TDRD5_HUMAN
ID TDRD5_HUMAN Reviewed; 981 AA.
AC Q8NAT2; A1L4G5; B7ZLV0; Q5EBN4; Q5VTV0; Q6ZSK2;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tudor domain-containing protein 5;
GN Name=TDRD5; Synonyms=TUDOR3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Substantia nigra;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 195-981 (ISOFORM 3), AND VARIANT LYS-722.
RC TISSUE=Brain, and Testis;
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 [4]
RP IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20302647; DOI=10.1186/1745-6150-5-13;
RA Anantharaman V., Zhang D., Aravind L.;
RT "OST-HTH: a novel predicted RNA-binding domain.";
RL Biol. Direct 5:13-13(2010).
RN [5]
RP IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20305267; DOI=10.1093/bioinformatics/btq122;
RA Callebaut I., Mornon J.P.;
RT "LOTUS, a new domain associated with small RNA pathways in the germline.";
RL Bioinformatics 26:1140-1144(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 1-101.
RG Structural genomics consortium (SGC);
RT "Crystal structure of conserved motif in TDRD5.";
RL Submitted (AUG-2011) to the PDB data bank.
CC -!- FUNCTION: Required during spermiogenesis to participate in the
CC repression transposable elements and prevent their mobilization, which
CC is essential for the germline integrity. Probably acts via the piRNA
CC metabolic process, which mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and govern the methylation and subsequent repression of
CC transposons. Required for chromatoid body (CB) assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to
CC chromatoid body (CB) and pi-body (also called intermitochondrial
CC cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA
CC processing for spermatogenesis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3;
CC IsoId=Q8NAT2-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8NAT2-1; Sequence=VSP_023968;
CC -!- SIMILARITY: Belongs to the TDRD5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03815.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK092142; BAC03815.1; ALT_FRAME; mRNA.
DR EMBL; AK127370; BAC86946.1; -; mRNA.
DR EMBL; AL160286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043368; AAH43368.1; -; mRNA.
DR EMBL; BC089387; AAH89387.1; -; mRNA.
DR EMBL; BC130532; AAI30533.1; -; mRNA.
DR EMBL; BC144058; AAI44059.1; -; mRNA.
DR CCDS; CCDS1332.1; -. [Q8NAT2-3]
DR CCDS; CCDS55663.1; -. [Q8NAT2-1]
DR RefSeq; NP_001186014.1; NM_001199085.1. [Q8NAT2-1]
DR RefSeq; NP_001186018.1; NM_001199089.1. [Q8NAT2-1]
DR RefSeq; NP_001186020.1; NM_001199091.1. [Q8NAT2-3]
DR RefSeq; NP_001186021.1; NM_001199092.1.
DR RefSeq; NP_775804.2; NM_173533.3. [Q8NAT2-3]
DR RefSeq; XP_005244991.1; XM_005244934.1. [Q8NAT2-1]
DR RefSeq; XP_005244992.1; XM_005244935.4. [Q8NAT2-1]
DR RefSeq; XP_016855962.1; XM_017000473.1.
DR PDB; 3S93; X-ray; 2.28 A; A/B=1-101.
DR PDBsum; 3S93; -.
DR AlphaFoldDB; Q8NAT2; -.
DR SMR; Q8NAT2; -.
DR BioGRID; 127869; 7.
DR IntAct; Q8NAT2; 7.
DR MINT; Q8NAT2; -.
DR STRING; 9606.ENSP00000406052; -.
DR iPTMnet; Q8NAT2; -.
DR PhosphoSitePlus; Q8NAT2; -.
DR BioMuta; TDRD5; -.
DR DMDM; 134047943; -.
DR jPOST; Q8NAT2; -.
DR MassIVE; Q8NAT2; -.
DR PeptideAtlas; Q8NAT2; -.
DR PRIDE; Q8NAT2; -.
DR ProteomicsDB; 72696; -. [Q8NAT2-3]
DR ProteomicsDB; 72697; -. [Q8NAT2-1]
DR Antibodypedia; 2903; 19 antibodies from 12 providers.
DR Ensembl; ENST00000294848.12; ENSP00000294848.8; ENSG00000162782.16. [Q8NAT2-3]
DR Ensembl; ENST00000367614.5; ENSP00000356586.1; ENSG00000162782.16. [Q8NAT2-3]
DR Ensembl; ENST00000444136.6; ENSP00000406052.1; ENSG00000162782.16. [Q8NAT2-1]
DR GeneID; 163589; -.
DR KEGG; hsa:163589; -.
DR MANE-Select; ENST00000444136.6; ENSP00000406052.1; NM_001199085.3; NP_001186014.1. [Q8NAT2-1]
DR UCSC; uc001gnf.4; human. [Q8NAT2-3]
DR CTD; 163589; -.
DR DisGeNET; 163589; -.
DR GeneCards; TDRD5; -.
DR HGNC; HGNC:20614; TDRD5.
DR HPA; ENSG00000162782; Tissue enhanced (epididymis, testis).
DR MIM; 617748; gene.
DR neXtProt; NX_Q8NAT2; -.
