TSNAX_RAT
ID TSNAX_RAT Reviewed; 290 AA.
AC Q9JHB5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translin-associated protein X;
DE AltName: Full=Translin-associated factor X;
GN Name=Tsnax; Synonyms=Trax;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION IN A DNA-BINDING COMPLEX WITH TSN.
RC TISSUE=Brain;
RX PubMed=9681436; DOI=10.1046/j.1471-4159.1998.71020471.x;
RA Taira E., Finkenstadt P.M., Baraban J.M.;
RT "Identification of translin and trax as components of the GS1 strand-
RT specific DNA binding complex enriched in brain.";
RL J. Neurochem. 71:471-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts in combination with TSN as an endonuclease involved in
CC the activation of the RNA-induced silencing complex (RISC). Possible
CC role in spermatogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits.
CC Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9. Interacts with the
CC homodimeric form of C1D following gamma-radiation. Interacts with TSN
CC and C1D in a mutually exclusive manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Golgi apparatus {ECO:0000269|PubMed:9681436}. Nucleus {ECO:0000250}.
CC Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in
CC the Golgi complex of mid-late pachytene spermatocytes (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum.
CC {ECO:0000269|PubMed:9681436}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR EMBL; AF262357; AAF76149.1; -; mRNA.
DR EMBL; BC081715; AAH81715.1; -; mRNA.
DR RefSeq; NP_071598.1; NM_022262.3.
DR AlphaFoldDB; Q9JHB5; -.
DR SMR; Q9JHB5; -.
DR IntAct; Q9JHB5; 1.
DR STRING; 10116.ENSRNOP00000063911; -.
DR iPTMnet; Q9JHB5; -.
DR PhosphoSitePlus; Q9JHB5; -.
DR jPOST; Q9JHB5; -.
DR PaxDb; Q9JHB5; -.
DR PRIDE; Q9JHB5; -.
DR Ensembl; ENSRNOT00000071827; ENSRNOP00000063911; ENSRNOG00000049784.
DR GeneID; 64028; -.
DR KEGG; rno:64028; -.
DR CTD; 7257; -.
DR RGD; 621574; Tsnax.
DR eggNOG; KOG3066; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_067225_1_0_1; -.
DR InParanoid; Q9JHB5; -.
DR OMA; DTCMETC; -.
DR OrthoDB; 1213910at2759; -.
DR PhylomeDB; Q9JHB5; -.
DR Reactome; R-RNO-426486; Small interfering RNA (siRNA) biogenesis.
DR PRO; PR:Q9JHB5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000049784; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q9JHB5; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:1902555; C:endoribonuclease complex; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031687; F:A2A adenosine receptor binding; IPI:RGD.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
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 Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Golgi apparatus; Isopeptide bond; Magnesium; Metal-binding; Nucleus;
KW Reference proteome; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..290
FT /note="Translin-associated protein X"
FT /id="PRO_0000191689"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..208
FT /note="Interaction with C1D"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99598"
SQ SEQUENCE 290 AA; 33005 MW; 22233361904A5882 CRC64;
MNGKEGPGGF RKRKHDNFPH NQRREGKDAS SSSPVMLAFK SFQQELDTRH DKYERLVKLS
RDITVESKRT IFLLHRITSA PDMEEILTES ESKLDGVRQK MLQVAQELSG EDMHQFHRAV
TTGLQEYVEA VSFQHFIRTR SLISMEEINR QLTFTTDDSG KESKAPPADG QDKQLVTWRL
KITPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS
KKLYTLKQSL SKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEESIS
