TRD7A_DANRE
ID TRD7A_DANRE Reviewed; 1079 AA.
AC A6NAF9; Q7ZTW1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Tudor domain-containing protein 7A;
GN Name=tdrd7a; Synonyms=tdrd7; ORFNames=zgc:56669;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=18507824; DOI=10.1186/1471-213x-8-58;
RA Strasser M.J., Mackenzie N.C., Dumstrei K., Nakkrasae L.I., Stebler J.,
RA Raz E.;
RT "Control over the morphology and segregation of Zebrafish germ cell
RT granules during embryonic development.";
RL BMC Dev. Biol. 8:58-58(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RX PubMed=17084698; DOI=10.1016/j.cub.2006.08.086;
RA Mishima Y., Giraldez A.J., Takeda Y., Fujiwara T., Sakamoto H.,
RA Schier A.F., Inoue K.;
RT "Differential regulation of germline mRNAs in soma and germ cells by
RT zebrafish miR-430.";
RL Curr. Biol. 16:2135-2142(2006).
RN [4]
RP INDUCTION.
RX PubMed=19013519; DOI=10.1016/j.mod.2008.10.006;
RA Slanchev K., Stebler J., Goudarzi M., Cojocaru V., Weidinger G., Raz E.;
RT "Control of Dead end localization and activity--implications for the
RT function of the protein in antagonizing miRNA function.";
RL Mech. Dev. 126:270-277(2009).
RN [5]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=19838299; DOI=10.1371/journal.pone.0007513;
RA Takeda Y., Mishima Y., Fujiwara T., Sakamoto H., Inoue K.;
RT "DAZL relieves miRNA-mediated repression of germline mRNAs by controlling
RT poly(A) tail length in zebrafish.";
RL PLoS ONE 4:E7513-E7513(2009).
RN [6]
RP INDUCTION.
RX PubMed=20371629; DOI=10.1096/fj.09-148403;
RA Liu W., Collodi P.;
RT "Zebrafish dead end possesses ATPase activity that is required for
RT primordial germ cell development.";
RL FASEB J. 24:2641-2650(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. Probably
CC required during spermatogenesis (By similarity). Required for
CC structural integrity of granules in primordial germ cells (PGCs).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to cytoplasmic RNA
CC granules (By similarity). Component of the meiotic nuage, also named P
CC granule, a germ-cell-specific organelle required to repress transposon
CC activity during meiosis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6NAF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NAF9-2; Sequence=VSP_041321, VSP_041322;
CC -!- DEVELOPMENTAL STAGE: In embryos, expression is restricted to primordial
CC germ cells (PGCs). {ECO:0000269|PubMed:19838299}.
CC -!- INDUCTION: Down-regulated by miR-430 in somatic cells. Down-regulation
CC is relieved by dnd that acts by protecting the 3'-UTR of tdrd7 from
CC miR-430-mediated RNA deadenylation. {ECO:0000269|PubMed:17084698,
CC ECO:0000269|PubMed:19013519, ECO:0000269|PubMed:19838299,
CC ECO:0000269|PubMed:20371629}.
CC -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
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DR EMBL; EF643554; ABR24798.1; -; mRNA.
DR EMBL; BC052137; AAH52137.1; -; mRNA.
DR RefSeq; NP_998270.1; NM_213105.1.
DR AlphaFoldDB; A6NAF9; -.
DR SMR; A6NAF9; -.
DR STRING; 7955.ENSDARP00000040306; -.
DR PaxDb; A6NAF9; -.
DR PeptideAtlas; A6NAF9; -.
DR GeneID; 406379; -.
DR CTD; 406379; -.
DR ZFIN; ZDB-GENE-040426-2103; tdrd7a.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; A6NAF9; -.
DR PRO; PR:A6NAF9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0043186; C:P granule; IDA:ZFIN.
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; IMP:ZFIN.
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; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Differentiation; Reference proteome;
KW Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1..1079
FT /note="Tudor domain-containing protein 7A"
FT /id="PRO_0000409518"
FT DOMAIN 3..76
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 205..270
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 366..434
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 519..576
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 708..765
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041321"
FT VAR_SEQ 408..913
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041322"
FT CONFLICT 195
FT /note="A -> P (in Ref. 2; AAH52137)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010..1012
FT /note="KEV -> QEA (in Ref. 2; AAH52137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1079 AA; 121331 MW; F0F93BF68D4A7495 CRC64;
MSDVELVKKM LRAVLQSSKH GVAMARLQGD YRALTGEMIP FRKFGHDTLE SFLRSIPGVV
RLERSITGEV MCFAGVCEET AHIAQLVARQ KNVKKTGCSK LLNFQMRART SHLFSHNVKP
RLSLRQPSNM THPGRGSVTS FYSTQRKLYS NDLPSSRAPA WQMNRKSPVP EKTSVVPSKI
NTNIKTPLKK TSGTAAQQKP VNRADVELVQ GRIKQLLQKY SSGVWLSKIP QLYKSMFQEE
LHIIQEVEKW THICTVEKPG SNNIVDRLVY PVLEPVPKAS PVPVKSPCKQ SPNTALLKQP
TLTQKTTRTF RTLAINIPQS TPKPQTPLSP TSPNSTMIDF TLSETPKTQS LSPITPPSTP
PAHQPLTTEL KQKLRQLLNK YSQGLWAHGL PQLFQEAFGC AFPQYVLEDL SLLADTCMVE
YPMPDNRKRA ILYTLPCQVQ TQPRSRPPPL VLPCTSNPHV PPLIIPTADF HSVFVIEINS
TNNVVVRFAG GGYSKSLEVM EEEMQNFYNN IGAGLCLLSP KIGQLVAVAS SDGAMLRAQV
HQLSEDKVKV YFLDHGFFDL VSRKTLFQLR DQFMTLPFQA TTCQLAGLEP FSTDPVVLKT
LQSLAVGRSL LAEIVEREDT PLVVLYDTSE NDDVNVTAMC LKALQDKSME NPLQVNSVYT
NVCVTNVCSD GSVYCQLPSR GQAKLKDIMD KIEAHFISQL TWELLVSRPF CGKVCLAKYK
GKWARAEIIN LHGSHVLDIL FLDLGLPASL EVSELREIPP IFLKELITIP PQAIKCLLED
LNVDRAVWPP EAVLWLRETV HNKAPSCMKI VKLDETRTVH IYLFCGNEAQ DIHDSVNRQL
ASCPFWKQDV YANKINKASE LFLPDAGEPS GSSPAPSNAL TLPPQLNLPL VGQNMDVFVS
VACHPGHFVL QPWQDLYKLV VLMGEMVLFY NKQEVTTVDI QKNNVYAAKI DNNWHRVLVK
GLLTNGLVSV YELDYGKYEL INYTQLQPLI EEFRQLPFQG ISAQLADVKK EVWCEEASMV
FRNHVEKKPL VAQIESVEEG EWPWERKISV YLVDTTQENK DIWIHNIMKE FLDEISRDA
