ID A0A452GA75_CAPHI Unreviewed; 400 AA.
AC A0A452GA75;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|Ensembl:ENSCHIP00000033539.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000033539.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000033539.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000033539.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR EMBL; LWLT01000014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452GA75; -.
DR STRING; 9925.ENSCHIP00000033539; -.
DR Ensembl; ENSCHIT00000041418.1; ENSCHIP00000033539.1; ENSCHIG00000027058.1.
DR GeneTree; ENSGT00950000183113; -.
DR Proteomes; UP000291000; Chromosome 13.
DR Bgee; ENSCHIG00000027058; Expressed in spleen and 16 other cell types or tissues.
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:0000255; P:allantoin metabolic process; IEA:Ensembl.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0043605; P:amide catabolic process; IEA:Ensembl.
DR GO; GO:0006196; P:AMP catabolic process; IEA:Ensembl.
DR GO; GO:0044209; P:AMP salvage; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0046059; P:dAMP catabolic process; IEA:Ensembl.
DR GO; GO:0046061; P:dATP catabolic process; IEA:Ensembl.
DR GO; GO:0006157; P:deoxyadenosine catabolic process; IEA:Ensembl.
DR GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR GO; GO:0002314; P:germinal center B cell differentiation; IEA:Ensembl.
DR GO; GO:0002467; P:germinal center formation; IEA:Ensembl.
DR GO; GO:0032263; P:GMP salvage; IEA:Ensembl.
DR GO; GO:0046101; P:hypoxanthine biosynthetic process; IEA:Ensembl.
DR GO; GO:0046103; P:inosine biosynthetic process; IEA:Ensembl.
DR GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0002901; P:mature B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0070256; P:negative regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:0060407; P:negative regulation of penile erection; IEA:Ensembl.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0043084; P:penile erection; IEA:Ensembl.
DR GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0002636; P:positive regulation of germinal center formation; IEA:Ensembl.
DR GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
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:0006939; P:smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0046111; P:xanthine biosynthetic process; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 15..352
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 400 AA; 44675 MW; 3A2C2EF1AC19B05D CRC64;
MGVCFFSFPS APLQVELHVH LDGAIKPETI LYYGRKRGIA LPADTPEGLQ NIIGMDKPLS
LPDFLAKFNY YMPAIAGCRE AVKRIAYEFM EMKAKEGVVY VEVRYSPHLL ANSKVEPIPW
NQAEGDLTPD EVVSLVSQGL QEGERDFGVK VRSILCCMRH QPSWSPEVVE LCKKYREQTV
VAIDLAGDET IKGSSLFPGH VEAYTEAVKS GVHRTVHAGE VGPATVVKEA VDTLKTERLG
HGYHTLEDAA LYNRLLQENM HFEVCPWSSY LTGAWKPDTE HPVVRFKNDQ ANYSLNTDDP
LIFKSTLDTD YQMTKRDMSF TEEEFKRLNI NAAKSSFLPE DEKKELLDLL YEAYGMPPLA
SAGMFLVDLL GWRPALAPVW LPGAFSRTLS TPLPGTTKAG
//
