ADAT2_HUMAN
ID ADAT2_HUMAN Reviewed; 191 AA.
AC Q7Z6V5; A6NL12; B3KWY3; Q7Z327; Q8IY39;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=tRNA-specific adenosine deaminase 2;
DE EC=3.5.4.33 {ECO:0000305};
DE AltName: Full=Deaminase domain-containing protein 1;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT2;
GN Name=ADAT2; Synonyms=DEADC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-191 (ISOFORM 1).
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=12457566; DOI=10.1016/s0300-9084(02)01446-3;
RA Schaub M., Keller W.;
RT "RNA editing by adenosine deaminases generates RNA and protein diversity.";
RL Biochimie 84:791-803(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-185 IN COMPLEX WITH ZINC IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human tRNA-specific adenosine-34 deaminase subunit
RT ADAT2.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Probably participates in deamination of adenosine-34 to
CC inosine in many tRNAs. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q7Z6V5; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-2809203, EBI-741200;
CC Q7Z6V5; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2809203, EBI-744081;
CC Q7Z6V5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2809203, EBI-358489;
CC Q7Z6V5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2809203, EBI-5235340;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z6V5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6V5-2; Sequence=VSP_025582;
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37955.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK126201; BAG54295.1; -; mRNA.
DR EMBL; BX538182; CAD98054.1; -; mRNA.
DR EMBL; AL031320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47868.1; -; Genomic_DNA.
DR EMBL; BC037955; AAH37955.2; ALT_INIT; mRNA.
DR CCDS; CCDS43511.1; -. [Q7Z6V5-1]
DR CCDS; CCDS69219.1; -. [Q7Z6V5-2]
DR RefSeq; NP_001273188.1; NM_001286259.1. [Q7Z6V5-2]
DR RefSeq; NP_872309.2; NM_182503.2. [Q7Z6V5-1]
DR RefSeq; XP_011533742.1; XM_011535440.1.
DR RefSeq; XP_011533746.1; XM_011535444.2. [Q7Z6V5-2]
DR RefSeq; XP_016865749.1; XM_017010260.1. [Q7Z6V5-2]
DR RefSeq; XP_016865750.1; XM_017010261.1.
DR RefSeq; XP_016865751.1; XM_017010262.1. [Q7Z6V5-2]
DR PDB; 3DH1; X-ray; 2.80 A; A/B/C/D=20-185.
DR PDBsum; 3DH1; -.
DR AlphaFoldDB; Q7Z6V5; -.
DR SMR; Q7Z6V5; -.
DR BioGRID; 126410; 17.
DR IntAct; Q7Z6V5; 6.
DR STRING; 9606.ENSP00000237283; -.
DR iPTMnet; Q7Z6V5; -.
DR MetOSite; Q7Z6V5; -.
DR PhosphoSitePlus; Q7Z6V5; -.
DR BioMuta; ADAT2; -.
DR DMDM; 74750199; -.
DR EPD; Q7Z6V5; -.
DR jPOST; Q7Z6V5; -.
DR MassIVE; Q7Z6V5; -.
DR MaxQB; Q7Z6V5; -.
DR PaxDb; Q7Z6V5; -.
DR PeptideAtlas; Q7Z6V5; -.
DR PRIDE; Q7Z6V5; -.
DR ProteomicsDB; 69466; -. [Q7Z6V5-1]
DR ProteomicsDB; 69467; -. [Q7Z6V5-2]
DR Antibodypedia; 33139; 63 antibodies from 19 providers.
DR DNASU; 134637; -.
DR Ensembl; ENST00000237283.9; ENSP00000237283.8; ENSG00000189007.16. [Q7Z6V5-1]
DR Ensembl; ENST00000606514.5; ENSP00000475651.1; ENSG00000189007.16. [Q7Z6V5-2]
DR GeneID; 134637; -.
DR KEGG; hsa:134637; -.
DR MANE-Select; ENST00000237283.9; ENSP00000237283.8; NM_182503.3; NP_872309.2.
DR UCSC; uc003qjj.4; human. [Q7Z6V5-1]
DR CTD; 134637; -.
DR DisGeNET; 134637; -.
DR GeneCards; ADAT2; -.
DR HGNC; HGNC:21172; ADAT2.
DR HPA; ENSG00000189007; Low tissue specificity.
DR MIM; 615388; gene.
DR neXtProt; NX_Q7Z6V5; -.
DR OpenTargets; ENSG00000189007; -.
DR PharmGKB; PA162375592; -.
DR VEuPathDB; HostDB:ENSG00000189007; -.
DR eggNOG; KOG1018; Eukaryota.
DR GeneTree; ENSGT00390000000280; -.
DR HOGENOM; CLU_025810_8_3_1; -.
DR InParanoid; Q7Z6V5; -.
DR OMA; PCQMCAG; -.
DR OrthoDB; 1616309at2759; -.
DR PhylomeDB; Q7Z6V5; -.
DR TreeFam; TF313782; -.
DR PathwayCommons; Q7Z6V5; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q7Z6V5; -.
DR BioGRID-ORCS; 134637; 335 hits in 1080 CRISPR screens.
DR ChiTaRS; ADAT2; human.
DR EvolutionaryTrace; Q7Z6V5; -.
DR GenomeRNAi; 134637; -.
DR Pharos; Q7Z6V5; Tbio.
DR PRO; PR:Q7Z6V5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z6V5; protein.
DR Bgee; ENSG00000189007; Expressed in rectum and 131 other tissues.
DR Genevisible; Q7Z6V5; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Metal-binding;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..191
FT /note="tRNA-specific adenosine deaminase 2"
FT /id="PRO_0000287653"
FT DOMAIN 20..145
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.7"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_025582"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:3DH1"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3DH1"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:3DH1"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3DH1"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:3DH1"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:3DH1"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3DH1"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3DH1"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3DH1"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3DH1"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3DH1"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:3DH1"
SQ SEQUENCE 191 AA; 21046 MW; 7F2881A100A1782E CRC64;
MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN
EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP
LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK
SKVRKKECQK S
