TDRD7_MOUSE
ID TDRD7_MOUSE Reviewed; 1086 AA.
AC Q8K1H1; B1AWG7; B1AWH5; Q8R181;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Retina;
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 SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH CABLES1 AND CDK17,
RP AND INTERACTION WITH CABLES1.
RC TISSUE=Brain;
RX PubMed=11527406; DOI=10.1006/bbrc.2001.5493;
RA Yamochi T., Nishimoto I., Okuda T., Matsuoka M.;
RT "ik3-1/Cables is associated with Trap and Pctaire2.";
RL Biochem. Biophys. Res. Commun. 286:1045-1050(2001).
RN [4]
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17141210; DOI=10.1016/j.ydbio.2006.10.046;
RA Hosokawa M., Shoji M., Kitamura K., Tanaka T., Noce T., Chuma S.,
RA Nakatsuji N.;
RT "Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
RT composition, intracellular localization, and function in male germ cells in
RT mice.";
RL Dev. Biol. 301:38-52(2007).
RN [5]
RP INTERACTION WITH PIWIL1.
RX PubMed=19584108; DOI=10.1101/gad.1814809;
RA Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT "Proteomic analysis of murine Piwi proteins reveals a role for arginine
RT methylation in specifying interaction with Tudor family members.";
RL Genes Dev. 23:1749-1762(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=21436445; DOI=10.1126/science.1195970;
RA Lachke S.A., Alkuraya F.S., Kneeland S.C., Ohn T., Aboukhalil A.,
RA Howell G.R., Saadi I., Cavallesco R., Yue Y., Tsai A.C., Nair K.S.,
RA Cosma M.I., Smith R.S., Hodges E., Alfadhli S.M., Al-Hajeri A.,
RA Shamseldin H.E., Behbehani A., Hannon G.J., Bulyk M.L., Drack A.V.,
RA Anderson P.J., John S.W., Maas R.L.;
RT "Mutations in the RNA granule component TDRD7 cause cataract and
RT glaucoma.";
RL Science 331:1571-1576(2011).
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:0000269|PubMed:21436445}.
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. {ECO:0000269|PubMed:11527406,
CC ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19584108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11527406,
CC ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:21436445}.
CC Note=Localizes to cytoplasmic RNA granules. 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.
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed in
CC spermatogonia, spermatocytes and round spermatids (at protein level).
CC Also expressed in the developing lens. {ECO:0000269|PubMed:17141210,
CC ECO:0000269|PubMed:21436445}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, it is expressed in differentiating
CC fiber cells in the posterior lens, but not in the anterior epithelium
CC of the lens (AEL). {ECO:0000269|PubMed:21436445}.
CC -!- DISRUPTION PHENOTYPE: Mice develop cataracts and glaucoma and males are
CC sterile. Within 4 weeks of birth, mice develop a posterior cataract
CC that becomes severe with age. At later stages, the lens fiber cell
CC compartment develops vacuoles with lens capsule rupture and extrusion
CC of fiber cell mass into the vitreous. In addition, the mass of fiber
CC cells passes through the pupil into the anterior chamber of the eye. By
CC 4 months of age, iris flattening is detected and anterior chamber depth
CC increased. By 6 months of age, the intraocular pressure (IOP) is
CC elevated in some mutants, and the incidence of elevated IOP increases
CC with age, leading to glaucome. Severe optic nerve atrophy characterized
CC by retinal ganglion cell axon loss and excavative remodeling of the
CC optic nerve are observed. In addition, males display sterility due to
CC an arrest in spermatogenesis at the round spermatid stage, likely due
CC to a chromatoid body defect. {ECO:0000269|PubMed:21436445}.
CC -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM17034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM22130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL732615; CAM17026.1; -; Genomic_DNA.
DR EMBL; AL732615; CAM17034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772381; CAM17034.1; JOINED; Genomic_DNA.
DR EMBL; AL772381; CAM22130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL732615; CAM22130.1; JOINED; Genomic_DNA.
DR EMBL; BC025099; AAH25099.1; -; mRNA.
DR EMBL; BC029689; AAH29689.1; -; mRNA.
DR CCDS; CCDS18142.1; -.
DR RefSeq; NP_001277404.1; NM_001290475.1.
DR RefSeq; NP_666254.1; NM_146142.2.
DR RefSeq; XP_006537580.1; XM_006537517.3.
DR PDB; 2LH9; NMR; -; A=1-76.
DR PDB; 2LY1; NMR; -; A=223-400.
DR PDB; 2LY2; NMR; -; A=223-400.
DR PDBsum; 2LH9; -.
DR PDBsum; 2LY1; -.
DR PDBsum; 2LY2; -.
DR AlphaFoldDB; Q8K1H1; -.
DR BMRB; Q8K1H1; -.
DR SMR; Q8K1H1; -.
DR STRING; 10090.ENSMUSP00000099993; -.
DR iPTMnet; Q8K1H1; -.
