ADA2_DANRE
ID ADA2_DANRE Reviewed; 503 AA.
AC P58781; Q7ZVJ3; Q8UVU4;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Adenosine deaminase 2-A {ECO:0000250|UniProtKB:Q9NZK5};
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:Q9NZK5};
DE AltName: Full=Cat eye syndrome critical region protein 1 homolog A;
DE Flags: Precursor;
GN Name=ada2a {ECO:0000250|UniProtKB:Q9NZK5}; Synonyms=cecr1, cecr1a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11738815; DOI=10.1016/s0378-1119(01)00762-4;
RA Maier S.A., Podemski L., Graham S.W., McDermid H.E., Locke J.;
RT "Characterization of the adenosine deaminase-related growth factor (ADGF)
RT gene family in Drosophila.";
RL Gene 280:27-36(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adenosine deaminase that may contribute to the degradation of
CC extracellular adenosine, a signaling molecule that controls a variety
CC of cellular responses. May play a role in the regulation of cell
CC proliferation (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily. {ECO:0000305}.
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DR EMBL; AF384217; AAL40922.1; -; mRNA.
DR EMBL; BC045839; AAH45839.1; -; mRNA.
DR RefSeq; NP_001028889.2; NM_001033717.2.
DR AlphaFoldDB; P58781; -.
DR SMR; P58781; -.
DR STRING; 7955.ENSDARP00000067907; -.
DR PaxDb; P58781; -.
DR GeneID; 373884; -.
DR KEGG; dre:373884; -.
DR CTD; 373884; -.
DR ZFIN; ZDB-GENE-030902-4; ada2a.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; P58781; -.
DR OrthoDB; 430357at2759; -.
DR PhylomeDB; P58781; -.
DR Reactome; R-DRE-5683826; Surfactant metabolism.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR PRO; PR:P58781; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004000; F:adenosine deaminase activity; ISS:UniProtKB.
DR GO; GO:0031685; F:adenosine receptor binding; ISS:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006154; P:adenosine catabolic process; ISS:UniProtKB.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
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 PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF08451; A_deaminase_N; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01431; adm_rel; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..503
FT /note="Adenosine deaminase 2-A"
FT /id="PRO_0000006727"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..152
FT /evidence="ECO:0000250"
FT CONFLICT 151
FT /note="Y -> H (in Ref. 1; AAL40922)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> Y (in Ref. 1; AAL40922)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="P -> S (in Ref. 1; AAL40922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57506 MW; F489CEF647FAF1AC CRC64;
MHVLFLGDLM WIYLLLLCCA SCNGRPDPRK RDALIGLEAS RRTGGDITLN EREKLLDGKL
QKLKQHDMEA GQFPPSMHFF KAKRLIDQSP VFNLIQKMPK GAALHVHDFA MVSVDWLVKN
VTYRENCYVC FTDKQTVQFI FSSGPPASSS YCSSWTLLRS LREKIKNTTE LDNSFIRNLT
LFTEDPDRAY PNQDTVWERF EQVFLVAYGL VTYAPVFKDY LYEGLRQFYE DNIMYVEIRA
LLPQTYELDG RLNDKDWSMA ACQEVVNQFK KHHPDFIGAR VIFTVHRKIN ATEAVKTVEE
AMILRRNFPD VMAGFDFVGQ EDLGRPLWYF KDALSLPEDK GFNLPYFFHA GETDSQGTDV
DQNLMDALLF NTTRIGHGFA LARHPVVKEM ARKMDVPIEV CPISNQVLKL VSDLRDHPAA
VLMAEGHPLV ISSDDPAVFG ATALSHDFYE AFMGFGGMSF NLGTLKELAL NSLRYSTLPS
QRKEEAIDAL LVKWDKFVWE SLL
