ID F7HUL2_CALJA Unreviewed; 1096 AA.
AC F7HUL2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Tudor domain-containing protein 7 {ECO:0000256|ARBA:ARBA00013425};
GN Name=TDRD7 {ECO:0000313|EMBL:JAB13795.1,
GN ECO:0000313|Ensembl:ENSCJAP00000047380.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000047380.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000047380.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB13795.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB46091.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB32137.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB13795.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB39686.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000047380.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025023}.
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.
CC {ECO:0000256|ARBA:ARBA00025868}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TDRD7 family.
CC {ECO:0000256|ARBA:ARBA00007740}.
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DR EMBL; GAMS01009341; JAB13795.1; -; mRNA.
DR EMBL; GAMR01001795; JAB32137.1; -; mRNA.
DR EMBL; GAMQ01002165; JAB39686.1; -; mRNA.
DR EMBL; GAMP01006664; JAB46091.1; -; mRNA.
DR RefSeq; XP_002743155.1; XM_002743109.1.
DR RefSeq; XP_008998087.1; XM_008999839.1.
DR STRING; 9483.ENSCJAP00000047380; -.
DR Ensembl; ENSCJAT00000057817.4; ENSCJAP00000047380.2; ENSCJAG00000010731.5.
DR GeneID; 100396834; -.
DR KEGG; cjc:100396834; -.
DR CTD; 23424; -.
DR GeneTree; ENSGT00890000139482; -.
DR HOGENOM; CLU_283554_0_0_1; -.
DR OMA; CKGKWSR; -.
DR OrthoDB; 5403690at2759; -.
DR Proteomes; UP000008225; Chromosome 1.
DR Bgee; ENSCJAG00000010731; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035770; C:ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR CDD; cd09986; LOTUS_1_TDRD7; 1.
DR CDD; cd09973; LOTUS_2_TDRD7; 1.
DR CDD; cd09974; LOTUS_3_TDRD7; 1.
DR CDD; cd20427; Tudor_TDRD7_rpt1; 1.
DR CDD; cd20428; Tudor_TDRD7_rpt2; 1.
DR CDD; cd20429; Tudor_TDRD7_rpt3; 1.
DR Gene3D; 2.30.30.140; -; 3.
DR Gene3D; 2.40.50.90; -; 3.
DR Gene3D; 3.30.420.610; LOTUS domain-like; 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 InterPro; IPR047448; Tudor_TDRD7_rpt2.
DR InterPro; IPR047449; Tudor_TDRD7_rpt3.
DR PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22948:SF29; TUDOR DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12872; OST-HTH; 1.
DR Pfam; PF00567; TUDOR; 3.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 3.
DR PROSITE; PS51644; HTH_OST; 3.
DR PROSITE; PS50304; TUDOR; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 3..76
FT /note="HTH OST-type"
FT /evidence="ECO:0000259|PROSITE:PS51644"
FT DOMAIN 231..300
FT /note="HTH OST-type"
FT /evidence="ECO:0000259|PROSITE:PS51644"
FT DOMAIN 335..404
FT /note="HTH OST-type"
FT /evidence="ECO:0000259|PROSITE:PS51644"
FT DOMAIN 511..568
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 701..758
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 126..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 123341 MW; ACE5256992D86844 CRC64;
MPEGDLVSKM LRAVLQSHKN GVALPRLQGE YRSLTGDWIP FKQLGFPTLE AYLRSVPAVV
RIETSRSGEI TCYAVACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
ATLRQPGFAS NFSIGKKPNP PLLRDKGNSA GVKSDAETSL YTLQTTLGNE AFKDIPMQRH
VTMSTNNRFS PKAFIQPPLQ IHLSRTSAKE MSDNLNQTVE KPNVTPPASY KMDEVQNRVK
EILNKHNNGI WISKLPHFYK ELYKEDLNQG ILQQFEHWPH ICTVEKPCSG GQDLLLYPAK
RKQILRSELD TEKVPPSPLP APKQTPPLKG GLPVMPGDFK EKVAELLVKY TSGLWASALP
KAFEEMYKVK FPEDALKNLA SLSDVCTIDY ISGNPQKAIL YAKLPLPTEK IQKDAGQAHG
DHDIKTMVEQ EYLQIKETIA ESANTFMEDI TVPPLMIPTE ASPSVLVVEL SNTNEVVIRY
VGKDYSAAQE LMEDEMKEYY SKNPKVTPVQ AVHVGQLLAI NAEEDAWLRA QVISTEENKI
KVCYVDYGFS ENVEKSKAYK LNPKFCSLSF QATKCKLAGL EVLSDDPDLV KVVESLTCGK
IFAVEILDKA DIPLVVLYDT SGEDDININA SCLKAICDKS LEVHLQVDAM YTNVKVTNIC
SDGTLYCQVP CKGLNKLNDL LHKIEDYFHC KHMTSECFVS LPFCGKICLF RCKGKWLRVE
ITNVHSSRAL DVQFLDSGTV TSVKVSELRE IPPRFLQEMI AIPPQAIKCC LADLPQSIGM
WTPDAVLWLR DSVLNCWDCS IKVTKVDETR GIAHVYLFTP ENFPDPHRSI NLQITNADLW
KHQKDVFLSA ISSGAGSPDS KNGNMPVSGN TGENIRKNLT DVIKKSMVDH TGSFSTEELP
PPVLLSKPGE HMDVYIPVAC HPGYFVIQPW QEIHKLEVLM EEMILYYSVS EERHIAVEKD
QVYAAKVENK WHRVLLKGIL TNGLVSVYEL DYGKHELVNI RKVQPLVDMF RKLPFQAVTA
QLAGVKCNQW CEEASMVFRN HVEKKPLVAL VQTVIENANP WDRKVVIYLV DTSLPDTDIW
IHDFMSEYLI ELSKVN
//
