ID L5M7E5_MYODS Unreviewed; 1098 AA.
AC L5M7E5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Tudor domain-containing protein 7 {ECO:0000256|ARBA:ARBA00013425};
GN ORFNames=MDA_GLEAN10021556 {ECO:0000313|EMBL:ELK34210.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34210.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(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. 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; KB103229; ELK34210.1; -; Genomic_DNA.
DR RefSeq; XP_006758515.1; XM_006758452.2.
DR AlphaFoldDB; L5M7E5; -.
DR GeneID; 102773503; -.
DR KEGG; myd:102773503; -.
DR CTD; 23424; -.
DR eggNOG; KOG2039; Eukaryota.
DR OrthoDB; 5403690at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
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 233..302
FT /note="HTH OST-type"
FT /evidence="ECO:0000259|PROSITE:PS51644"
FT DOMAIN 337..406
FT /note="HTH OST-type"
FT /evidence="ECO:0000259|PROSITE:PS51644"
FT DOMAIN 513..570
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 703..760
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 123679 MW; 7D3301548B4A9464 CRC64;
MLEADLVSKM LRAVLQSHKN GIVLPRLQGE YKSLTGDWIP FKQLGYPSLE AYLRSVPAVV
RIETSRSGET TCYAVACTET ARIAQLVARQ RSSKRKTGRQ VNCQMRVKKT MPFFLEGKPK
ATLRQPGFSS DFSISRKPNA ALSRDRGNAL GVKPEAELPP YTAHTHVGSD VFKSVPMQRH
VTMPTNNRFG PKASLPPPLQ IHLSRTCTKE MSDNLNQTVE KSNVTPPASY TYKMDEVQNR
IKEMLDKHSN GIWMSKLPHF YKELYKEELN QGIVQQCEHW PHICTVERPY SGGQDLLLYP
AKRKQLLRSE PAPEKVPPSP LPAPTQVSPL RGCPTVMPGD FKEKVSELLV KYSNGLWASA
LPKAFEDTYK VKFPEDALKN LALLSDVCTI DYISGNRKKA ILYAKLPLPA NKTLMDAGHA
HGDYAFRSMI EEEYMQIEEN AVESADTILE NVMVPPLVIP TEASPSVLVV ELSNTNEVVI
RYVGKDYSAA QELMEDEMKD YYSRTPRITP VQTVHVGQLL AVHAEEDAWL RAQITSTEGN
RIKVCYVDYG FSENVEKSKA YKLNPRFCSL SFQATKCKLA GLEALSDDPG LVKVVESLTC
GKIFAVEILE KADIPLVILY DTSGEDDINI NATCLKAICD KSLEAHLQVD AMYTNVRVTN
ICSDGTLYCQ VPCKGLNKLN DLLQKIEDYF HCKHMTSEYF VSLPFCGKIC LFHCKGKWLR
VEIMNVHSSR TLDVQFLDSG TVTSVKVSEL REIPSRFLRE MVSIPSQAIR CCLADVPQSV
GMWTPDAVLW LRDSVLNCSD CSIKVTKVDE TRGVNHVYLF TPKNFPDPHR SINRQITNAD
LWKHQKDVFL SALASDAGSP NSRGGHTIAA SSSGENIRKS LVEVSRKPVV DHISSFSTEQ
LPPPVHLAKS GEHMDVYVPV ACHPGYFVIQ RWQEIHKLEV LMEEMILYYS VSEERRVAVE
KDQVYAAKVE NKWHRVLLKG ILTNGLVSVY ELDYGKHELV NIRKVQPLVD MFRKLPFQAV
TAQLAGVKCN QWSEEASMVF RNHVEKRPLV ALVQTVIEGA YPWDQKAVVY LVDTSLPDTD
IWIHDYMSEY LVELSKIN
//
