TDRD7_PONAB
ID TDRD7_PONAB Reviewed; 1098 AA.
AC Q5RAH6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Tudor domain-containing protein 7;
GN Name=TDRD7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859039; CAH91234.1; -; mRNA.
DR RefSeq; NP_001127391.1; NM_001133919.2.
DR AlphaFoldDB; Q5RAH6; -.
DR SMR; Q5RAH6; -.
DR STRING; 9601.ENSPPYP00000021765; -.
DR GeneID; 100174458; -.
DR KEGG; pon:100174458; -.
DR CTD; 23424; -.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; Q5RAH6; -.
DR OrthoDB; 1276848at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Cytoplasm; Differentiation; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spermatogenesis.
FT CHAIN 1..1098
FT /note="Tudor domain-containing protein 7"
FT /id="PRO_0000292551"
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..570
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 703..760
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 861..1098
FT /note="Interaction with CDK17"
FT /evidence="ECO:0000250"
FT REGION 893..1098
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 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1H1"
SQ SEQUENCE 1098 AA; 123661 MW; 5FDF4F122292F543 CRC64;
MLEGDLASKM LRAVLQSHKN GVALPRLQGE YRSLTGDWIP FKQLGFPTLE AYLRSVPAVV
RIETSRSGEI TCYAMACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
ATLRQPGFAS NFSVGKKPNL APLRDKGNSA VVKPDAEISP CMLHTTLGNE AFKDIPVQRH
VTMSTNNRFS PKASLQPPLQ MHLSRTSTKE MSDNLNQTVE KPNVTPPASY TYKMDEVQNR
IKEILNKHNN GIWISKLPHF YKELYKEDLN QGILQQFEHW PHICTVEKPC SGGQDLLLYP
AKRKQLLRSE LDTEKVPLSP LPGPKQTPPL KGCPTVMAGD FKEKVADLLV KYTSGLWASA
LPKAFEEMYK VKFPEDALKN LASLSDVCSI DYISGNPQKA ILYAKLPLPT DKIQKDAEQA
HGDHDIKAMV EQEYLQLEEN IAESANTFME YITVPPLMIP TEASPSVLVV ELSNTNEVVI
RYVGKDYSAA QELMEDEMKE YYSKNPKVTP VQAVNVGQLL AVNAEEDAWL RAQVISTEEN
KIKVCYVDYG FSENVEKSKA YKLNPKFCSL SFQATKCKLA GLEVLSDDPD LVKVVESLTC
GKIFAVEILD KADIPLVVLY DTSGEDDINI NATCLKAICD KSLEVHLQVD AMYTNVKVTN
ICSDGTLYCQ VPCKGLNKLS DLLRKIEDYF HCKHMTSECF VSLPFCGKIC LFHCKGKWLR
VEITNVHSSR ALDVQFLDSG TVTSVKVSEL REIPPRFLQE MIAIPPQAIK CCLADLPQSI
GMWTPDAVLW LRDSVLNCSD CSIKVTKVDE TRGIAHVYLF TPKNFPDPHR SINRQITNAD
LWKHQKDVFL SAISSGAGSP NSKNGNMRVS GDTGENFRKN LTDVIKKSMM DHTSSFSTEE
LPPPVHLSKP GEHMDVYVPV ACHPGYFVIQ PWQEIHKLEV LMEEMILYYS VSEERHIAVE
KDQVYAAKVE NKWHRVLLKG ILTNGLVSVY ELDYGKHELV NIRKVQPLAD MFRKLPFQAV
TAQLAGVKCT QWSEEASMVF RNRVEKKPLV ALVQTVIENA NPWDRKVVVY LVDTSLPDTD
IWIHDFMSEY LIELSKVN
