TATD3_MOUSE
ID TATD3_MOUSE Reviewed; 294 AA.
AC Q3U1C6; Q6P8H6; Q9DB58;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative deoxyribonuclease TATDN3;
DE EC=3.1.21.-;
GN Name=Tatdn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U1C6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1C6-2; Sequence=VSP_030051;
CC Name=3;
CC IsoId=Q3U1C6-3; Sequence=VSP_030049, VSP_030050;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005193; BAB23875.1; -; mRNA.
DR EMBL; AK156071; BAE33572.1; -; mRNA.
DR EMBL; BC061248; AAH61248.1; ALT_INIT; mRNA.
DR CCDS; CCDS48484.1; -. [Q3U1C6-3]
DR CCDS; CCDS48485.1; -. [Q3U1C6-1]
DR RefSeq; NP_001156894.1; NM_001163422.1. [Q3U1C6-3]
DR AlphaFoldDB; Q3U1C6; -.
DR SMR; Q3U1C6; -.
DR STRING; 10090.ENSMUSP00000106518; -.
DR PhosphoSitePlus; Q3U1C6; -.
DR MaxQB; Q3U1C6; -.
DR PaxDb; Q3U1C6; -.
DR PRIDE; Q3U1C6; -.
DR ProteomicsDB; 263253; -. [Q3U1C6-1]
DR ProteomicsDB; 263254; -. [Q3U1C6-2]
DR ProteomicsDB; 263255; -. [Q3U1C6-3]
DR Antibodypedia; 51781; 30 antibodies from 13 providers.
DR Ensembl; ENSMUST00000085633; ENSMUSP00000082773; ENSMUSG00000026632. [Q3U1C6-3]
DR GeneID; 68972; -.
DR KEGG; mmu:68972; -.
DR UCSC; uc007ebz.2; mouse. [Q3U1C6-3]
DR CTD; 128387; -.
DR MGI; MGI:1916222; Tatdn3.
DR VEuPathDB; HostDB:ENSMUSG00000026632; -.
DR eggNOG; KOG3020; Eukaryota.
DR GeneTree; ENSGT00720000108846; -.
DR HOGENOM; CLU_031506_7_0_1; -.
DR InParanoid; Q3U1C6; -.
DR BioGRID-ORCS; 68972; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tatdn3; mouse.
DR PRO; PR:Q3U1C6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U1C6; protein.
DR Bgee; ENSMUSG00000026632; Expressed in spermatocyte and 216 other tissues.
DR ExpressionAtlas; Q3U1C6; baseline and differential.
DR Genevisible; Q3U1C6; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..294
FT /note="Putative deoxyribonuclease TATDN3"
FT /id="PRO_0000313596"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT VAR_SEQ 160..189
FT /note="GAEQVLLHAFDGRPSVAMEGVRAGYYFSIP -> EAEACETAASEFYLLRNR
FT FTCARTRKADTE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030049"
FT VAR_SEQ 190..294
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030050"
FT VAR_SEQ 225..236
FT /note="TRNEPCNISIAA -> LCSLSDTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030051"
FT CONFLICT 27
FT /note="K -> R (in Ref. 1; BAB23875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 32436 MW; 8BD2EDF6678D75F4 CRC64;
MGLGLVDCHC HLSASDFDND LDDVLEKARK ANVMALVAVA EHAGEFERIM QLSERYNGFV
LPCLGVHPVQ ELSPEKPRSV TLKDLDVALP IIEKYKDRLL AIGEVGLDFT PRYAGTDEEK
EEQRQVLIRQ VQLAKRLNVP LNVHSRSAGR PTISLLREQG AEQVLLHAFD GRPSVAMEGV
RAGYYFSIPP SIVRSGQKQK LVKQLPLSSI CLETDSPALG PEKLTRNEPC NISIAAEFIA
QVKGISVEEV REVTTRNAFR LFPKLQSLLQ KELQSHPLQA KSAQGSAGES KGLL
