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TDRD5_RAT
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   03-AUG-2022, entry version 69.
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}.
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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   PaxDb; B4F7C4; -.
DR   PeptideAtlas; B4F7C4; -.
DR   PRIDE; B4F7C4; -.
DR   GeneID; 289129; -.
DR   KEGG; rno:289129; -.
DR   UCSC; RGD:1307078; rat.
DR   CTD; 163589; -.
DR   RGD; 1307078; Tdrd5.
DR   eggNOG; KOG2039; Eukaryota.
DR   HOGENOM; CLU_013593_0_0_1; -.
DR   InParanoid; B4F7C4; -.
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:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR   GO; GO:0030719; P:P granule organization; ISS:UniProtKB.
DR   GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR   CDD; cd09975; LOTUS_2_TDRD5; 1.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.420.610; -; 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   Pfam; PF12872; OST-HTH; 3.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00333; TUDOR; 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
 
 
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