TDRD5_CANLF
ID TDRD5_CANLF Reviewed; 985 AA.
AC E2QTD3;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Tudor domain-containing protein 5;
GN Name=TDRD5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
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 AlphaFoldDB; E2QTD3; -.
DR SMR; E2QTD3; -.
DR STRING; 9615.ENSCAFP00000020370; -.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; E2QTD3; -.
DR Proteomes; UP000002254; 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 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Differentiation; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..985
FT /note="Tudor domain-containing protein 5"
FT /id="PRO_0000408347"
FT DOMAIN 7..80
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 127..202
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 300..374
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 530..589
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 98..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VCS6"
SQ SEQUENCE 985 AA; 110613 MW; EF623DA36DA53536 CRC64;
MSEQERVQEC LRKEIRSLLI STKDGLTPQQ LEKEYLLMVG NHLPLRILGY RSTMELVLDM
PDVVTVSPCG DGTIILRAIP DESTKGIANL VAKQRSSHKV RNSMQKGRPS VCSGSSSRRR
VPYRGRVPPI LPAVVKSELK DLLALSPVLL SDFEKAFARR FGRSFQYVQY GFLSMFEVLN
AASDVISVEQ TRAGSLLMLK RSISEEKQRG WPAVTKGGKM FTQPFRMKQQ GSYSTGSPVA
KACFSQPTSN MEPPKQILNA EKTFKSNVVE TSRLNHTEKL NQLENTFKSV ISQIGPGGTI
NPELKHKLRF VVSKFPEGLL ISKLLREFEI MFKEQLSPKQ LGFLNVTELV GALSDILRVE
FREGEQDLLV FDANMKPLAS VQSDKKIDVK ACVSSPPRNS LSTAAVKETA WDCLPKNHRE
PEQKICKKPN LVVKPLQLQV GVNKSELNLA MANHDIPPDA VRDKKLCRLP PLDTSTLVGV
FVEYIISPSQ FYIRIYSRDS SELLEDMMIE MRRCYSNQLV SDRYAMPEYF IQPGHLCCVR
ISEDKWWYRV IIHRVLGKQE VEVFYPDFGN IGTVQKSSLR FLKWCYTKLP AQAIPCSLAW
VRPVEEHWTS RAIIQFQKLC GLKPLVGVVD EYVDGILNIF LCDTSSNEDV YFHHVLRTEG
HAIVCRENVP SKGFRELNPL ALYTKSSAGP EDVVLTELGC PSQQHYFNED REISPQSKEN
ELPTLDEIPI GMPCLESVTI GDDVWDENWL PLQAKMGKGG DAPSHLFTSS RGGKKPYLSC
KEMPQKDWCF SAPKDMWDDS WQPSSLVNGM KVEVQKQEEL SAQEKNIGTT RSQKQPNLES
SSDSPTLPKL EEFYISLVES QQSAEGSQFE PSSIQTQVKQ MQLSTAALST TPAAVDSPEK
HSGSVESSPE SLKNDFSSSH AITVFKDKSH GAMDQLSLIL SPEHQISQKL YIPRSTATAA
LGAAARLATS RRLLHWYPSV KRMEA
