TRD7B_DANRE
ID TRD7B_DANRE Reviewed; 1085 AA.
AC E7FDW8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Tudor domain-containing protein 7B;
GN Name=tdrd7b;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to cytoplasmic RNA
CC granules. {ECO:0000250}.
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DR EMBL; BX664612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR382383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005166552.1; XM_005166495.3.
DR AlphaFoldDB; E7FDW8; -.
DR SMR; E7FDW8; -.
DR STRING; 7955.ENSDARP00000101927; -.
DR PaxDb; E7FDW8; -.
DR PRIDE; E7FDW8; -.
DR Ensembl; ENSDART00000108540; ENSDARP00000101927; ENSDARG00000077523.
DR GeneID; 100004703; -.
DR CTD; 100004703; -.
DR ZFIN; ZDB-GENE-150109-14; tdrd7b.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00890000139482; -.
DR HOGENOM; CLU_283554_0_0_1; -.
DR InParanoid; E7FDW8; -.
DR OMA; VMAGDFK; -.
DR OrthoDB; 1276848at2759; -.
DR PRO; PR:E7FDW8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000077523; Expressed in caudal fin and 21 other tissues.
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; Reference proteome; Repeat; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..1085
FT /note="Tudor domain-containing protein 7B"
FT /id="PRO_0000409519"
FT DOMAIN 3..76
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 229..299
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 340..410
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 496..554
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 686..743
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 112..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 121834 MW; F1860576E62CA9EE CRC64;
MADEELVKKM VRAVLQSSKS GLSLSDLQVE YKDLTGELIP YKQLGYVTLD ALLHSMPSIV
KLDKGQSGEV MCHATTGNEM AHITKLAARQ RTAKKTGRPQ VVNCQMRVKP AAPLVLNAKP
RTSLRQPDHR GRLGRGGGRG HGDTRTGCMR DPQLDGKGGR PHNTPPNTPS RKPSLPSERP
EKRMTLPSRF QKEVHAHILR NPQHINVPSN LNENTTPPKP RLPHSAPYSP KLVQSRLQEV
LNKHSNGLWV SKLPQLYREH YKQDLPSEAL KELENWTHIC TVEKPCSSKP QELLLYPAKE
TSQITPTPTH DRSPSHHKKP QTQRPSLTAK SNTPESPKAL SPDLKQKLGE LLLKYSSGLW
AHALPKLYQD TYKCKLPEFV LDQLTLLSDI CTIDYPVPDN PKRAILYAKV VEDENRNQSG
LAGQEMKLER RLSSQTVPPL VIPRVEYPSV LVVDASDTNC VILRYIGEGY SKAQEKLEDE
MREFYRQDNT KMALRSPSPG QLTAVGAEEE DDIIRAQVCE VMADKVKVYY VDHGFSEVIS
IRKLFELNEK FYRLPFQATK CKLAGLESFS QEQAVLKKLE SIATGKILLA EILEREDMPL
VVLYDTSQDD DVNINAACMK ALQDRSLESP LKVNSAYMNV SVTSVCSDGT IYCQVPSRGL
TKLNEILEKT ENYFHSQVTS ESLVSRPFCG KNCLARYKGK WSRVEITNLH GSRVLDILFV
DVGVQASVEV IELREIPPPL LRDLISTPAQ ALKCCLAGLP VSVGLWTPDA VQWLRDTVLH
ISDCSLKIAK VDETKRLAHV YLFTSKNFHD TSCSLNQQLA DSDLWNHQKD VFLSSRGPLK
SLNVPTATQT SSLKTDRGDK ALHTPKKTSP PLGSKSTPAG SPPERLSLPP ALELPEIGQN
MDVFVSVACH PGHFVLQPWQ DMYKLVVLMG EMILHYNKME EKALKVEKNQ VCAAKVENNW
YRVLVKGVLT NGLVSVFQLD YGKHELVSGT KLRPLTQEFC QLPFQAITAQ LAGLKPRQWS
EEASIVFRNH VEKKPLVAQL ESVQEASQPW ERKVMIYLVD TSQEERDIWL HDIMAEFTDE
MTKTA
