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   27-MAR-2024, entry version 148.
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.ENSMUSP00000103406; -.
DR   iPTMnet; Q8K1H1; -.
DR   PhosphoSitePlus; Q8K1H1; -.
DR   MaxQB; Q8K1H1; -.
DR   PaxDb; 10090-ENSMUSP00000099993; -.
DR   PeptideAtlas; Q8K1H1; -.
DR   ProteomicsDB; 262748; -.
DR   Pumba; Q8K1H1; -.
DR   Antibodypedia; 14331; 102 antibodies from 22 providers.
DR   DNASU; 100121; -.
DR   Ensembl; ENSMUST00000102929.2; ENSMUSP00000099993.2; ENSMUSG00000035517.18.
DR   GeneID; 100121; -.
DR   KEGG; mmu:100121; -.
DR   UCSC; uc008stc.2; mouse.
DR   AGR; MGI:2140279; -.
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; 5403690at2759; -.
DR   BioGRID-ORCS; 100121; 4 hits in 79 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 235 other cell types or tissues.
DR   ExpressionAtlas; Q8K1H1; baseline and differential.
DR   GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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: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 processing; 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; cd09986; LOTUS_1_TDRD7; 1.
DR   CDD; cd09973; LOTUS_2_TDRD7; 1.
DR   CDD; cd09974; LOTUS_3_TDRD7; 1.
DR   CDD; cd20428; Tudor_TDRD7_rpt2; 1.
DR   CDD; cd20429; Tudor_TDRD7_rpt3; 1.
DR   Gene3D; 2.30.30.140; -; 3.
DR   Gene3D; 2.40.50.90; -; 3.
DR   Gene3D; 3.30.420.610; LOTUS domain-like; 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   InterPro; IPR047448; Tudor_TDRD7_rpt2.
DR   InterPro; IPR047449; Tudor_TDRD7_rpt3.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22948:SF29; TUDOR DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF12872; OST-HTH; 1.
DR   Pfam; PF00567; TUDOR; 3.
DR   SMART; SM00333; TUDOR; 3.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 3.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 2.
DR   Genevisible; Q8K1H1; MM.
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
//