ADA2_XENLA
ID ADA2_XENLA Reviewed; 510 AA.
AC Q2VQV9; Q1X7G3; Q6GNZ3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Adenosine deaminase 2 {ECO:0000250|UniProtKB:Q9NZK5};
DE EC=3.5.4.4 {ECO:0000269|PubMed:18032387};
DE AltName: Full=Cat eye syndrome critical region protein 1;
DE Flags: Precursor;
GN Name=ada2 {ECO:0000250|UniProtKB:Q9NZK5}; Synonyms=cecr1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16245011; DOI=10.1007/s00239-005-0046-y;
RA Maier S.A., Galellis J.R., McDermid H.E.;
RT "Phylogenetic analysis reveals a novel protein family closely related to
RT adenosine deaminase.";
RL J. Mol. Evol. 61:776-794(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=18032387; DOI=10.1074/jbc.m709279200;
RA Iijima R., Kunieda T., Yamaguchi S., Kamigaki H., Fujii-Taira I.,
RA Sekimizu K., Kubo T., Natori S., Homma K.J.;
RT "The extracellular adenosine deaminase growth factor, ADGF/CECR1, plays a
RT role in Xenopus embryogenesis via the adenosine/P1 receptor.";
RL J. Biol. Chem. 283:2255-2264(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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. Stimulates cell proliferation.
CC {ECO:0000269|PubMed:18032387}.
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:0000269|PubMed:18032387};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for adenosine {ECO:0000269|PubMed:18032387};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at stage 20 in the somites. At
CC stage 22 is also detected in the cement gland, and at stage 30 is
CC expressed in the somites, pronephros, eye, cement gland, neural tube,
CC and neural floor plate. {ECO:0000269|PubMed:18032387}.
CC -!- MISCELLANEOUS: Morpholino knockdown of the protein results in reduced
CC body size, abnormalities of the body axis, and changes in expression of
CC developmental marker genes.
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; AY902778; AAX10952.1; -; mRNA.
DR EMBL; AY986979; AAY42597.1; -; mRNA.
DR EMBL; BC073357; AAH73357.1; -; mRNA.
DR RefSeq; NP_001090531.1; NM_001097062.1.
DR AlphaFoldDB; Q2VQV9; -.
DR SMR; Q2VQV9; -.
DR DNASU; 779128; -.
DR GeneID; 779128; -.
DR KEGG; xla:779128; -.
DR CTD; 779128; -.
DR Xenbase; XB-GENE-6254244; ada2.L.
DR SABIO-RK; Q2VQV9; -.
DR Proteomes; UP000186698; Chromosome 3L.
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 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..510
FT /note="Adenosine deaminase 2"
FT /id="PRO_0000387959"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..153
FT /evidence="ECO:0000250"
FT CONFLICT 36
FT /note="I -> M (in Ref. 3; AAH73357)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="H -> R (in Ref. 3; AAH73357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57453 MW; 40D44EAC0318B031 CRC64;
MACVSHWLLL LSLASATLSR PLWSERNGLI EMENSIRLGG NIILTPSEAT ANQKLMTVKG
AEFKEAESTG LFPPSMHFFK ARPLIQQSHV FSILHQMPKG GALHLHDFAI LSVDWLVKNA
SYMADCYMCL TRDGGVRFLF AKPAPVGMLP PGCSEWILLE TYRKKLGDVT EFDKGLIRNL
TLLTDSPEPH IPSQDEIWRR FEGAFITASG LICYAPVFKE YFYESLRELY EDNIQYLEMR
AMLPPVYELD GTVHDQFWSM AIYRDMANKF VGAHPDFLGA KIIYTVHRHE DLAQVTEAVH
LAMKLMEAFP EIMAGFDLVG QEDAGHSLYQ LSDALNIPSK LGVKLPYFFH AGETNWQGKD
VDENVLDALL LNTTRIGHGY ALLKHPVARN LSLELNVPLE ICPISNQVLL LVSDLRNHPA
AVLMAEGHPL VVSSDDPSIF GAQGISYDFY EMFMGIGGAK ADLRTLKKLA ENSIKYSALS
KEGKEKLTEI WQKKWDKFIK DLAMNWKKEL
