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TDRD7_CHICK
ID   TDRD7_CHICK             Reviewed;        1071 AA.
AC   E1C3S7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Tudor domain-containing protein 7;
GN   Name=TDRD7;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21436445; DOI=10.1126/science.1195970;
RA   Lachke S.A., Alkuraya F.S., Kneeland S.C., Ohn T., Aboukhalil A.,
RA   Howell G.R., Saadi I., Cavallesco R., Yue Y., Tsai A.C., Nair K.S.,
RA   Cosma M.I., Smith R.S., Hodges E., Alfadhli S.M., Al-Hajeri A.,
RA   Shamseldin H.E., Behbehani A., Hannon G.J., Bulyk M.L., Drack A.V.,
RA   Anderson P.J., John S.W., Maas R.L.;
RT   "Mutations in the RNA granule component TDRD7 cause cataract and
RT   glaucoma.";
RL   Science 331:1571-1576(2011).
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 specific genes in the developing lens. Also required
CC       during spermatogenesis. {ECO:0000269|PubMed:21436445}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to
CC       cytoplasmic RNA granules. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the developing lens.
CC       {ECO:0000269|PubMed:21436445}.
CC   -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
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DR   EMBL; AADN02060121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02060133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1C3S7; -.
DR   SMR; E1C3S7; -.
DR   PaxDb; E1C3S7; -.
DR   VEuPathDB; HostDB:geneid_430492; -.
DR   InParanoid; E1C3S7; -.
DR   PhylomeDB; E1C3S7; -.
DR   Proteomes; UP000000539; 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; IMP:UniProtKB.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP: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; 2.
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; 1.
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; Reference proteome; Repeat; RNA-binding;
KW   Spermatogenesis.
FT   CHAIN           1..1071
FT                   /note="Tudor domain-containing protein 7"
FT                   /id="PRO_0000409517"
FT   DOMAIN          3..76
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          221..289
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          330..399
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          500..557
FT                   /note="Tudor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   DOMAIN          689..746
FT                   /note="Tudor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          295..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  121561 MW;  34F25C0F8292717B CRC64;
     MQEPDLVAKA LRSVLHSSKH GIPLSELQDE YRSLTGEWIP FRHLGYATLE AYVASIPEVV
     RIERNQTGEV TCHAVACPET IYVRVWAVAH KRTSPIFLLF CCRQNIEKTL QMIRVLDICA
     IFKDPRWSSE VSFVVSVSVC LRRDQLSHHG FKRSCTFTCP EGLPLIQMVS FPIKSILSEK
     GLIPAYEKNH SNSEFYFSLT DNLNASGVET HTVASGRSVP NISEIQNRIK EILSKYRNGV
     WLSKIAQVYE ETYREELSTT VLRQLEHWPH VCTVEKVRTG DQTYRILYPS KRIPPAVKSN
     TEQDQASQNV TSSKAGPVLK TSREAESASC SSDFKQNVVN ILVKYPCGLW ADALPKLYQD
     AYQRKFPEGI LNNLQLLSDV CVVDYVSNVP QKAILYVKTQ SCTDENLNVT EKVQIPDGAK
     ATAEQQHEES KEQYPESISS VPPLVIPSEG PVSVLVIDVN NPNELIIRYV GKDYSGAQEQ
     MEDKMKAYYS KNSTASQITF PSVGQLVAVH TEEEAWLRAQ IISVEDKRLK LSCFCTYFGC
     ITFRMCKPKE NTHCCMKQCT SHKCKLTGLE VFSDDPLLLK AVELQAYHKI CAVEILERSD
     IPVFVLYDTS GEDDININAT CLKALYDKSF ELNLQVDTLY TNVRVTSILS DGNMYCQLPS
     EGLSKLSEVL QKIEYYLLHQ ETSEFNVSQP YCGKICLFLC KGKWTRVEIT IIHSRRALGV
     RFIDTGRVAY VKVTDLREIP SQFLREVIKI PPQAIKCCLA DLPPDTGMWT PEAVLWLRDN
     VMDYAEFSMQ VSVMEKRCVL KFWKAFIPIS YLLADRSINR RINAVLWKHQ KDVFLSVTSQ
     GLAPPKHLNQ GRLEKSDSLE PAVESRGVES ATDVPPPLPL SEVGGFMDVY VSVACHPGHF
     IVQPWKEIHN LEALMEEMIL YYSMAEERPV NIGTNKLYAA KIENRWYRVI VKGILRKGFL
     SVYVLDYGKH EVISIDKVQP LLDKFRKLPF QAIKAELAGV KSQQWSEEAS IIFRNRVEKK
     PLVAQIQAIN ESTNSWDRKV VTYLVDTSIP DTDVWIHDFV CQSLAELSEA D
 
 
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