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Database: UniProt
Entry: F1RXY7_PIG
LinkDB: F1RXY7_PIG
Original site: F1RXY7_PIG 
ID   F1RXY7_PIG              Unreviewed;       206 AA.
AC   F1RXY7; A0A287AYW6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 4.
DT   27-MAR-2024, entry version 80.
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|Ensembl:ENSSSCP00000016669.4,
GN   ECO:0000313|VGNC:VGNC:95556};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016669.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016669.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016669.4,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000016669.4}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; F1RXY7; -.
DR   PeptideAtlas; F1RXY7; -.
DR   Ensembl; ENSSSCT00000017129.5; ENSSSCP00000016669.4; ENSSSCG00000015729.5.
DR   VGNC; VGNC:95556; TSN.
DR   GeneTree; ENSGT00940000153568; -.
DR   HOGENOM; CLU_079179_3_0_1; -.
DR   TreeFam; TF323690; -.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Bgee; ENSSSCG00000015729; Expressed in oocyte and 42 other cell types or tissues.
DR   ExpressionAtlas; F1RXY7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016070; P:RNA metabolic process; IEA:InterPro.
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:UP000008227};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
SQ   SEQUENCE   206 AA;  23675 MW;  636C1E6548B88D34 CRC64;
     EIRKVVQSLE QTAREILTLL QGVHQGAGFQ DIPKRCLKAR EHFGTVKTHL TSLKTKFPAE
     QYYRFHEHWR FVLQRLVFLA AFVVYLESET LVTREAVTEI LGIEPDREKG FHLDVEDYLS
     GVLILASELS RLSVNSVTAG DYARPLHIST FINELDSGFR LLNLKNDSLR KRYDGLKYDV
     KKVEEVVYDL SIRGFNKETV AACSEK
//
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