ID   TDRD7_RAT               Reviewed;        1113 AA.
AC   Q9R1R4; Q5FVD0;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Tudor domain-containing protein 7;
DE   AltName: Full=PCTAIRE2-binding protein;
DE   AltName: Full=Tudor repeat associator with PCTAIRE-2;
DE            Short=Trap;
GN   Name=Tdrd7; Synonyms=Pctaire2bp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH CDK16 AND
RP   CDK17, AND INTERACTION WITH CDK17.
RC   TISSUE=Hypothalamus;
RX   PubMed=10727952; DOI=10.1046/j.1432-1327.2000.01218.x;
RA   Hirose T., Kawabuchi M., Tamaru T., Okumura N., Nagai K., Okada M.;
RT   "Identification of tudor repeat associator with PCTAIRE 2 (Trap). A novel
RT   protein that interacts with the N-terminal domain of PCTAIRE 2 in rat
RT   brain.";
RL   Eur. J. Biochem. 267:2113-2121(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-874, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to
CC       cytoplasmic RNA granules (By similarity). Present in chromatoid body
CC       (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or
CC       polar granules in Drosophila germ cells), also named processing bodies
CC       (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic
CC       CBs (also called intermitochondrial cementin) in pachytene
CC       spermatocytes and as a single perinuclear CB in haploid round
CC       spermatids (By similarity). According to PubMed:10727952 localizes
CC       preferentially on the periphery of mitochondria. {ECO:0000250,
CC       ECO:0000269|PubMed:10727952}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R1R4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R1R4-2; Sequence=VSP_041317;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC       {ECO:0000269|PubMed:10727952}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 16 dpc onwards.
CC       {ECO:0000269|PubMed:10727952}.
CC   -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB030644; BAA82968.1; -; mRNA.
DR   EMBL; BC090066; AAH90066.1; -; mRNA.
DR   RefSeq; NP_620226.1; NM_138871.1. [Q9R1R4-1]
DR   RefSeq; XP_006238173.1; XM_006238111.3. [Q9R1R4-2]
DR   RefSeq; XP_008761926.1; XM_008763704.1. [Q9R1R4-2]
DR   RefSeq; XP_017449156.1; XM_017593667.1. [Q9R1R4-1]
DR   AlphaFoldDB; Q9R1R4; -.
DR   BMRB; Q9R1R4; -.
DR   SMR; Q9R1R4; -.
DR   STRING; 10116.ENSRNOP00000013726; -.
DR   iPTMnet; Q9R1R4; -.
DR   PhosphoSitePlus; Q9R1R4; -.
DR   PaxDb; Q9R1R4; -.
DR   Ensembl; ENSRNOT00000085738; ENSRNOP00000068568; ENSRNOG00000055779. [Q9R1R4-1]
DR   GeneID; 85425; -.
DR   KEGG; rno:85425; -.
DR   UCSC; RGD:619724; rat. [Q9R1R4-1]
DR   CTD; 23424; -.
DR   RGD; 619724; Tdrd7.
DR   eggNOG; KOG2039; Eukaryota.
DR   GeneTree; ENSGT00890000139482; -.
DR   InParanoid; Q9R1R4; -.
DR   OMA; CKGKWSR; -.
DR   OrthoDB; 1276848at2759; -.
DR   PhylomeDB; Q9R1R4; -.
DR   PRO; PR:Q9R1R4; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000055779; Expressed in testis and 19 other tissues.
DR   Genevisible; Q9R1R4; RN.
DR   GO; GO:0033391; C:chromatoid body; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR   GO; GO:0043186; C:P granule; ISO:RGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR   GO; GO:0007281; P:germ cell development; ISO:RGD.
DR   GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR   GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   CDD; cd09974; LOTUS_3_TDRD7; 1.
DR   CDD; cd04508; TUDOR; 3.
DR   Gene3D; 2.40.50.90; -; 3.
DR   Gene3D; 3.30.420.610; -; 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   Pfam; PF12872; OST-HTH; 2.
DR   Pfam; PF00567; TUDOR; 3.
DR   SMART; SM00333; TUDOR; 3.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Differentiation; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..1113
FT                   /note="Tudor domain-containing protein 7"
FT                   /id="PRO_0000183171"
FT   DOMAIN          3..76
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          249..318
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          352..421
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          528..585
FT                   /note="Tudor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   DOMAIN          718..775
FT                   /note="Tudor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          320..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..1113
FT                   /note="Interaction with CDK17"
FT                   /evidence="ECO:0000269|PubMed:10727952"
FT   REGION          908..1113
FT                   /note="Interaction with CABLES1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        321..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         874
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         177..204
FT                   /note="SVTVLRSHPEASKLQFMGYSPKPHCLLL -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041317"
SQ   SEQUENCE   1113 AA;  125310 MW;  752E2C6CA0D6148A CRC64;
     MLEADLVSKM LRAVLQSHKN GIVLPRLQGE YRSLTGDWIP FKQLGYPTLE AYLRSVPAVV
     RIEASRSGEI VCYAVACTET ARIAQLVARQ RTSKRKTGRQ INCQMRVKKT MPFFLEGKPK
     ATLRQPGFAS DYSISKKPNP TLLREKGSTL GAKADVDMPP YPDAPVQRHV SMSANSSVTV
     LRSHPEASKL QFMGYSPKPH CLLLFSPKSS LPAPFQTHIS RACPKEVNDN LNQTVEKPNV
     TPPASYTNKM DEVQNRIKEI LDKHNNGIWI SKLPHFYKEF YKEDLNQGVL QQFEHWPHIC
     TVEKPCGGGQ DLLLYPAKRE QPLRSDQDPE KERPPPPPAP RQEVPSKGSP AVMPDVKEKV
     AELLGKYSSG LWASALPKAF EDMYKVKFPE DALKNLASLS DVCTINYISG NTQKAILYAK
     LPLPTDKILK DEAQAQGDFD IKSMIEQEYL QIEKNMAESA DDFVEDITVP PLVIPTEASP
     SVLVVELSNT NDVVIRYVGK DYSAAQELME DEMKEYYSRN PRVTPIQTVH VGQLLAVNAE
     EDAWLRAQII STDENKIKVC YVDYGFCENI EKSKAYRLNP RFCSLSFQAT KCKLAGLEIL
     NDDPNLVKVV ESLTCGKIFA VEILDKSDIP LVVLYDTSGE DDININATCL KAICDRSLEV
     HLQVDAMYTN VKVTNICSDG TLYCQVPCKG LNKLNDLLHK TEDYFHCKHM TSEYFISLPF
     CGKICLFHCK GKWLRVEITN VHSSRALDVQ FLDSGNSTSV KVSELREIPP RFLQEMLAIP
     PQAIKCCLAD LPQSIGMWTP DAVLWLRDSV LNCSDCSIKV TKVDEARGVA YVYLFTPKNF
     PDPHRSINRQ ITNADLWKHQ KDVFLSAVSA AASSPGNRNA STPAPGSPAE SLRKSHPEVL
     RKSVLDHTSS FSLEELPPPV HLSKSGEHMD VYVPVACHPG HFVIQPWQEI HKLEVLMEEM
     ILYYSVSEER HIAVERDQVY AAKVENKWYR VLLKGILTNG LVSVYELDYG KHELVNIRKV
     QPLVDVFRKL PFQAVTAQLA GVKCSQWSEE ASMVFRNHVE KKPLVALVQT VIEHANPWDR
     KVVVYLVDTS LPDTDTWIHD FMSQYLVELS KAN