DR PhosphoSitePlus; Q8K1H1; -.
DR MaxQB; Q8K1H1; -.
DR PaxDb; Q8K1H1; -.
DR PeptideAtlas; Q8K1H1; -.
DR PRIDE; Q8K1H1; -.
DR ProteomicsDB; 262748; -.
DR Antibodypedia; 14331; 89 antibodies from 20 providers.
DR DNASU; 100121; -.
DR Ensembl; ENSMUST00000102929; ENSMUSP00000099993; ENSMUSG00000035517.
DR GeneID; 100121; -.
DR KEGG; mmu:100121; -.
DR UCSC; uc008stc.2; mouse.
DR CTD; 23424; -.
DR MGI; MGI:2140279; Tdrd7.
DR VEuPathDB; HostDB:ENSMUSG00000035517; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00890000139482; -.
DR HOGENOM; CLU_283554_0_0_1; -.
DR InParanoid; Q8K1H1; -.
DR OrthoDB; 1276848at2759; -.
DR BioGRID-ORCS; 100121; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Tdrd7; mouse.
DR PRO; PR:Q8K1H1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K1H1; protein.
DR Bgee; ENSMUSG00000035517; Expressed in epithelium of lens and 232 other tissues.
DR ExpressionAtlas; Q8K1H1; baseline and differential.
DR Genevisible; Q8K1H1; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0043186; C:P granule; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0007281; P:germ cell development; IDA:MGI.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP: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; IMP: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 3D-structure; Cataract; Cytoplasm; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1..1086
FT /note="Tudor domain-containing protein 7"
FT /id="PRO_0000183170"
FT DOMAIN 3..76
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 222..291
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 325..394
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 501..558
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 691..748
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..1086
FT /note="Interaction with CDK17"
FT /evidence="ECO:0000250"
FT REGION 881..1086
FT /note="Interaction with CABLES1"
FT /evidence="ECO:0000269|PubMed:11527406"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:2LH9"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2LH9"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2LH9"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:2LH9"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2LH9"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2LH9"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2LH9"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:2LY1"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:2LY1"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2LY1"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:2LY1"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:2LY1"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:2LY1"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:2LY1"
SQ SEQUENCE 1086 AA; 122174 MW; 90FF74E1CDD24F86 CRC64;
MLEADLVSKM LRAVLQSHKN GIVLPRLQGE YRSLTGDWIP FKQLGYPTLE AYLRSVPAVV
RIEASRSGEI VCYAVACTET ARIAQLVARQ RTSKRKIGRQ INCQMRVKKA MPFFLEGKPK
ATLRQPGFAS DYSISRKPNS ALLRDRGSAL GVKADVDMPP YPDTPVQRHA SMSANSRFSP
KSSLPASFQT HISRACPTEV NDNLNQTVEK PNITPPASYT NKMDEVQNRI KEILDKHNNG
IWISKLPHFY KEFYKEDLNQ GVLQQFEHWP HICTVEKPCG GGQDSLLYPA RREQPLKSDQ
DPEKELPPPP PAPKQEVPSQ GSPAVMPDVK EKVAELLGKY SSGLWASALP KAFEDMYKVK
FPEDALKNLA SLSDVCTINY ISGNTQKAIL YAKLPLPTDK ILKDEGQAQG DFDIKSMIEQ
EYLQIEKNMA ESADEFLEDI TVPPLVIPTE ASPSVLVVEL SNTNDVVIRY VGKDYSAAQE
LMEDEMKEFY SKNPRVTPIQ TVHVGQLLAV NAEEDAWLRA QIISTDENKI KVCYVDYGFC
ENIEKSKAYR LNPRFCSLSF QATKCKLAGL EVLNDDPDLV KAVESLTCGK IFAVEILDKS
DVPLVVLYDT SGEDDININA TCLKAICDRS LQVHLQVDAM YTNVKVTNIC SDGTLYCQVP
CKGLNKLNDL LHKTEDYFHC KHMTSEYFIS LPFCGKICLF HCKGKWLRVE ITNVHSSRAL
DVQFLDSGNS TSVKVSELRE IPPRFLQEML AIPPQAIKCC LADLPQSIGM WTPDAVLWLR
DSVLNCSDCS IKVTKMDETK GVAYVYLFTP NNFPDPHRSI NRQITNADLW KHQKDVFLSA
VSTAASSPGN RNGGTPAPGS PAESLRKSHP EVIKKSVLDH TSSFSLEELP PPVHLSRSGE
HMDVYVPVAC HPGHFVIQPW QEIHKLEVLM EEMILYYSVS EERHIAVERD QVYAAKVENK
WYRVLLKGIL TNGLVSVYEL DYGKHELVNI RKVQPLVDVF RKLPFQAVTA QLAGVKCSQW
SEEASMVFRN HVEKKALVAL VQTVVEHTNP WDRKVVLYLV DTSLPDTDTW IHDFMSQYLL
ELSKVN
