TATD2_HUMAN
ID TATD2_HUMAN Reviewed; 761 AA.
AC Q93075; Q3MIL9; Q5BKU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Putative deoxyribonuclease TATDN2;
DE EC=3.1.21.-;
GN Name=TATDN2; Synonyms=KIAA0218;
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], AND VARIANT LEU-358.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-256.
RC TISSUE=Brain, and Lymph;
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=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q17R31};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q17R31};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13208.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D86972; BAA13208.2; ALT_INIT; mRNA.
DR EMBL; CH471055; EAW64070.1; -; Genomic_DNA.
DR EMBL; BC090935; AAH90935.1; -; mRNA.
DR EMBL; BC101770; AAI01771.1; -; mRNA.
DR EMBL; BC101776; AAI01777.1; -; mRNA.
DR CCDS; CCDS33698.1; -.
DR RefSeq; NP_055575.3; NM_014760.3.
DR AlphaFoldDB; Q93075; -.
DR SMR; Q93075; -.
DR BioGRID; 115140; 15.
DR IntAct; Q93075; 4.
DR STRING; 9606.ENSP00000287652; -.
DR GlyGen; Q93075; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q93075; -.
DR PhosphoSitePlus; Q93075; -.
DR BioMuta; TATDN2; -.
DR DMDM; 209572689; -.
DR EPD; Q93075; -.
DR jPOST; Q93075; -.
DR MassIVE; Q93075; -.
DR MaxQB; Q93075; -.
DR PaxDb; Q93075; -.
DR PeptideAtlas; Q93075; -.
DR PRIDE; Q93075; -.
DR ProteomicsDB; 75704; -.
DR Antibodypedia; 49486; 11 antibodies from 6 providers.
DR DNASU; 9797; -.
DR Ensembl; ENST00000287652.8; ENSP00000287652.4; ENSG00000157014.11.
DR Ensembl; ENST00000448281.7; ENSP00000408736.2; ENSG00000157014.11.
DR GeneID; 9797; -.
DR KEGG; hsa:9797; -.
DR MANE-Select; ENST00000448281.7; ENSP00000408736.2; NM_014760.4; NP_055575.3.
DR UCSC; uc003bvf.4; human.
DR CTD; 9797; -.
DR GeneCards; TATDN2; -.
DR HGNC; HGNC:28988; TATDN2.
DR HPA; ENSG00000157014; Low tissue specificity.
DR MIM; 619330; gene.
DR neXtProt; NX_Q93075; -.
DR OpenTargets; ENSG00000157014; -.
DR PharmGKB; PA134959721; -.
DR VEuPathDB; HostDB:ENSG00000157014; -.
DR eggNOG; KOG3020; Eukaryota.
DR GeneTree; ENSGT00940000155616; -.
DR HOGENOM; CLU_019741_1_0_1; -.
DR InParanoid; Q93075; -.
DR OMA; ATDYVMY; -.
DR OrthoDB; 207731at2759; -.
DR PhylomeDB; Q93075; -.
DR TreeFam; TF324192; -.
DR PathwayCommons; Q93075; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q93075; -.
DR BioGRID-ORCS; 9797; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; TATDN2; human.
DR GenomeRNAi; 9797; -.
DR Pharos; Q93075; Tdark.
DR PRO; PR:Q93075; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q93075; protein.
DR Bgee; ENSG00000157014; Expressed in type B pancreatic cell and 196 other tissues.
DR ExpressionAtlas; Q93075; baseline and differential.
DR Genevisible; Q93075; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR CDD; cd01310; TatD_DNAse; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01137; TATD_1; 1.
DR PROSITE; PS01090; TATD_2; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..761
FT /note="Putative deoxyribonuclease TATDN2"
FT /id="PRO_0000201993"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 499
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 501
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 593
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 593
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 630
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 655
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 707
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT VARIANT 217
FT /note="H -> R (in dbSNP:rs2241314)"
FT /id="VAR_047028"
FT VARIANT 256
FT /note="V -> I (in dbSNP:rs394558)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047029"
FT VARIANT 358
FT /note="P -> L (in dbSNP:rs2075352)"
FT /evidence="ECO:0000269|PubMed:9039502"
FT /id="VAR_047030"
SQ SEQUENCE 761 AA; 85023 MW; 11BF3683608EE617 CRC64;
MASERGKVKH NWSSTSEGCP RKRSCLREPC DVAPSSRPAQ RSASRSGGPS SPKRLKAQKE
DDVACSRRLS WGSSRRRNNS SSSFSPHFLG PGVGGAASKG CLIRNTRGFL SSGGSPLRPA
NASLEEMASL EEEACSLKVD SKDSSHNSTN SEFAAEAEGQ NDTIEEPNKV QKRKRDRLRD
QGSTMIYLKA IQGILGKSMP KRKGEAATRA KPSAAEHPSH GEGPARSEGP AKTAEGAARS
VTVTAAQKEK DATPEVSMEE DKTVPERSSF YDRRVVIDPQ EKPSEEPLGD RRTVIDKCSP
PLEFLDDSDS HLEIQKHKDR EVVMEHPSSG SDWSDVEEIS TVRFSQEEPV SLKPSAVPEP
SSFTTDYVMY PPHLYSSPWC DYASYWTSSP KPSSYPSTGS SSNDAAQVGK SSRSRMSDYS
PNSTGSVQNT SRDMEASEEG WSQNSRSFRF SRSSEEREVK EKRTFQEEMP PRPCGGHASS
SLPKSHLEPS LEEGFIDTHC HLDMLYSKLS FQGTFTKFRK IYSSSFPKEF QGCISDFCDP
RTLTDCLWEE LLKEDLVWGA FGCHPHFARY YSESQERNLL QALRHPKAVA FGEMGLDYSY
KCTTPVPEQH KVFERQLQLA VSLKKPLVIH CREADEDLLE IMKKFVPPDY KIHRHCFTGS
YPVIEPLLKY FPNMSVGFTA VLTYSSAWEA REALRQIPLE RIIVETDAPY FLPRQVPKSL
CQYAHPGLAL HTVREIARVK DQPLSLTLAA LRENTSRLYS L
