ID A0A2U3V9F7_TURTR Unreviewed; 228 AA.
AC A0A2U3V9F7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Translin {ECO:0000256|ARBA:ARBA00022196};
DE AltName: Full=Component 3 of promoter of RISC {ECO:0000256|ARBA:ARBA00030513};
GN Name=TSN {ECO:0000313|RefSeq:XP_004329236.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_004329236.1};
RN [1] {ECO:0000313|RefSeq:XP_004329236.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_004329236.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00025374}.
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:0000256|ARBA:ARBA00025410}.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits,
CC DNA/RNA binding occurs inside the ring.
CC {ECO:0000256|ARBA:ARBA00011685}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the translin family.
CC {ECO:0000256|ARBA:ARBA00005902}.
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DR RefSeq; XP_004329236.1; XM_004329188.3.
DR AlphaFoldDB; A0A2U3V9F7; -.
DR SMR; A0A2U3V9F7; -.
DR STRING; 9739.ENSTTRP00000005532; -.
DR Ensembl; ENSTTRT00000005851; ENSTTRP00000005532; ENSTTRG00000005854.
DR GeneID; 101336968; -.
DR InParanoid; A0A2U3V9F7; -.
DR OMA; DAFHFTI; -.
DR OrthoDB; 5472346at2759; -.
DR Proteomes; UP000245320; Chromosome 7.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 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:SF2; TRANSLIN; 1.
DR PANTHER; PTHR10741; TRANSLIN AND TRANSLIN ASSOCIATED PROTEIN X; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; Translin; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Magnesium {ECO:0000256|PIRSR:PIRSR602848-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602848-1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
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
//
