ID A0A1S3SHD8_SALSA Unreviewed; 531 AA.
AC A0A1S3SHD8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN Name=LOC106609445 {ECO:0000313|RefSeq:XP_014063770.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014063770.1};
RN [1] {ECO:0000313|RefSeq:XP_014063770.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014063770.1};
RG RefSeq;
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}.
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DR RefSeq; XP_014063770.1; XM_014208295.1.
DR AlphaFoldDB; A0A1S3SHD8; -.
DR STRING; 8030.ENSSSAP00000005839; -.
DR PaxDb; 8030-ENSSSAP00000005839; -.
DR Ensembl; ENSSSAT00000006251; ENSSSAP00000005839; ENSSSAG00000002881.
DR GeneID; 106609445; -.
DR KEGG; sasa:106609445; -.
DR CTD; 559295; -.
DR OrthoDB; 4403at2759; -.
DR Proteomes; UP000087266; Chromosome ssa07.
DR Bgee; ENSSSAG00000002881; Expressed in brain and 16 other cell types or tissues.
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 GO; GO:0060837; P:blood vessel endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0030223; P:neutrophil differentiation; IEA:Ensembl.
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:SF44; ADENOSINE DEAMINASE; 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:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 54..120
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 218..509
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 531 AA; 60292 MW; 04C2BA345DFBC52E CRC64;
MSGLKKDFHS WFFQPPMTLQ NKVVLPSRGR YTITLQLAAV MCCVTVCGGT PDPRQRETMI
HQEASRQTGG RVQLTGAEQR LDAHLRKLKE QEMAAAQFPP AFHFFKARPL IHKSPIFSLL
QRMPKGAALH IHSSSLVSVD WLVKNITYRP HCYICFTRGR SVRFVFSSRR PFPTWDCLYW
QLLKTLRADM ADPTDFDYSL MQNLTLFTED PDTTYPSQDA VWERFEMAFV ALAGLVTYAP
VFKDFLYKGL EQLFHDNIMY LELRTGLSRT YELDGSIHDK AWSLRTYQEV TQQFVAEHPS
FLGVRLIISV HRVLSVSDVK AAVKEAIQMQ KDFPEFVAGF DLVGREDRGR PLWFFREALS
LPAELGVTLP YFFHAGETDQ EGTEVDENIL DALLFNTTRI GHGYALAHHP LAKELSRNGN
VAVEVCPISN QVLKLVSDLR NHPAAVLMSE GHPMVVSSDD PSLFGTTGLS YDFYEVYVGI
GGLRANLGTL KELAINSIRY SSLPSQLKER GLAMWQKTWD KFISENSHSN P
//
