TDRD7_BOVIN
ID TDRD7_BOVIN Reviewed; 1098 AA.
AC A6QLE1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Tudor domain-containing protein 7;
GN Name=TDRD7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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; BC147932; AAI47933.1; -; mRNA.
DR RefSeq; NP_001093779.1; NM_001100309.1.
DR RefSeq; XP_015328029.1; XM_015472543.1.
DR AlphaFoldDB; A6QLE1; -.
DR SMR; A6QLE1; -.
DR STRING; 9913.ENSBTAP00000004845; -.
DR PaxDb; A6QLE1; -.
DR PRIDE; A6QLE1; -.
DR Ensembl; ENSBTAT00000004845; ENSBTAP00000004845; ENSBTAG00000003719.
DR GeneID; 506702; -.
DR KEGG; bta:506702; -.
DR CTD; 23424; -.
DR VEuPathDB; HostDB:ENSBTAG00000003719; -.
DR VGNC; VGNC:35721; TDRD7.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00890000139482; -.
DR HOGENOM; CLU_283554_0_0_1; -.
DR InParanoid; A6QLE1; -.
DR OMA; CKGKWSR; -.
DR OrthoDB; 1276848at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000003719; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; A6QLE1; baseline and differential.
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 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_0000409516"
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; 123899 MW; E1C6DECF2A35F6E9 CRC64;
MLEADLVSKM LRAVLQSHKN GIALPRLQGE YRSLTGDWIP FKQLGYPTLE AYLRSVPAVV
RIETSRSGEV TCYAVACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
ATLRQPGFSS DFSVSKKPNS TLLRNKGISL GVKSDAEVLP YTLQTTIGNE VFKDVPVQSH
MTMSTNNRFS PKASLPPRFQ MHLSRTCTKE MSDNLNQAVE KPNVTPPASY TYKMDEVQNR
IKEILNKHSN GIWISKLPHF YKELYKEELN QGILQQFEHW PHICTVEKPC SGGQDLLLYP
AKRKQLLRSE LNTEKVPPSP LPAPKQIPPL KGCPAVMPGD FKEKVAELLV KYSSGLWASA
LPKTFEDMYK VKLPEDALKN LDLLSDVCTV DYISGNPQKA ILYAKLPSPA DKILKDAEQA
HGNYDIKSTV EQEYLQIEEN IAESTDTFME TVTIPPLIIP TETSPSVLVV ELSNTNEVVI
RYVGKDYSAA QELMEDEMKE YYSKNSKVTP VQTVQIGQLL AVNAEEDAWL RAQVISMEEG
KIKVCYVDYG FSENVEKSKA YRLNPKFCSL SFQATKCKLA GLEVLSDDPD LVKVVESLTC
GKIFAVEILE KTDIPLVVLY DTSGEDDINI NATCLKAICD KSLEVHLQVD AMYTNVRVTN
ICSDGTLYCQ VPCKGLNKLN DLLHKIEEYF HCKHMTSEYF VSLPFCGKVC LFHCKGKWLR
VEITNVHSSR ALDVQFLDAG TVTSVKVSEL REIPPRFLQE MISVPPQAIK CCLADLPQSI
GMWTPDAVLW LRDSVLNCSD CSIKVTKVDE TRGIAHIYLF TPKNFPDPHR SINRQITNAD
LWKHQKDVFL SAISSGASSP NTKSANTPIL GNTGETFRKS LTDVLKKSVV NHPSSFFTKE
LPPPVHLSKP GEHMDVYVPV ACHPGYFVIQ PWQEIHKLEV LMEEMILYYS VSEERHVAVE
KDQVYAAKVE NKWHRVLLKG ILTNGLVSVY ELDYGKHELV NMRKVQPLAD MFRKLPFQAV
TAQLAGVKCN QWSEEASMVF RNHVEKKPLV ALVQTVIENT NPWDRKVVVY LVDTSLPDTD
IWIHDFMSEY LVELSKVN
