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TATD1_MOUSE
ID   TATD1_MOUSE             Reviewed;         295 AA.
AC   Q6P8M1; Q8BY37;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Deoxyribonuclease TATDN1;
DE            EC=3.1.21.-;
GN   Name=Tatdn1;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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 1).
RC   TISSUE=Testis;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and 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).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-46, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Deoxyribonuclease which catalyzes (in vitro) the decatenation
CC       of kinetoplast DNA, which are circular DNA catenated to each other,
CC       producing linear DNA molecules (By similarity). Plays an important role
CC       in chromosomal segregation and cell cycle progression during eye
CC       development probably via its DNA decatenation activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q6GML7}.
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=2;
CC       Name=1;
CC         IsoId=Q6P8M1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P8M1-2; Sequence=VSP_030046, VSP_030047;
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
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DR   EMBL; AK042248; BAC31203.1; -; mRNA.
DR   EMBL; BC061187; AAH61187.1; -; mRNA.
DR   CCDS; CCDS88768.1; -. [Q6P8M1-1]
DR   RefSeq; NP_780360.1; NM_175151.4.
DR   RefSeq; XP_006521428.1; XM_006521365.3.
DR   AlphaFoldDB; Q6P8M1; -.
DR   SMR; Q6P8M1; -.
DR   BioGRID; 213619; 9.
DR   STRING; 10090.ENSMUSP00000105783; -.
DR   iPTMnet; Q6P8M1; -.
DR   PhosphoSitePlus; Q6P8M1; -.
DR   EPD; Q6P8M1; -.
DR   MaxQB; Q6P8M1; -.
DR   PaxDb; Q6P8M1; -.
DR   PeptideAtlas; Q6P8M1; -.
DR   PRIDE; Q6P8M1; -.
DR   ProteomicsDB; 254817; -. [Q6P8M1-1]
DR   ProteomicsDB; 254818; -. [Q6P8M1-2]
DR   Antibodypedia; 13907; 95 antibodies from 19 providers.
DR   DNASU; 69694; -.
DR   Ensembl; ENSMUST00000228538; ENSMUSP00000154677; ENSMUSG00000050891. [Q6P8M1-1]
DR   GeneID; 69694; -.
DR   KEGG; mmu:69694; -.
DR   UCSC; uc007vtr.1; mouse. [Q6P8M1-2]
DR   UCSC; uc007vtt.1; mouse. [Q6P8M1-1]
DR   CTD; 83940; -.
DR   MGI; MGI:1916944; Tatdn1.
DR   VEuPathDB; HostDB:ENSMUSG00000050891; -.
DR   eggNOG; KOG3020; Eukaryota.
DR   GeneTree; ENSGT00940000156272; -.
DR   InParanoid; Q6P8M1; -.
DR   OMA; PNEAPRI; -.
DR   OrthoDB; 897451at2759; -.
DR   PhylomeDB; Q6P8M1; -.
DR   TreeFam; TF324192; -.
DR   BioGRID-ORCS; 69694; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Tatdn1; mouse.
DR   PRO; PR:Q6P8M1; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q6P8M1; protein.
DR   Bgee; ENSMUSG00000050891; Expressed in knee joint and 226 other tissues.
DR   ExpressionAtlas; Q6P8M1; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; 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   PIRSF; PIRSF005902; DNase_TatD; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01091; TATD_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..295
FT                   /note="Deoxyribonuclease TATDN1"
FT                   /id="PRO_0000313591"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         222
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   MOD_RES         27
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         46
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   VAR_SEQ         264
FT                   /note="I -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030046"
FT   VAR_SEQ         265
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030047"
SQ   SEQUENCE   295 AA;  33365 MW;  2731F702DBE57CB8 CRC64;
     MSLFKFVDIG INLTDPMFRG IYRGVQKHQD DLQDVIERAI QIGVKKFMIT GGSLQDSKDA
     LQLAQTNDMF FSTVGCHPTR CDEFEKGSPD QYLAGLLSLA ENNKGKVVAI GECGLDFDRL
     QFCPKDTQLK YFEKQFELSE QTQLPMFLHC RNSHTEFLDI MRRNRDRYVG GVVHSFDGTK
     EAAAALVDLG LYIGFNGCSL KTEANLEVLK SIPSEKLMIE TDAPWCGVKS THAGSKYINT
     SFPTKKKWEN GHCLKDRNEP CHIIQILEIM SAVREEDPLE LANTLYNNTI KVFFS
 
 
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