TDRD1_ORYLA
ID TDRD1_ORYLA Reviewed; 1133 AA.
AC A9CPT4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Tudor domain-containing protein 1;
GN Name=tdrd1;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18224712; DOI=10.1002/dvdy.21448;
RA Aoki Y., Nagao I., Saito D., Ebe Y., Kinjo M., Tanaka M.;
RT "Temporal and spatial localization of three germline-specific proteins in
RT medaka.";
RL Dev. Dyn. 237:800-807(2008).
CC -!- FUNCTION: Plays a central role during spermatogenesis by participating
CC in the repression transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons. Required for the localization of Piwi
CC proteins to the meiotic nuage. Involved in the piRNA metabolic process
CC by ensuring the entry of correct transcripts into the normal piRNA pool
CC and limiting the entry of cellular transcripts into the piRNA pathway.
CC May act by allowing the recruitment of piRNA biogenesis or loading
CC factors that ensure the correct entry of transcripts and piRNAs into
CC Piwi proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and PIWIL4
CC (when methylated on arginine residues) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC meiotic nuage, also named P granule, a germ-cell-specific organelle
CC required to repress transposon activity during meiosis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in both the ovary and testis in the
CC adult. Present in migrating primordial germ cells (PGCs) and also in
CC the germ cells in both the gonadal primordia (stage 33), and in the
CC developing ovary and testis. {ECO:0000269|PubMed:18224712}.
CC -!- SIMILARITY: Belongs to the TDRD1 family. {ECO:0000305}.
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DR EMBL; AB306932; BAF94306.1; -; mRNA.
DR RefSeq; NP_001116401.1; NM_001122929.2.
DR STRING; 8090.ENSORLP00000006085; -.
DR GeneID; 100144383; -.
DR KEGG; ola:100144383; -.
DR CTD; 56165; -.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; A9CPT4; -.
DR OrthoDB; 703199at2759; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 4.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Differentiation; Meiosis; Metal-binding;
KW Reference proteome; Repeat; RNA-mediated gene silencing; Zinc; Zinc-finger.
FT CHAIN 1..1133
FT /note="Tudor domain-containing protein 1"
FT /id="PRO_0000367316"
FT DOMAIN 204..264
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 435..494
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 656..714
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 904..962
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT ZN_FING 75..111
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 1133 AA; 123303 MW; C673E4339FA7F31A CRC64;
MNELRMPNLV RPNRPLREPA SRPLTPSRFP VPSQPDAAYT GSAAGSTGLG SPGPAIMDGS
TSFGLVQPAP TAHFCHYCGQ QGIFRCKGCK KTPYCSVDCQ REDWKAHRHM CKSFDPETVG
ENMKESPDSD NVREDSLNIQ RIYLKDLNAT KYTKGAEIQG AVVEFNSPGR FFFLPEDPKV
MEALMSITAE XQKXPSSTVG TPYVPCVGEV CSVQFSXDLN WYRGLIQTLA ADQKTAHVLY
IDYGNAENVP VERIKPLNIA TKPYCPCAME CQXAGVVPIV DSWSTECCMT VRQLLGGKTL
TIKLVDTLKN GRVHTVDIQL SIGKQLSTFL LEQGYAFAEA AAVGSAPAKK DPSALLEASM
ENFKRCCEGK DINEWAQPPE PLTLTIGDRF SVVVSHFQSP TDFIVQKVEN AGVIQDLQLK
LREHCSGVET QQDFRPAPGT VCCAQFSEDK QWYRAQVLAY STEKSVCVGY IDFGNSEEVD
LNHLRPISPA LLALPKQAIS CILAGVQPVE DSWSEECIST MLRMIANKTV NVEIQSAHKG
KALVAIIEGE GYSEINVAEL LISANYAAPA DSNTLQQTEE TTASAEPPAS PPVCEPLVWS
CVELPSDGQT VVLSTSAVTS PAEFYCCVGP TTDHQVLMEL GVQLKQHCQS DSTYFVPKVG
EPCCVKFSGD GKWYRAMVKE LLGDVVKVNF VDFGHNMIVG KGCLRSITPK LLKLPFQAVR
CWLAGVKPAG SEWSSEALLW FQNLVDGAQL LARVVSVSQQ GYGVELESGG QSVAAALVSQ
QFAKPSGNLS KDPVRSPTTK QEDLRGGDQS QALTPASNDT QAVCEDGKSE EEPSEVATFS
SAWKTAELPL NETFQPCVAA VINPTLFYLL HPIQNVDQQK LQEVMLELAL HCSNYQSSSS
VDTRPVPGAA CCAQFSVDKI WYRAIILEVG EAEMSVVYAD YGNSEKVPVS QILPIPTRLL
QLPFKIIRCT LAGNEHFPVE WPPQVQQVFR SELLNVMATV QSFDGSANVL SLALPPERGG
RNLAAVIQEM LHVHRKGSPL PDASQTPGSD ATEPSCIKLG STTASPDEPE DAAEPADAVT
NTQESTPQEQ KEMDQATSVH DLQGPGCCCQ SLKKQMDRLE KMVQLLLSLQ AEG
