ID A0A3Q1NIS4_BOVIN Unreviewed; 512 AA.
AC A0A3Q1NIS4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN Name=ADA2 {ECO:0000313|Ensembl:ENSBTAP00000071963.1,
GN ECO:0000313|VGNC:VGNC:54400};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000071963.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000071963.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071963.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000071963.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071963.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00001466};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily.
CC {ECO:0000256|ARBA:ARBA00006083}.
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 AlphaFoldDB; A0A3Q1NIS4; -.
DR PaxDb; 9913-ENSBTAP00000023021; -.
DR Ensembl; ENSBTAT00000067814.1; ENSBTAP00000071963.1; ENSBTAG00000017313.6.
DR VEuPathDB; HostDB:ENSBTAG00000017313; -.
DR VGNC; VGNC:54400; ADA2.
DR GeneTree; ENSGT00950000183113; -.
DR OMA; SMKQCIE; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000017313; Expressed in blood and 100 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1NIS4; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006154; P:adenosine catabolic process; IEA:InterPro.
DR CDD; cd01321; ADGF; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR013659; A_deaminase_N.
DR InterPro; IPR006331; ADGF.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01431; adm_rel; 1.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF39; ADENOSINE DEAMINASE 2; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF08451; A_deaminase_N; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..512
FT /note="adenosine deaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018781331"
FT DOMAIN 26..99
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 189..493
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 512 AA; 57961 MW; 17EA91EA4106DCCE CRC64;
MSGRLAPPSL LLALVVSSFC PATSRSGDET RNQLLTREKM MRVGGQLVLT WEEELANQRL
RALKEAEMHE ALSTGNILPS MHFFQAKSLI EKSEVFNILK KMPKGAALHV HDFSITSPDW
LVKNATYRPH CYFCFTRRGT PQFRFAHLTT PTPKPAECPQ WVLLEKFRKG LRNVSEFDNS
LLRNLTLMTE NPHVTYADQD AIWAKFETIF FVLGGLVSYA PVFRDYLSQG LEEFYQDNVL
YLEIRASLHP VYELDGTIYS QEWLVRTYEE VAHNFAKTHP GFIGIKLIFS DHRTKNESLI
KKSIQTAMDL RVKFPGIVAG FDLVGREDTG YTLYDYREAL MIPASRGVHL PYFFHAGETD
WEGTSVDRNL LDAVILNSTR IGHGFALSKH PAVLAEAWKK DIPIEVCPIS NQVLKLVSDL
RNHPAAVMMA AGYPMVISSD DPAAFGARGL SYDFYEAFMG IGGMSADLRT LKQLAINSIR
YSTLSETKKK SAMETWEERW QKFVAGLARG PR
//
