TSN_PONAB
ID TSN_PONAB Reviewed; 228 AA.
AC Q5R7P2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Translin;
DE EC=3.1.-.-;
DE AltName: Full=Component 3 of promoter of RISC;
DE Short=C3PO;
GN Name=TSN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860070; CAH92218.1; -; mRNA.
DR RefSeq; NP_001128876.2; NM_001135404.2.
DR AlphaFoldDB; Q5R7P2; -.
DR SMR; Q5R7P2; -.
DR STRING; 9601.ENSPPYP00000014254; -.
DR GeneID; 100189807; -.
DR KEGG; pon:100189807; -.
DR CTD; 7247; -.
DR eggNOG; KOG3067; Eukaryota.
DR InParanoid; Q5R7P2; -.
DR OrthoDB; 1187354at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; 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:0016070; P:RNA metabolic process; IEA:InterPro.
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_0000270210"
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; 26201 MW; DCFBB71FBC3C1D3F CRC64;
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK
AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT
EILGMEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK
