ADAT1_HUMAN
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 03-AUG-2022, entry version 139.
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; 7.
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; Q9BUB4; -.
DR PeptideAtlas; Q9BUB4; -.
DR PRIDE; Q9BUB4; -.
DR ProteomicsDB; 79070; -. [Q9BUB4-1]
DR ProteomicsDB; 79071; -. [Q9BUB4-2]
DR Antibodypedia; 16832; 168 antibodies from 22 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 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; IGRCQNV; -.
DR OrthoDB; 947117at2759; -.
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; 7 hits in 1073 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 169 other 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:0008033; P:tRNA processing; IMP:UniProtKB.
DR InterPro; IPR002466; A_deamin.
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
