ID   TDRD7_AILME             Reviewed;        1101 AA.
AC   D2H0H6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Tudor domain-containing protein 7;
GN   Name=TDRD7; ORFNames=PANDA_002927;
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
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   EMBL; GL192407; EFB16852.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2H0H6; -.
DR   SMR; D2H0H6; -.
DR   STRING; 9646.ENSAMEP00000005179; -.
DR   eggNOG; KOG2039; Eukaryota.
DR   HOGENOM; CLU_283554_0_0_1; -.
DR   InParanoid; D2H0H6; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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..1101
FT                   /note="Tudor domain-containing protein 7"
FT                   /id="PRO_0000409514"
FT   DOMAIN          3..76
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          233..302
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          337..406
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          513..573
FT                   /note="Tudor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   DOMAIN          706..763
FT                   /note="Tudor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          126..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..1101
FT                   /note="Interaction with CDK17"
FT                   /evidence="ECO:0000250"
FT   REGION          896..1101
FT                   /note="Interaction with CABLES1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHU6"
FT   MOD_RES         862
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1H1"
SQ   SEQUENCE   1101 AA;  123818 MW;  9E570792D9AED5D4 CRC64;
     MLEADLVSKM LRAVLQSHKN GIALPRLQGE YRSLTGDWIP FKQLGYPTLE AYLRSVPAVV
     RIETSRSGEI TCYAMACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
     ATLRQPGISS DFSINKKPNP TLLRDRGNSL GVKSDAEMPP YTLHTTIGSQ VFKDVPVQRH
     VTMSTNNRFS PKASLPPPFQ MHLSRTCAKE MSDNLNQTVE KPNVTPPASY TYKMDEVQNR
     IKEILNKHNN GIWISKLPHF YKELYKEELN QGILQQFEHW PHICTVEKPC SGGQDLLLYP
     AKRKQLLRSE LDGEKVPPSP LPAPKQLPPL KGCPAAMPGD FKEKVAELLA KYSSGLWASA
     LPKAFEDMYK VKFPEDALKN LASLSDVCTI DYISGNPQKA ILYAKLPLPA DKILKDAGQA
     HGDYDIKSMI EQEYLQIEEN ISKSADTFVE NTTVPPLIIP TEASPSVLVV ELSNTNEVVI
     RYVGKDYSAA QELMEDEMKE YYSKNPKVMP VQTVHIGQLL AVNAEEDAWL RAQIISTEEN
     KIKASTVCYV DYGFSENIEK SKAYKLNPKF CSLSFQATKC KLAGLEVLSD DPDLVKVVES
     LTCGKIFAVE ILEKADIPLV VLYDTSGEDD VNINATCLKA ICDKSLEAHL QIDAMYTNVR
     VTNICSDGTL YCQVPCKGLN KLNDLLHKIE DYFHCKHMTS EYFVSLPFCG KVCLFHCKGK
     WLRVEITNVH SSRALDVQFL DSGTVTSVKV SELREIPPRF LQEIIVIPPQ AIKCCLADLP
     QSIGMWTPDA VLWLRDSVLN CSDCSIKVTK VDETRGIAHI YLFTPKNFPD PHRSINRQIT
     NADLWKHQKD VFLSAISSAA SSPNSKSGGT PIPGNSGENF RKSITDAIKK SVVDHSSSFS
     MQELPPPVHL SKPGEHMDVY VPVACHPGYF VIQPWQEIHK LEVLMEEMIL YYSVSEERHV
     AVEKDQVYAA KVENKWHRVL LKGILTNGLV SVYELDYGKH ELVNIRKVQP LADVFRKLPF
     QAVTAQLAGV KCNQWSEEAS MVFRNHVEKK PLVALVQTVI ENANPWDRKV VVYLVDTSLP
     DTDIWIHDFM SEYLVELSKV N