TDRD6_XENLA
ID TDRD6_XENLA Reviewed; 1905 AA.
AC Q90WE3;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Tudor domain-containing 6-like {ECO:0000305};
DE Short=tdrd6-like;
DE AltName: Full=Xenopus tudor repeat {ECO:0000303|PubMed:12112575};
GN Name=tdrd6 {ECO:0000312|Xenbase:XB-GENE-6079334};
GN Synonyms=xtr {ECO:0000312|EMBL:BAB62226.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAB62226.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12112575; DOI=10.1002/mrd.90003;
RA Ikema Y., Hiyoshi M., Daiyasu H., Toh H., Mori M., Takamune K.;
RT "Two novel genes expressed in Xenopus germ line: characteristic features of
RT putative protein structures, their gene expression profiles and their
RT possible roles in gametogenesis and embryogenesis.";
RL Mol. Reprod. Dev. 62:421-430(2002).
RN [2]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15771630; DOI=10.1111/j.1440-169x.2005.00787.x;
RA Hiyoshi M., Nakajo N., Abe S., Takamune K.;
RT "Involvement of Xtr (Xenopus tudor repeat) in microtubule assembly around
RT nucleus and karyokinesis during cleavage in Xenopus laevis.";
RL Dev. Growth Differ. 47:109-117(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FRGY2, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21314676; DOI=10.1111/j.1440-169x.2009.01121.x;
RA Golam Mostafa M., Sugimoto T., Hiyoshi M., Kawasaki H., Kubo H.,
RA Matsumoto K., Abe S., Takamune K.;
RT "Xtr, a plural tudor domain-containing protein, coexists with FRGY2 both in
RT cytoplasmic mRNP particle and germ plasm in Xenopus embryo: its possible
RT role in translational regulation of maternal mRNAs.";
RL Dev. Growth Differ. 51:595-605(2009).
CC -!- FUNCTION: Tudor domain-containing protein involved in germ cell
CC development, more specifically the formation of chromatoid body (during
CC spermiogenesis), Balbiani body (during oogenesis), germ plasm (upon
CC fertilization), and for proper miRNA expression and spliceosome
CC maturation (By similarity). Component of cytoplasmic mRNP particle
CC through interaction with FRGY2, and binds to maternal mRNA related to
CC cell cycle (RCC1, RHAMM, INCENP-A, MAD2L1, HELLS) and a germ plasm
CC specific mRNA (Dead end/Dnd1), it is proposed a role in translational
CC activation of the maternal mRNAs repressed in mRNP particle
CC (PubMed:21314676). {ECO:0000250|UniProtKB:F1R237,
CC ECO:0000250|UniProtKB:P61407, ECO:0000269|PubMed:21314676}.
CC -!- SUBUNIT: Interacts with FRGY2 (a component of messenger
CC ribonucleoprotein (mRNP) particle)during germ cell develpoment.
CC {ECO:0000269|PubMed:21314676}.
CC -!- INTERACTION:
CC Q90WE3; A8KBF3: piwil2; Xeno; NbExp=4; IntAct=EBI-7191460, EBI-7191401;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21314676}.
CC Note=Localizes in the germ plasm, most precisely in the cytoplasmic
CC mRNP particle (messenger ribonucleoprotein, which corresponds to mRNA
CC with bound proteins). {ECO:0000269|PubMed:21314676}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12112575}.
CC -!- DEVELOPMENTAL STAGE: Presents exclusively in early embryonic and
CC germline cells (PubMed:15771630, PubMed:21314676). Expressed in both
CC spermatogenic and oogenic cells except for round spermatids and the
CC later stage (PubMed:12112575). Expressed in early stage embryos and
CC decrease after the gastrula stage (PubMed:12112575).
CC {ECO:0000269|PubMed:12112575, ECO:0000269|PubMed:15771630,
CC ECO:0000269|PubMed:21314676}.
CC -!- DOMAIN: The tudor domains recognize and bind to proteins with
CC dimethylated arginine residues. {ECO:0000250|UniProtKB:P61407}.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function in embryos causes arrest of
CC karyokinesis progression. {ECO:0000269|PubMed:15771630}.
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DR EMBL; AB066588; BAB62226.1; -; mRNA.
DR RefSeq; NP_001082149.1; NM_001088680.1.
DR AlphaFoldDB; Q90WE3; -.
DR IntAct; Q90WE3; 1.
DR MINT; Q90WE3; -.
DR GeneID; 398252; -.
DR KEGG; xla:398252; -.
DR CTD; 398252; -.
DR Xenbase; XB-GENE-6079334; tdrd6.L.
DR OrthoDB; 496838at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398252; Expressed in testis and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd04508; TUDOR; 5.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00567; TUDOR; 5.
DR SMART; SM00333; TUDOR; 4.
DR PROSITE; PS50304; TUDOR; 5.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Oogenesis; Reference proteome; Repeat;
KW Spermatogenesis.
