ID A0A2U3W9E8_ODORO Unreviewed; 290 AA.
AC A0A2U3W9E8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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|RefSeq:XP_004404928.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004404928.1};
RN [1] {ECO:0000313|RefSeq:XP_004404928.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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_004404928.1; XM_004404871.1.
DR AlphaFoldDB; A0A2U3W9E8; -.
DR STRING; 9708.A0A2U3W9E8; -.
DR GeneID; 101378069; -.
DR KEGG; oro:101378069; -.
DR CTD; 7257; -.
DR InParanoid; A0A2U3W9E8; -.
DR OrthoDB; 10121at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd14805; Translin-like; 1.
DR InterPro; IPR016069; Translin_C.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000245340}.
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"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-2"
SQ SEQUENCE 290 AA; 33070 MW; E96E03C6D2172581 CRC64;
MSSKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH DKYERLVKLS
RDITVESKRT IFLLHRITSA PDTEEILTDS EIKLDGVRQK ILQVAQELSG EDMHQFHRAI
TTGLQEYVEA VSFQHFIKTR SLISMDEINK QLIFTTEEYG KENKTPSSDA QDKQFGTWRL
KITPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS
KKLYTLKQSL AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS
//
