TSN_MOUSE
ID TSN_MOUSE Reviewed; 228 AA.
AC Q62348;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Translin;
DE EC=3.1.-.-;
DE AltName: Full=Component 3 of promoter of RISC;
DE Short=C3PO;
DE AltName: Full=Testis/brain RNA-binding protein;
DE Short=TB-RBP;
GN Name=Tsn;
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 [MRNA].
RC TISSUE=Thymus;
RX PubMed=9244443; DOI=10.1006/geno.1997.4796;
RA Aoki K., Inazawa J., Takahashi T., Nakahara K., Kasai M.;
RT "Genomic structure and chromosomal localization of the gene encoding
RT translin, a recombination hotspot binding protein.";
RL Genomics 43:237-241(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 DNA/RNA-BINDING REGION.
RX PubMed=10025964; DOI=10.1016/s0014-5793(99)00010-1;
RA Aoki K., Suzuki K., Ishida R., Kasai M.;
RT "The DNA binding activity of Translin is mediated by a basic region in the
RT ring-shaped structure conserved in evolution.";
RL FEBS Lett. 443:363-366(1999).
RN [4]
RP FUNCTION IN RISC ACTIVATION, AND ENDONUCLEASE ACTIVITY.
RX PubMed=15491149; DOI=10.1021/bi048847l;
RA Wang J., Boja E.S., Oubrahim H., Chock P.B.;
RT "Testis brain ribonucleic acid-binding protein/translin possesses both
RT single-stranded and double-stranded ribonuclease activities.";
RL Biochemistry 43:13424-13431(2004).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), AND SUBUNIT.
RX PubMed=12079346; DOI=10.1016/s0022-2836(02)00364-9;
RA Pascal J.M., Hart P.J., Hecht N.B., Robertus J.D.;
RT "Crystal structure of TB-RBP, a novel RNA-binding and regulating protein.";
RL J. Mol. Biol. 319:1049-1057(2002).
CC -!- FUNCTION: DNA-binding protein that specifically recognizes consensus
CC sequences at the breakpoint junctions in chromosomal translocations,
CC mostly involving immunoglobulin (Ig)/T-cell receptor gene segments.
CC Seems to recognize single-stranded DNA ends generated by staggered
CC breaks occurring at recombination hot spots.
CC {ECO:0000269|PubMed:15491149}.
CC -!- FUNCTION: Exhibits both single-stranded and double-stranded
CC endoribonuclease activity. May act as an activator of RNA-induced
CC silencing complex (RISC) by facilitating endonucleolytic cleavage of
CC the siRNA passenger strand. {ECO:0000269|PubMed:15491149}.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits,
CC DNA/RNA binding occurs inside the ring. {ECO:0000269|PubMed:12079346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus.
CC -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR EMBL; X81464; CAA57222.1; -; mRNA.
DR EMBL; Y12568; CAA73151.1; -; Genomic_DNA.
DR EMBL; Y12569; CAA73151.1; JOINED; Genomic_DNA.
DR EMBL; Y12570; CAA73151.1; JOINED; Genomic_DNA.
DR EMBL; Y12571; CAA73151.1; JOINED; Genomic_DNA.
DR EMBL; Y12572; CAA73151.1; JOINED; Genomic_DNA.
DR EMBL; BC004615; AAH04615.1; -; mRNA.
DR CCDS; CCDS35690.1; -.
DR RefSeq; NP_035780.1; NM_011650.3.
DR PDB; 1KEY; X-ray; 2.65 A; A/B/C/D=1-228.
DR PDBsum; 1KEY; -.
DR AlphaFoldDB; Q62348; -.
DR SMR; Q62348; -.
DR BioGRID; 204347; 15.
DR ComplexPortal; CPX-4629; C3PO endoribonuclease complex.
DR STRING; 10090.ENSMUSP00000027623; -.
DR iPTMnet; Q62348; -.
DR PhosphoSitePlus; Q62348; -.
DR EPD; Q62348; -.
DR jPOST; Q62348; -.
DR MaxQB; Q62348; -.
DR PaxDb; Q62348; -.
DR PRIDE; Q62348; -.
DR ProteomicsDB; 297996; -.
DR Antibodypedia; 33410; 234 antibodies from 34 providers.
DR Ensembl; ENSMUST00000027623; ENSMUSP00000027623; ENSMUSG00000026374.
DR GeneID; 22099; -.
DR KEGG; mmu:22099; -.
DR UCSC; uc007cib.1; mouse.
DR CTD; 7247; -.
DR MGI; MGI:109263; Tsn.
DR VEuPathDB; HostDB:ENSMUSG00000026374; -.
DR eggNOG; KOG3067; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_079179_0_0_1; -.
DR InParanoid; Q62348; -.
DR OMA; LHAGFQI; -.
DR OrthoDB; 1187354at2759; -.
DR PhylomeDB; Q62348; -.
DR TreeFam; TF323690; -.
DR Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
DR BioGRID-ORCS; 22099; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tsn; mouse.
DR EvolutionaryTrace; Q62348; -.
DR PRO; PR:Q62348; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q62348; protein.
DR Bgee; ENSMUSG00000026374; Expressed in respiratory primordium and 253 other tissues.
DR ExpressionAtlas; Q62348; baseline and differential.
DR Genevisible; Q62348; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:1902555; C:endoribonuclease complex; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0030422; P:siRNA processing; ISO:MGI.
DR CDD; cd14819; Translin; 1.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
DR InterPro; IPR033956; Translin.
DR InterPro; IPR016069; Translin_C.
DR InterPro; IPR002848; Translin_fam.
DR InterPro; IPR016068; Translin_N.
DR InterPro; IPR036081; Translin_sf.
DR PANTHER; PTHR10741; PTHR10741; 1.
DR PANTHER; PTHR10741:SF2; PTHR10741:SF2; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA-binding; Endonuclease; Hydrolase;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..228
FT /note="Translin"
FT /id="PRO_0000191684"
FT REGION 86..90
FT /note="DNA/RNA binding"
FT REGION 177..198
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15631"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15631"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15631"
FT HELIX 3..43
FT /evidence="ECO:0007829|PDB:1KEY"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 54..75
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 92..110
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:1KEY"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:1KEY"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1KEY"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:1KEY"
SQ SEQUENCE 228 AA; 26201 MW; 39FBB4FCC5AA375C CRC64;
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGTG FQDIPKRCLK
AREHFSTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT
EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACGEK
