ID   TSNAX_PONAB             Reviewed;         290 AA.
AC   Q5RC21;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Translin-associated protein X;
DE   AltName: Full=Translin-associated factor X;
GN   Name=TSNAX; Synonyms=TRAX;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm
CC       in the presence of TSN. Accumulate in the Golgi complex of mid-late
CC       pachytene spermatocytes (By similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR   EMBL; CR858461; CAH90689.1; -; mRNA.
DR   RefSeq; NP_001125379.1; NM_001131907.2.
DR   AlphaFoldDB; Q5RC21; -.
DR   SMR; Q5RC21; -.
DR   STRING; 9601.ENSPPYP00000000113; -.
DR   Ensembl; ENSPPYT00000000122; ENSPPYP00000000113; ENSPPYG00000000112.
DR   GeneID; 100172282; -.
DR   KEGG; pon:100172282; -.
DR   CTD; 7257; -.
DR   eggNOG; KOG3066; Eukaryota.
DR   GeneTree; ENSGT00940000153568; -.
DR   HOGENOM; CLU_067225_1_0_1; -.
DR   InParanoid; Q5RC21; -.
DR   OrthoDB; 1213910at2759; -.
DR   TreeFam; TF323633; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:1902555; C:endoribonuclease complex; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; 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   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030422; P:siRNA processing; IEA:Ensembl.
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   2: Evidence at transcript 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_0000191688"
FT   REGION          1..32
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;  33112 MW;  D38B0DD96B50C0B9 CRC64;
     MSNKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH DKYERLVKLS
     RDITVESKRT IFLLHRITSA PDMEDILTES EIKLDGVRQK IFQVAQELSG EDMHQFHRAI
     TTGLQEYVEA VSFQHFIKTR SLISMDEINK QLIFTTEDNG KENKTPSSDA QDKQFGTWRL
     RVTPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS
     KKLYTLKQSL AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS