ID TDRD5_RAT Reviewed; 995 AA. AC B4F7C4; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 75. DE RecName: Full=Tudor domain-containing protein 5; GN Name=Tdrd5; 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 [LARGE SCALE MRNA]. RC TISSUE=Brain; 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). CC -!- FUNCTION: Required during spermiogenesis to participate in the CC repression transposable elements and prevent their mobilization, which CC is essential for the germline integrity. Probably acts via the piRNA CC metabolic process, which mediates the repression of transposable CC elements during meiosis by forming complexes composed of piRNAs and CC Piwi proteins and govern the methylation and subsequent repression of CC transposons. Required for chromatoid body (CB) assembly (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to CC chromatoid body (CB) and pi-body (also called intermitochondrial CC cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA CC processing for spermatogenesis. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TDRD5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC168218; AAI68218.1; -; mRNA. DR RefSeq; NP_001128212.1; NM_001134740.1. DR AlphaFoldDB; B4F7C4; -. DR SMR; B4F7C4; -. DR STRING; 10116.ENSRNOP00000005353; -. DR PhosphoSitePlus; B4F7C4; -. DR PaxDb; 10116-ENSRNOP00000005353; -. DR PeptideAtlas; B4F7C4; -. DR GeneID; 289129; -. DR KEGG; rno:289129; -. DR UCSC; RGD:1307078; rat. DR AGR; RGD:1307078; -. DR CTD; 163589; -. DR RGD; 1307078; Tdrd5. DR eggNOG; KOG2039; Eukaryota. DR HOGENOM; CLU_013593_0_0_1; -. DR InParanoid; B4F7C4; -. DR OrthoDB; 3061370at2759; -. DR PhylomeDB; B4F7C4; -. DR TreeFam; TF342664; -. DR PRO; PR:B4F7C4; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB. DR GO; GO:0043186; C:P granule; IBA:GO_Central. DR GO; GO:0071546; C:pi-body; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0030719; P:P granule organization; ISS:UniProtKB. DR GO; GO:0034587; P:piRNA processing; IBA:GO_Central. DR GO; GO:0141007; P:siRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB. DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central. DR CDD; cd09985; LOTUS_1_TDRD5; 1. DR CDD; cd09975; LOTUS_2_TDRD5; 1. DR CDD; cd09976; LOTUS_3_TDRD5; 1. DR CDD; cd20419; Tudor_TDRD5; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 2.40.50.90; -; 1. DR Gene3D; 3.30.420.610; LOTUS domain-like; 3. DR InterPro; IPR041966; LOTUS-like. DR InterPro; IPR025605; OST-HTH/LOTUS_dom. DR InterPro; IPR035437; SNase_OB-fold_sf. DR InterPro; IPR037982; TDRD5_LOTUS_2. DR InterPro; IPR002999; Tudor. DR PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1. DR PANTHER; PTHR22948:SF19; TUDOR DOMAIN-CONTAINING PROTEIN 5; 1. DR Pfam; PF12872; OST-HTH; 3. DR Pfam; PF00567; TUDOR; 1. DR SMART; SM00333; TUDOR; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS51644; HTH_OST; 3. DR PROSITE; PS50304; TUDOR; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Developmental protein; Differentiation; Phosphoprotein; KW Reference proteome; Repeat; Spermatogenesis. FT CHAIN 1..995 FT /note="Tudor domain-containing protein 5" FT /id="PRO_0000408348" FT DOMAIN 7..80 FT /note="HTH OST-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975" FT DOMAIN 122..197 FT /note="HTH OST-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975" FT DOMAIN 291..365 FT /note="HTH OST-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975" FT DOMAIN 533..592 FT /note="Tudor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT REGION 747..781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 857..892 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 911..960 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..777 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 946 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5VCS6" SQ SEQUENCE 995 AA; 111327 MW; D802E761DDD5E1F4 CRC64; MSEQERIQDC LRKEIRSLLI STKDGLTPQQ LEKEYLLMVG NHLPLRILGY RSTMELVLDM PDVVSVCPCG DGTVILKAIP DESTKGIASL VAKQRRSHKV RNSMQKGRSS VCSGRVPYRG RVPPILPAVV KSELKDLLAL SPVLLSDFEK AFARRFGRSF QYMQYGFLSM FEVLSAASDV ICVEQTRAGS LLTLKKSASE EKQREWPAGK IFTQPFRMKQ QGSYSTGFPV TKTRFSQPIS NMEPPKQVLS MEKIPMFNTV EASRLSHTEK LNQLESTFKS VIAQIGPGGT VDPDLKHKIK FVVSKFPQGL FISKLLGEFE LVFKEQLSPK QLGFLNVTEL VGALSDILRV EFSEEKQDLL VFDADLRPLL PAGPLSSVRN SCLVQPDKRI EANAWASSPS RNSLSTVAVK KTTWDCPLKN HKEAEQKAYK KPNLVVKPLQ LQVETNKSQL SLSMANHDIP PDAVRAKKLC RLPPLDTSTL VGVFVEYIIS PSQFYVRIYS RDSSELLEDM MIEMRRCYSN QLVSDRYVMP EYFIQPGHLC CVRISEDKWW YRVIIHRILG KKEVEVFYPD FGNIGTVQKS SLRFLKCCYT KLPAQAIPCS LAWVRPAEEH WTSKAILHFQ KLCGLKPLVG VVDEYIDGIL NIFLCDTSSN EDVYFHHVLR TEGHAIVCRE NAPSKGFRDF NPPALYTNSS AAPGDMVLTE LGHPAQQHYL NEDGEILQQP QQDINDEKSI SHLKSVSEEL LKDSKLGPLK TRESCEEEPQ WSILKPKDPK EENEDEVPTG MPCLESVTIG DDIWDENWLP LQAKMGKAGG PASHLFTSSL VGKKQYQTRG ETTRKDWCFS TSKDIWDDSW QPLGLANDVK GRTHTPEGPI AQEKNIGTTR IRKQPDLQYP LDSSTLPKLE EFYISLIKSQ QSAEGSQSEP ASIQTPLKPG QASSTAPSST PAAGDSPENH SGSAPDFSEA LHSSKYSHGC LGSSCAVSHV QEPPALVPQC ERREA //