ID   TSN_BOVIN               Reviewed;         228 AA.
AC   Q08DM8; A1L5B5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Translin;
DE            EC=3.1.-.-;
DE   AltName: Full=Component 3 of promoter of RISC;
DE            Short=C3PO;
GN   Name=TSN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits,
CC       DNA/RNA binding occurs inside the ring. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR   EMBL; BT029902; ABM06148.1; -; mRNA.
DR   EMBL; BC123663; AAI23664.1; -; mRNA.
DR   RefSeq; NP_001068890.1; NM_001075422.1.
DR   AlphaFoldDB; Q08DM8; -.
DR   SMR; Q08DM8; -.
DR   STRING; 9913.ENSBTAP00000007959; -.
DR   PaxDb; Q08DM8; -.
DR   PRIDE; Q08DM8; -.
DR   Ensembl; ENSBTAT00000069948; ENSBTAP00000059780; ENSBTAG00000006059.
DR   GeneID; 509943; -.
DR   KEGG; bta:509943; -.
DR   CTD; 7247; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006059; -.
DR   VGNC; VGNC:36422; TSN.
DR   eggNOG; KOG3067; Eukaryota.
DR   GeneTree; ENSGT00940000153568; -.
DR   HOGENOM; CLU_079179_0_0_1; -.
DR   InParanoid; Q08DM8; -.
DR   OMA; LHAGFQI; -.
DR   OrthoDB; 1187354at2759; -.
DR   TreeFam; TF323690; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000006059; Expressed in choroid plexus and 104 other tissues.
DR   ExpressionAtlas; Q08DM8; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:1902555; C:endoribonuclease complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..228
FT                   /note="Translin"
FT                   /id="PRO_0000270209"
FT   REGION          86..90
FT                   /note="DNA/RNA binding"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   228 AA;  26169 MW;  4BAAF20BEA7C4B6C CRC64;
     MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK
     AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLES ETLVTREAVT
     EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
     FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK