ID   ADAT1_HUMAN             Reviewed;         502 AA.
AC   Q9BUB4; Q9NVB7; Q9UNG3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=tRNA-specific adenosine deaminase 1;
DE            Short=hADAT1;
DE            EC=3.5.4.34;
DE   AltName: Full=tRNA-specific adenosine-37 deaminase;
GN   Name=ADAT1;
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 [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND VARIANT ASN-167.
RC   TISSUE=Brain;
RX   PubMed=10430867; DOI=10.1073/pnas.96.16.8895;
RA   Maas S., Gerber A.P., Rich A.;
RT   "Identification and characterization of a human tRNA-specific adenosine
RT   deaminase related to the ADAR family of pre-mRNA editing enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:8895-8900(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Teratocarcinoma;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in
CC         tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855,
CC         Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34;
CC         Evidence={ECO:0000269|PubMed:10430867};
CC   -!- COFACTOR:
CC       Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC       {ECO:0000250};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BUB4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BUB4-2; Sequence=VSP_025579;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10430867}.
CC   -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
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DR   EMBL; AF125188; AAD48376.1; -; mRNA.
DR   EMBL; AK001687; BAA91837.1; -; mRNA.
DR   EMBL; BC002758; AAH02758.1; -; mRNA.
DR   CCDS; CCDS10922.1; -. [Q9BUB4-1]
DR   RefSeq; NP_001311373.1; NM_001324444.1. [Q9BUB4-2]
DR   RefSeq; NP_001311374.1; NM_001324445.1. [Q9BUB4-1]
DR   RefSeq; NP_001311375.1; NM_001324446.1. [Q9BUB4-2]
DR   RefSeq; NP_036223.2; NM_012091.4. [Q9BUB4-1]
DR   AlphaFoldDB; Q9BUB4; -.
DR   SMR; Q9BUB4; -.
DR   BioGRID; 117081; 11.
DR   IntAct; Q9BUB4; 1.
DR   MINT; Q9BUB4; -.
DR   STRING; 9606.ENSP00000310015; -.
DR   iPTMnet; Q9BUB4; -.
DR   PhosphoSitePlus; Q9BUB4; -.
DR   BioMuta; ADAT1; -.
DR   DMDM; 74733201; -.
DR   EPD; Q9BUB4; -.
DR   jPOST; Q9BUB4; -.
DR   MassIVE; Q9BUB4; -.
DR   MaxQB; Q9BUB4; -.
DR   PaxDb; 9606-ENSP00000310015; -.
DR   PeptideAtlas; Q9BUB4; -.
DR   ProteomicsDB; 79070; -. [Q9BUB4-1]
DR   ProteomicsDB; 79071; -. [Q9BUB4-2]
DR   Pumba; Q9BUB4; -.
DR   Antibodypedia; 16832; 176 antibodies from 23 providers.
DR   DNASU; 23536; -.
DR   Ensembl; ENST00000307921.7; ENSP00000310015.3; ENSG00000065457.11. [Q9BUB4-1]
DR   Ensembl; ENST00000564657.2; ENSP00000457501.2; ENSG00000065457.11. [Q9BUB4-1]
DR   GeneID; 23536; -.
DR   KEGG; hsa:23536; -.
DR   MANE-Select; ENST00000564657.2; ENSP00000457501.2; NM_001324445.2; NP_001311374.1.
DR   UCSC; uc002feo.3; human. [Q9BUB4-1]
DR   AGR; HGNC:228; -.
DR   CTD; 23536; -.
DR   GeneCards; ADAT1; -.
DR   HGNC; HGNC:228; ADAT1.
DR   HPA; ENSG00000065457; Low tissue specificity.
DR   MIM; 604230; gene.
DR   neXtProt; NX_Q9BUB4; -.
DR   OpenTargets; ENSG00000065457; -.
DR   PharmGKB; PA24558; -.
DR   VEuPathDB; HostDB:ENSG00000065457; -.
DR   eggNOG; KOG2777; Eukaryota.
DR   GeneTree; ENSGT00940000157942; -.
DR   HOGENOM; CLU_005382_5_2_1; -.
DR   InParanoid; Q9BUB4; -.
DR   OMA; QPLTCGY; -.
DR   OrthoDB; 118472at2759; -.
DR   PhylomeDB; Q9BUB4; -.
DR   TreeFam; TF315806; -.
DR   BRENDA; 3.5.4.34; 2681.
DR   PathwayCommons; Q9BUB4; -.
DR   Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR   SignaLink; Q9BUB4; -.
DR   BioGRID-ORCS; 23536; 10 hits in 1151 CRISPR screens.
DR   GenomeRNAi; 23536; -.
DR   Pharos; Q9BUB4; Tbio.
DR   PRO; PR:Q9BUB4; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9BUB4; Protein.
DR   Bgee; ENSG00000065457; Expressed in oocyte and 171 other cell types or tissues.
DR   ExpressionAtlas; Q9BUB4; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR   GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IMP:UniProtKB.
DR   GO; GO:0043829; F:tRNA-specific adenosine-37 deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IMP:UniProtKB.
DR   InterPro; IPR002466; A_deamin.
DR   PANTHER; PTHR46516; TRNA-SPECIFIC ADENOSINE DEAMINASE 1; 1.
DR   PANTHER; PTHR46516:SF1; TRNA-SPECIFIC ADENOSINE DEAMINASE 1; 1.
DR   Pfam; PF02137; A_deamin; 1.
DR   SMART; SM00552; ADEAMc; 1.
DR   PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Phosphoprotein;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..502
FT                   /note="tRNA-specific adenosine deaminase 1"
FT                   /id="PRO_0000287646"
FT   DOMAIN          63..501
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   REGION          174..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         93
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         302
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHI2"
FT   VAR_SEQ         1..149
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025579"
FT   VARIANT         167
FT                   /note="H -> N (in dbSNP:rs3743598)"
FT                   /evidence="ECO:0000269|PubMed:10430867"
FT                   /id="VAR_032340"
FT   VARIANT         203
FT                   /note="T -> N (in dbSNP:rs3743599)"
FT                   /id="VAR_032341"
FT   VARIANT         226
FT                   /note="I -> V (in dbSNP:rs56029288)"
FT                   /id="VAR_061098"
FT   VARIANT         242
FT                   /note="T -> P (in dbSNP:rs3743600)"
FT                   /id="VAR_055649"
FT   CONFLICT        61
FT                   /note="V -> I (in Ref. 1; AAD48376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="F -> L (in Ref. 2; BAA91837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="I -> T (in Ref. 1; AAD48376)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  55392 MW;  3664E4C50DA9DFE0 CRC64;
     MWTADEIAQL CYEHYGIRLP KKGKPEPNHE WTLLAAVVKI QSPADKACDT PDKPVQVTKE
     VVSMGTGTKC IGQSKMRKNG DILNDSHAEV IARRSFQRYL LHQLQLAATL KEDSIFVPGT
     QKGVWKLRRD LIFVFFSSHT PCGDASIIPM LEFEDQPCCP VFRNWAHNSS VEASSNLEAP
     GNERKCEDPD SPVTKKMRLE PGTAAREVTN GAAHHQSFGK QKSGPISPGI HSCDLTVEGL
     ATVTRIAPGS AKVIDVYRTG AKCVPGEAGD SGKPGAAFHQ VGLLRVKPGR GDRTRSMSCS
     DKMARWNVLG CQGALLMHLL EEPIYLSAVV IGKCPYSQEA MQRALIGRCQ NVSALPKGFG
     VQELKILQSD LLFEQSRSAV QAKRADSPGR LVPCGAAISW SAVPEQPLDV TANGFPQGTT
     KKTIGSLQAR SQISKVELFR SFQKLLSRIA RDKWPHSLRV QKLDTYQEYK EAASSYQEAW
     STLRKQVFGS WIRNPPDYHQ FK
//