ADAT3_HUMAN
ID ADAT3_HUMAN Reviewed; 351 AA.
AC Q96EY9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable inactive tRNA-specific adenosine deaminase-like protein 3;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT3;
GN Name=ADAT3; Synonyms=TAD3;
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].
RC TISSUE=Skin;
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 [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-332.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [5]
RP VARIANT NEDBGF MET-128.
RX PubMed=23620220; DOI=10.1136/jmedgenet-2012-101378;
RA Alazami A.M., Hijazi H., Al-Dosari M.S., Shaheen R., Hashem A.,
RA Aldahmesh M.A., Mohamed J.Y., Kentab A., Salih M.A., Awaji A.,
RA Masoodi T.A., Alkuraya F.S.;
RT "Mutation in ADAT3, encoding adenosine deaminase acting on transfer RNA,
RT causes intellectual disability and strabismus.";
RL J. Med. Genet. 50:425-430(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q96EY9; P32320: CDA; NbExp=3; IntAct=EBI-3922811, EBI-9250559;
CC Q96EY9; Q8WUP2: FBLIM1; NbExp=3; IntAct=EBI-3922811, EBI-3864120;
CC Q96EY9; O60504: SORBS3; NbExp=3; IntAct=EBI-3922811, EBI-741237;
CC -!- DISEASE: Neurodevelopmental disorder with brain abnormalities, poor
CC growth, and dysmorphic facies (NEDBGF) [MIM:615286]: An autosomal
CC recessive disorder characterized by global developmental delay,
CC impaired intellectual development, and speech delay apparent from
CC infancy or early childhood. Most patients have dysmorphic facial
CC features, and white matter abnormalities on brain imaging. More
CC variable features may include teeth anomalies, distal joint
CC contractures, spasticity, peripheral neuropathy, and behavioral
CC problems. {ECO:0000269|PubMed:23620220}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Val-225 is present instead of the conserved Glu which is an
CC active site in the cytidine and deoxycytidylate deaminase family of
CC enzymes. It is suggested that this protein may act as a regulatory
CC subunit. {ECO:0000305}.
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DR EMBL; BC011824; AAH11824.1; -; mRNA.
DR RefSeq; NP_001316462.1; NM_001329533.1.
DR RefSeq; NP_612431.2; NM_138422.3.
DR AlphaFoldDB; Q96EY9; -.
DR SMR; Q96EY9; -.
DR BioGRID; 125231; 24.
DR IntAct; Q96EY9; 6.
DR STRING; 9606.ENSP00000332448; -.
DR iPTMnet; Q96EY9; -.
DR PhosphoSitePlus; Q96EY9; -.
DR BioMuta; ADAT3; -.
DR DMDM; 74731634; -.
DR EPD; Q96EY9; -.
DR jPOST; Q96EY9; -.
DR MassIVE; Q96EY9; -.
DR MaxQB; Q96EY9; -.
DR PaxDb; Q96EY9; -.
DR PeptideAtlas; Q96EY9; -.
DR PRIDE; Q96EY9; -.
DR ProteomicsDB; 76475; -.
DR DNASU; 113179; -.
DR GeneID; 113179; -.
DR KEGG; hsa:113179; -.
DR CTD; 113179; -.
DR DisGeNET; 113179; -.
DR GeneCards; ADAT3; -.
DR HGNC; HGNC:25151; ADAT3.
DR MalaCards; ADAT3; -.
DR MIM; 615286; phenotype.
DR MIM; 615302; gene.
DR neXtProt; NX_Q96EY9; -.
DR Orphanet; 363528; Intellectual disability-strabismus syndrome.
DR PharmGKB; PA162375609; -.
DR eggNOG; KOG2771; Eukaryota.
DR InParanoid; Q96EY9; -.
DR OrthoDB; 1301800at2759; -.
DR PhylomeDB; Q96EY9; -.
DR TreeFam; TF313277; -.
DR PathwayCommons; Q96EY9; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q96EY9; -.
DR BioGRID-ORCS; 113179; 329 hits in 1071 CRISPR screens.
DR GenomeRNAi; 113179; -.
DR Pharos; Q96EY9; Tdark.
DR PRO; PR:Q96EY9; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q96EY9; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Disease variant; Intellectual disability; Metal-binding;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..351
FT /note="Probable inactive tRNA-specific adenosine deaminase-
FT like protein 3"
FT /id="PRO_0000287658"
FT DOMAIN 171..336
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VARIANT 128
FT /note="V -> M (in NEDBGF)"
FT /evidence="ECO:0000269|PubMed:23620220"
FT /id="VAR_069778"
FT VARIANT 332
FT /note="R -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035804"
SQ SEQUENCE 351 AA; 38071 MW; 6CE25F534BBE92F9 CRC64;
MEPAPGLVEQ PKCLEAGSPE PEPAPWQALP VLSEKQSGDV ELVLAYAAPV LDKRQTSRLL
KEVSALHPLP AQPHLKRVRP SRDAGSPHAL EMLLCLAGPA SGPRSLAELL PRPAVDPRGL
GQPFLVPVPA RPPLTRGQFE EARAHWPTSF HEDKQVTSAL AGRLFSTQER AAMQSHMERA
VWAARRAAAR GLRAVGAVVV DPASDRVLAT GHDCSCADNP LLHAVMVCVD LVARGQGRGT
YDFRPFPACS FAPAAAPQAV RAGAVRKLDA DEDGLPYLCT GYDLYVTREP CAMCAMALVH
ARILRVFYGA PSPDGALGTR FRIHARPDLN HRFQVFRGVL EEQCRWLDPD T
