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Database: UniProt
Entry: A9CPT4
LinkDB: A9CPT4
Original site: A9CPT4 
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   08-MAY-2019, entry version 62.
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;
OC   Oryziinae; Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   in medaka.";
RL   Dev. Dyn. 237:800-807(2008).
CC   -!- FUNCTION: Plays a central role during spermatogenesis by
CC       participating in the repression transposable elements and
CC       preventing their mobilization, which is essential for the germline
CC       integrity. Acts via the piRNA metabolic process, which mediates
CC       the repression of transposable elements during meiosis by forming
CC       complexes composed of piRNAs and Piwi proteins and governs the
CC       methylation and subsequent repression of transposons. Required for
CC       the localization of Piwi proteins to the meiotic nuage. Involved
CC       in the piRNA metabolic process by ensuring the entry of correct
CC       transcripts into the normal piRNA pool and limiting the entry of
CC       cellular transcripts into the piRNA pathway. May act by allowing
CC       the recruitment of piRNA biogenesis or loading factors that ensure
CC       the correct entry of transcripts and piRNAs into Piwi proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and
CC       PIWIL4 (when methylated on arginine residues) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of
CC       the meiotic nuage, also named P granule, a germ-cell-specific
CC       organelle required to repress transposon activity during meiosis.
CC       {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
CC       in the germ cells in both the gonadal primordia (stage 33), and in
CC       the developing ovary and testis. {ECO:0000269|PubMed:18224712}.
CC   -!- SIMILARITY: Belongs to the TDRD1 family. {ECO:0000305}.
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   InParanoid; A9CPT4; -.
DR   KO; K18405; -.
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:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Meiosis; Metal-binding; Reference proteome; Repeat;
KW   RNA-mediated gene silencing; Zinc; Zinc-finger.
FT   CHAIN         1   1133       Tudor domain-containing protein 1.
FT                                /FTId=PRO_0000367316.
FT   DOMAIN      204    264       Tudor 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   DOMAIN      435    494       Tudor 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   DOMAIN      656    714       Tudor 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   DOMAIN      904    962       Tudor 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   ZN_FING      75    111       MYND-type. {ECO:0000255|PROSITE-
FT                                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
//
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