ID I3MW34_ICTTR Unreviewed; 168 AA.
AC I3MW34;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Translin-associated protein X {ECO:0000256|ARBA:ARBA00041076};
DE AltName: Full=Translin-associated factor X {ECO:0000256|ARBA:ARBA00042076};
GN Name=TSNAX {ECO:0000313|Ensembl:ENSSTOP00000016329.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000016329.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000016329.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037653}.
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.
CC {ECO:0000256|ARBA:ARBA00038594}.
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DR EMBL; AGTP01017323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01017324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01017325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005320428.1; XM_005320371.2.
DR AlphaFoldDB; I3MW34; -.
DR STRING; 43179.ENSSTOP00000016329; -.
DR Ensembl; ENSSTOT00000019756.2; ENSSTOP00000016329.2; ENSSTOG00000024989.2.
DR GeneID; 101967727; -.
DR CTD; 7257; -.
DR eggNOG; KOG3066; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_125030_0_0_1; -.
DR InParanoid; I3MW34; -.
DR OrthoDB; 10121at2759; -.
DR TreeFam; TF323633; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:1902555; C:endoribonuclease complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030422; P:siRNA processing; IEA:Ensembl.
DR InterPro; IPR002848; Translin_fam.
DR InterPro; IPR016068; Translin_N.
DR InterPro; IPR036081; Translin_sf.
DR PANTHER; PTHR10741; TRANSLIN AND TRANSLIN ASSOCIATED PROTEIN X; 1.
DR PANTHER; PTHR10741:SF5; TRANSLIN-ASSOCIATED PROTEIN X; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; Translin; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|PIRSR:PIRSR602848-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000256|PIRSR:PIRSR602848-1"
SQ SEQUENCE 168 AA; 19319 MW; 20C7C98BBD5BCED2 CRC64;
MSGKEGPGGF RKRKHDNFPH GQRREGKDVS ASSPVMLAFK SFQQELDARH DKYERLVKLS
RDITVESKRT IFLLHRITSA PDMEEILTES EVKLDGVRQK ILQVAQELSG EDMHQFHRAI
TTGLQEYVEA VSFQHFIKTR SLISMDEINK ELVFTTEDSG KENKTVRT
//