. DR SMR; Q4FK28; -. DR EPD; Q4FK28; -. DR MaxQB; Q4FK28; -. DR Antibodypedia; 700; 570 antibodies from 44 providers. DR DNASU; 11486; -. DR GeneID; 11486; -. DR KEGG; mmu:11486; -. DR AGR; MGI:87916; -. DR CTD; 100; -. DR MGI; MGI:87916; Ada. DR VEuPathDB; HostDB:ENSMUSG00000017697; -. DR HOGENOM; CLU_039228_0_1_1; -. DR OMA; NHFTIHA; -. DR OrthoDB; 36100at2759; -. DR PhylomeDB; Q4FK28; -. DR BioGRID-ORCS; 11486; 1 hit in 78 CRISPR screens. DR ChiTaRS; Ada; mouse. DR ExpressionAtlas; Q4FK28; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell. DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0006154; P:adenosine catabolic process; IEA:Ensembl. DR GO; GO:0046103; P:inosine biosynthetic process; IEA:Ensembl. DR GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IEA:Ensembl. DR GO; GO:0032261; P:purine nucleotide salvage; IEA:Ensembl. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0014074; P:response to purine-containing compound; IEA:Ensembl. DR GO; GO:0042110; P:T cell activation; IEA:Ensembl. DR CDD; cd01320; ADA; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00540; A_deaminase; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR028893; A_deaminase. DR InterPro; IPR001365; A_deaminase_dom. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01430; aden_deam; 1. DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1. DR PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. PE 1: Evidence at protein level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}. FT DOMAIN 10..348 FT /note="Adenosine deaminase" FT /evidence="ECO:0000259|Pfam:PF00962" SQ SEQUENCE 352 AA; 39992 MW; E53A8A1FABA148CD CRC64; MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII GMDKPLSLPG FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVDPMPWNQT EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS ILCCMRHQPS WSLEVLELCK KYNQKTVVAM DLAGDETIEG SSLFPGHVEA YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY HTIEDEALYN RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE YQ //