DR OpenTargets; ENSG00000162782; -.
DR PharmGKB; PA134953461; -.
DR VEuPathDB; HostDB:ENSG00000162782; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00940000159902; -.
DR HOGENOM; CLU_013593_0_0_1; -.
DR InParanoid; Q8NAT2; -.
DR OMA; YVMPEYF; -.
DR OrthoDB; 1115068at2759; -.
DR PhylomeDB; Q8NAT2; -.
DR TreeFam; TF342664; -.
DR PathwayCommons; Q8NAT2; -.
DR SignaLink; Q8NAT2; -.
DR BioGRID-ORCS; 163589; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; TDRD5; human.
DR GenomeRNAi; 163589; -.
DR Pharos; Q8NAT2; Tdark.
DR PRO; PR:Q8NAT2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NAT2; protein.
DR Bgee; ENSG00000162782; Expressed in right testis and 84 other tissues.
DR ExpressionAtlas; Q8NAT2; baseline and differential.
DR Genevisible; Q8NAT2; HS.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0030719; P:P granule organization; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR CDD; cd09975; LOTUS_2_TDRD5; 1.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
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; IPR037982; TDRD5_LOTUS_2.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF12872; OST-HTH; 3.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS51644; HTH_OST; 3.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Phosphoprotein; Reference proteome; Repeat;
KW Spermatogenesis.
FT CHAIN 1..981
FT /note="Tudor domain-containing protein 5"
FT /id="PRO_0000183166"
FT DOMAIN 7..80
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 127..202
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 295..369
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 525..584
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 98..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VCS6"
FT VAR_SEQ 720
FT /note="L -> LQDINDEKSLSHLKSESKEPLKDSEFESLKTCNKSFEEDPKWSNPEP
FT NDLKEENE (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023968"
FT VARIANT 104
FT /note="M -> T (in dbSNP:rs12066948)"
FT /id="VAR_031209"
FT VARIANT 239
FT /note="F -> V (in dbSNP:rs12069976)"
FT /id="VAR_052422"
FT VARIANT 358
FT /note="K -> E (in dbSNP:rs6704505)"
FT /id="VAR_031210"
FT VARIANT 722
FT /note="E -> K (in dbSNP:rs35448215)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_036706"
FT CONFLICT 126
FT /note="R -> S (in Ref. 3; AAI30533/AAI44059)"
FT /evidence="ECO:0000305"
FT HELIX 1..20
FT /evidence="ECO:0007829|PDB:3S93"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3S93"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3S93"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3S93"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3S93"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3S93"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3S93"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3S93"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3S93"
SQ SEQUENCE 981 AA; 109737 MW; 09FF49592C97C574 CRC64;
MSEQERIQEC LRKEIRSLLI STKDGLSPQE LEKEYLLMVG NHLPLRILGY RSTMELVLDM
PDVVRVCPGA GGTVILKAIP DESTKGIASL VAKQRSSHKL RNSMHKGRPS IYSGPRSHRR
VPYRGRVAPI LPAVVKSELK DLLALSPVLL SDFEKAFAKR FGRSFQYMQY GFLSMFEVLN
AASDVISVEQ TRAGSLLMLK KSVTEEKPRG CPAGKIFTQP FRMKQGSYST GFPVAKPCFS
QPTSNMEPPK QIMSMEKTSK LNVVETSRLN HTEKLNQLEN TFKSVIAQIG PGGTISSELK
HKIKFVVSKF PEGLFISKLL GEYEVIFKEQ LSPKKLGFLN VTELVGALSD ILHVEFRKGH
QDLLVFDADK KPLPPVQSDK KIEAKACVSS PPRNSLSTAA VKETVWNCPS KKQKEPQQKI
CKKPNLVVKP LQLQVETNKS ELNLAMANHD IPPDAVPNKK LCRLPPLDTS SLIGVFVEYI
ISPSQFYIRI YSRDSSELLE DMMIEMRRCY SNQLVSDRYV MPECFIQPGH LCCVRISEDK
WWYRVIIHRV LEKQEVEVFY PDFGNIGIVQ KSSLRFLKCC YTKLPAQAIP CSLAWVRPVE
EHWTSKAILQ FQKLCGLKPL VGVVDEYVDG ILNIFLCDTS SNEDVYFHHV LRTEGHAIVC
RENISSKGFS ELNPLALYTT SSGGPEDIVL TELGYPSQQH YFNEDRKISP QSKESELRIL
DEIPTGMPCL ESVTIGDDIW DENWLPLQAK MGKGGDAASH LFTASLGGKN QYSSCKEMPQ
KDWCFSTPKD TWDDSWQPSG LVNGTKVEVH KPEVLGAQEK NTGTNRTQKQ LDINGSSDSS
TLPKLEEFCT SLTQSEQSAD GSQSEPNNSQ TQPKQIQLST AAPCSTTAVD DSAEKPSGSV
ESSPEILKNE DFSSSRAITL YKDKRQESVD QLSLILSYEC QISQKLYIPR STATAALGAA
ARLATSRSLL HWYPSVKRME A
