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   08-NOV-2023, entry version 142.
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; 26.
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; 9606-ENSP00000332448; -.
DR   PeptideAtlas; Q96EY9; -.
DR   ProteomicsDB; 76475; -.
DR   Pumba; Q96EY9; -.
DR   DNASU; 113179; -.
DR   GeneID; 113179; -.
DR   KEGG; hsa:113179; -.
DR   AGR; HGNC:25151; -.
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; 1342940at2759; -.
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; 336 hits in 1142 CRISPR screens.
DR   GenomeRNAi; 113179; -.
DR   Pharos; Q96EY9; Tdark.
DR   PRO; PR:Q96EY9; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q96EY9; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   CDD; cd01285; nucleoside_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11079:SF156; INACTIVE TRNA-SPECIFIC ADENOSINE DEAMINASE-LIKE PROTEIN 3-RELATED; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 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
//