FT CHAIN 1..1905
FT /note="Tudor domain-containing 6-like"
FT /id="PRO_0000448695"
FT DOMAIN 1..30
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 215..279
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 435..491
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 853..910
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1060..1118
FT /note="Tudor 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 564..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1827..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1905 AA; 213660 MW; 275311110716F042 CRC64;
MVEVYFIDHG NTEMVDWYNV KKLPAELREM PGLAIHCCVA DICPLGVRWS PEAILAFKIA
VVDKKLIIYV VSKELHKYII EVLDNSRIEQ RSMAKILSAA GHAKYEEVEP VAQHTGNMSD
IDNETQQQFL GYINKDTSSL KTQQKEDVCS MEDDNSVPYS PYEDQFFEPG ATIEVVVSCI
ISPGLFWCQN ASLSSKLEKL MAKIQDYCSS TDCPYERGAY ACLAKSSCDG KWYRAFITNN
RPGSKANANQ VEVLYVDYGI TETVLVKDLR CIESELFDLK AQAFRCSLYN LIAPDSENPF
EWDTKATLSF HRFVDSSAKK CSEFKCTFFA TALVKTELSY IVDVFTPFAS ICKLLVELGH
AKQLSHTTLA PSVQLQTYYY SMHDIKIGGE EEVYITYVNS SLEFYCQLSR NTETIDMIAS
ATARVCSEVR KFELSVTPGP LCLAKFSDQQ WYRCFINTNK NSTDAFFVDY GNTEKVNKEE
MLPIPSDAYE LLHFPMQAIK CSLSDMPDTV PSDVVLWFEN HVLEKPLRAI IVAKETDGKL
IVELYDGSQQ INSILKTKLG WKSSRAEGSF GNSEKRNQLN DLDRGGRKET TSKFQPYSQG
SKFSPDLDGH SQNGLTYQKP EFQTKEREQF EQKPNLRTPR SYNNDREVYQ VQKNMSQSGF
APQKTGGFRS KDREAFEQRP NLKASGLYSQ GRETPSMSQN SSYSGFPPQK TGAFRSKERQ
VSEHKQNSNP PKFYNQERKL SPQLRKASQN GSSSQTEAFW SSGSDQSSEH KPDNASQQRR
STFQESKLTP PLSKLSDLPK QNIALGMKSS VYVAHTNTIS DFYVHIAQNT DLSNISEILN
NEKGPSDQLD EKYVNLGDLI CAFYEDGLYY RAVITEKCAD GLLAQYIDYG NTSVIPPTKI
YKLPPSLLSI PAMSICCALD KCTTSACEQN MDDLMLKFSE RTGDLELSCE FVQYNNRKWN
VILCDDQGCI NDLFISVSGD PMLNPPLPKE PSVTSETLIS ASLFVWNLPE LGETVEAFAS
AVDSPEHFWC QLATANVDSL AVKVQEAGEH SIHDGRFSAE IEVGSPCNVI YSDDNYWYRA
AVTKMKDDKV TVRFVDYGNE ETLQMEQVRR LPADIAAIPV QAFPCSLANF NLSEGCWSSE
ANTFFYDKVT EGLLEITVLH IQELGLCKIP QASVNVKYNG EDINCEMRRF WQDSFVNTNP
FTESLNAKEE TAIEDNVIPS QADEDDHSEP SEEPCASESI ETPAVDGEVL TANDETKLEA
LPVSSAEEAA EITDNTDVEL MRTEYLLHEV QKSSDLSCLE LTLDEDVPDE KNSGTPAVTP
LAAEDLCIDY DESNIKKSYS GVTTEMDNRE LHQDEDLDLW TSAAQDQEIA SSEILGDVPI
DKECNYSVEE ATDQSCTNIG LEEGPEPVEN AFTENINDET DIANVQSKGE EEEAYLVPEE
STVAECEIED FEPEVDLQSK ENEGLPDIPL LEGDGDDSVS PEEVSSHEMN EAEGLEDQDQ
ELLGYTGTER AMDDYEVLQS EEQAEDLVPE EDPGTETEHR SYLFEAEEAD LPSQEHKDFP
EQEEDRVAEH KNDISEPDLQ SKEQKEDLVP EEDPGTETEH RSYLFEAEET DLPSQEHKDT
VTYTDIPLLE GGVDDFGSKE TVSIDYNYEY VTEDVEDLDT ENQESQICIS GSDNRSKESG
PVDLQDFEDE VLFQYTEPTA DSASDVRQGD ECEFAAHSDE NIESPEHPVH TDSTADVCET
DVCEPEVADH CHLQDKVVSE RTECPVPDDR TKDDHQNNEC QCAVDPVENI ECQTPVCLVA
ADRSYTEYTW TVSETESGNM KNIEFQESPA EGDSVGSHGV GATEWKDGEP ESLVNPDTPL
LEGPVSVDIM HSSDNFEPET DDMEQMEQDQ GRMKIESSYV PAPSV
