TDRD5_DANRE
ID TDRD5_DANRE Reviewed; 905 AA.
AC Q1L981; A4QN69;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Tudor domain-containing protein 5;
GN Name=tdrd5; ORFNames=si:dkey-171o17.7;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1L981-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1L981-2; Sequence=VSP_041055;
CC -!- SIMILARITY: Belongs to the TDRD5 family. {ECO:0000305}.
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DR EMBL; BC134985; AAI34986.1; -; mRNA.
DR EMBL; CR381682; CAK05304.1; -; Genomic_DNA.
DR RefSeq; NP_001038315.1; NM_001044850.1. [Q1L981-1]
DR RefSeq; XP_005161770.1; XM_005161713.3.
DR AlphaFoldDB; Q1L981; -.
DR SMR; Q1L981; -.
DR IntAct; Q1L981; 2.
DR MINT; Q1L981; -.
DR STRING; 7955.ENSDARP00000122775; -.
DR PaxDb; Q1L981; -.
DR Ensembl; ENSDART00000134798; ENSDARP00000122775; ENSDARG00000071450. [Q1L981-1]
DR GeneID; 557999; -.
DR KEGG; dre:557999; -.
DR CTD; 163589; -.
DR ZFIN; ZDB-GENE-050208-502; tdrd5.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00390000001360; -.
DR HOGENOM; CLU_013593_1_0_1; -.
DR InParanoid; Q1L981; -.
DR OMA; YVMPEYF; -.
DR OrthoDB; 1115068at2759; -.
DR PhylomeDB; Q1L981; -.
DR TreeFam; TF342664; -.
DR PRO; PR:Q1L981; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000071450; Expressed in testis and 17 other tissues.
DR ExpressionAtlas; Q1L981; baseline.
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 PROSITE; PS51644; HTH_OST; 3.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..905
FT /note="Tudor domain-containing protein 5"
FT /id="PRO_0000281123"
FT DOMAIN 6..79
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 128..204
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 288..364
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 523..581
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 219..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 844..846
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041055"
FT CONFLICT 653
FT /note="H -> Y (in Ref. 2; AAI34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="I -> M (in Ref. 2; AAI34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="P -> H (in Ref. 2; AAI34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="V -> I (in Ref. 2; AAI34986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 101266 MW; 386C1C40B67F4282 CRC64;
MTQDQLLAGL KKDVRSLLVS SKHGLTPEHL RRDYQSMLGF PMPLRLLGFR NVLDMVKEMP
EVVRLEYQLD GNIILKAIGD DTTKGIEELV SKQRDHKPKP NNRKGKPGYF NISYPRLQPV
ILPRRGQAKP ALPAHLRSQL KQLLSHGPVR LSELESRYVA QFGKPLNVTQ YGFFSISEML
SAAMDFIIMQ QSRTGSQLLL RSAVTPQNQP ENLMRRFSMQ STSPKQRLAG FSPKASSLPE
RRPEVSLDPS SVSKPEPVKE EQSFEETVFK LEEELRQQIL EKGTAGTVSQ ELKEKLRKVV
AENGNGISIH NLPTEYQRMH GEELPVSQCG FLSVTEMVGA LSDTLAIQRG TDESESHWMV
VEFKPIDTQP CEPELSPGDG TTSSPTGELQ NPSSRAFYFS CPESAWEHEE TEPLTDSQES
DAELRVANKT IHQMVNLFPE LMVSRVSAVP LDAVRCQKLK PPVHRKEREL LPVLVEQTES
PSYFYIRFSQ NKEARALENM MIEMRSCYSY PDVAERYRLP DAYVRPGQVC CVAPRDMWFY
RVVIHEVFSE TEVKVYYVDY GDITKVERHS LRFLKACYAD LPAQAVPAML AGVRPITNIW
PASAVSCFQR LCCERTLVAG VHSYQEDFLL LFLCDTNTEE DVYVHLALIQ EGHAQPCSAA
YGLVSEKFNP VTSYFGYDQL EDVKESLSPF SCSPDAEIDS QGNDSPSSCR TASNSESGET
NLASIDVDPN LDLPPLEVIN VPDVNTAAKS ENVNPFEALV RKDPLFNSEW DQGWTAEDKT
DETKFELDVS TEQSKPETVY TPSPVQAAVG KQQLCASPVE PKVNATTCVN PHNPVPIQIN
CSYPVLPGVP VYPVKPPISQ FMMQLLGNPV YQGPGPNTAF QHLTSPLALR PAARMSAGGQ
ILHWS
