ID   TDRD7_CANLF             Reviewed;        1125 AA.
AC   E2RDV1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Tudor domain-containing protein 7;
GN   Name=TDRD7;
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: Component of specific cytoplasmic RNA granules involved in
CC       post-transcriptional regulation of specific genes: probably acts by
CC       binding to specific mRNAs and regulating their translation. Required
CC       for lens transparency during lens development, by regulating
CC       translation of genes such as CRYBB3 and HSPB1 in the developing lens.
CC       Also required during spermatogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC       TDRD7 and DDX4. Found in a complex containing CABLES1, CDK16 and CDK17.
CC       Interacts with CABLES1, CDK17 and PIWIL1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to
CC       cytoplasmic RNA granules (By similarity). Present in chromatoid body
CC       (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or
CC       polar granules in Drosophila germ cells), also named processing bodies
CC       (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic
CC       CBs (also called intermitochondrial cementin) in pachytene
CC       spermatocytes and as a single perinuclear CB in haploid round
CC       spermatids (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
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DR   AlphaFoldDB; E2RDV1; -.
DR   SMR; E2RDV1; -.
DR   STRING; 9612.ENSCAFP00000003516; -.
DR   PaxDb; E2RDV1; -.
DR   eggNOG; KOG2039; Eukaryota.
DR   InParanoid; E2RDV1; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR   GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   CDD; cd09974; LOTUS_3_TDRD7; 1.
DR   CDD; cd04508; TUDOR; 3.
DR   Gene3D; 2.40.50.90; -; 3.
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; IPR037978; TDRD7_LOTUS_3.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF12872; OST-HTH; 2.
DR   Pfam; PF00567; TUDOR; 3.
DR   SMART; SM00333; TUDOR; 3.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Differentiation; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; Spermatogenesis.
FT   CHAIN           1..1125
FT                   /note="Tudor domain-containing protein 7"
FT                   /id="PRO_0000409515"
FT   DOMAIN          3..76
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          260..329
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          364..433
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          540..597
FT                   /note="Tudor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   DOMAIN          730..787
FT                   /note="Tudor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          126..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..1125
FT                   /note="Interaction with CDK17"
FT                   /evidence="ECO:0000250"
FT   REGION          920..1125
FT                   /note="Interaction with CABLES1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHU6"
FT   MOD_RES         886
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1H1"
SQ   SEQUENCE   1125 AA;  126655 MW;  4C9E9982F1CBE2B8 CRC64;
     MLEADLVSKM LRAVLQSHKN GIALPRLQGE YRSLTGDWIP FKQLGYPTLE AYLRSVPAVV
     RIETSRSGEI TCYAMACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
     ATLRQPGFSS DFSVSKKPNP TLLRDKGNSL GVKSDAEMPP YTLHTTLRSE VFKDVPVQRH
     VTMSTNNRVI PMCSHPDVDP LQYVGSVFKK HKYLRFSPKA SLPPPFQMHL SRTCAKEMNG
     NLSQTVEKPN VTPPASYTYK MDEVQNRIKE ILNKHNNGIW ISKLPHFYKE LYKEELNQGI
     LQQFEHWPHI CTVEKPGSGG QDLLLYPAKR KQLLRSELDG EKVPPSPLPA PKQIPPLKGC
     PAVMPGDFKE KVAELLTKYS SGLWASALPK AFEDMYKMKF PEDALKNLAS LSDVCTIDYI
     SGNPQKAILY AKLPLPTDKI LKDAGQAHGD YDIKSMIEQE YLQIEENIAK SVDTFLENTA
     VPPLIIPTEA SPSVLVVELS NTNEVVIRYV GKDYSAAQEL MEDEMKEYYS KNPKVTPVQT
     VHVGQLLAVN AEEDAWLRAQ IISTEENRIK VCYVDYGFSE NIEKSKAYKL NPKFCSLSFQ
     ATKCKLAGLE VLSDDPDLVK VVESLTCGKI FAVEILEKAD IPLVVLYDTS GDDDVNINAT
     CLKAICDKSL EAHLQIDAMY TNVRVTNICS DGTLYCQVPC KGLNKLNDLL HKIEDYFHCK
     HMTSEYFVSL PFCGKVCLFH CKGKWLRVEI TNVHSSRALD VQFLDSGTVT SVKVSELREI
     PPRFLQEIIV IPPQAIKCCL ADLPQSIGMW TPDAVLWLRD SVLNCSDCSI KVTKVDETRG
     IAHIYLFTPK NFPDPHRSIN RQITNADLWK HQKDVFLSAI SSGTSSPNSK SGSTPVPGST
     GDNFRKSLTD AIKKSVVDHT SSLSVEELPP PVHLSKPGEH MDVYVPVACH PGYFVIQPWQ
     EIHKLEVLME EMILYYSVSE ERHVAVEKDQ VYAAKVENKW HRVLLKGILT NGLVSVYELD
     YGKHELVNIR KVQPLAAVFR KLPFQAVTAQ LAGVKCNQWS EEASMVFRNH VEKKPLVALV
     QTVIENANPW DRKVVVYLVD TSLPDTDIWI HDFMSEYLVE LSKVN