TDRD5_MOUSE
ID TDRD5_MOUSE Reviewed; 1040 AA.
AC Q5VCS6; A7YQ76; D3YXM4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tudor domain-containing protein 5;
GN Name=Tdrd5; Synonyms=Gm103;
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 MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 367-955 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15465492; DOI=10.1016/j.modgep.2004.04.002;
RA Smith J.M., Bowles J., Wilson M., Teasdale R.D., Koopman P.;
RT "Expression of the tudor-related gene Tdrd5 during development of the male
RT germline in mice.";
RL Gene Expr. Patterns 4:701-705(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND SER-943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=21383078; DOI=10.1083/jcb.201009043;
RA Yabuta Y., Ohta H., Abe T., Kurimoto K., Chuma S., Saitou M.;
RT "TDRD5 is required for retrotransposon silencing, chromatoid body assembly,
RT and spermiogenesis in mice.";
RL J. Cell Biol. 192:781-795(2011).
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.
CC {ECO:0000269|PubMed:21383078}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21383078}.
CC Note=Localizes to chromatoid body (CB) and pi-body (also called
CC intermitochondrial cementin), 2 cytoplasmic ribonucleoprotein granules
CC involved in RNA processing for spermatogenesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VCS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VCS6-2; Sequence=VSP_041054;
CC -!- TISSUE SPECIFICITY: Gonad-specific. Mainly expressed in testis. Present
CC at low level in ovary (at protein level). {ECO:0000269|PubMed:15465492,
CC ECO:0000269|PubMed:21383078}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in germ cells of the
CC developing testis, starting from 12.5 dpc. The protein is detected as
CC early as 13.5 dpc in embryonic testes, but expression declines around
CC the perinatal period and then is restored at around 2 weeks after
CC birth. Also detected in the embryonic ovary at a low level. In adult
CC testis, mainly present in the spermatocytes from the pachytene stage
CC onward (at protein level). {ECO:0000269|PubMed:15465492,
CC ECO:0000269|PubMed:21383078}.
CC -!- DISRUPTION PHENOTYPE: Male sterility because of spermiogenic arrest at
CC the round spermatid stage, with occasional failure in meiotic prophase.
CC Effects are due to demethylation and subsequent derepression of
CC transposable elements: germ cells fail to repress LINE-1 (L1)
CC retrotransposons with DNA-demethylated promoters. Defects in chromatoid
CC body (CB) and pi-body assembly are also observed. Interestingly, Tdrd5-
CC deficient round spermatids injected into oocytes contribute to fertile
CC offspring, showing that acquisition of a functional haploid genome may
CC be uncoupled from Tdrd5 function. {ECO:0000269|PubMed:21383078}.
CC -!- SIMILARITY: Belongs to the TDRD5 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; AK132674; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK133026; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC161414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099972; AAH99972.1; -; mRNA.
DR EMBL; AY522557; AAU04873.1; -; mRNA.
DR CCDS; CCDS56647.1; -. [Q5VCS6-1]
DR RefSeq; NP_001128213.1; NM_001134741.1. [Q5VCS6-1]
DR RefSeq; NP_001264659.1; NM_001277730.1. [Q5VCS6-2]
DR RefSeq; XP_006496796.1; XM_006496733.2. [Q5VCS6-2]
DR AlphaFoldDB; Q5VCS6; -.
DR SMR; Q5VCS6; -.
DR STRING; 10090.ENSMUSP00000137298; -.
DR iPTMnet; Q5VCS6; -.
DR PhosphoSitePlus; Q5VCS6; -.
DR jPOST; Q5VCS6; -.
DR PaxDb; Q5VCS6; -.
DR PRIDE; Q5VCS6; -.
DR ProteomicsDB; 254686; -. [Q5VCS6-1]
DR ProteomicsDB; 254687; -. [Q5VCS6-2]
DR Antibodypedia; 2903; 19 antibodies from 12 providers.
DR Ensembl; ENSMUST00000121146; ENSMUSP00000137298; ENSMUSG00000060985. [Q5VCS6-1]
DR GeneID; 214575; -.
DR KEGG; mmu:214575; -.
DR UCSC; uc029qui.1; mouse. [Q5VCS6-1]
DR UCSC; uc029quj.1; mouse. [Q5VCS6-2]
DR CTD; 163589; -.
DR MGI; MGI:2684949; Tdrd5.
DR VEuPathDB; HostDB:ENSMUSG00000060985; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00940000159902; -.
DR HOGENOM; CLU_013593_0_0_1; -.
DR InParanoid; Q5VCS6; -.
DR OMA; YVMPEYF; -.
DR OrthoDB; 1115068at2759; -.
DR PhylomeDB; Q5VCS6; -.
DR TreeFam; TF342664; -.
DR BioGRID-ORCS; 214575; 1 hit in 78 CRISPR screens.
DR PRO; PR:Q5VCS6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5VCS6; protein.
DR Bgee; ENSMUSG00000060985; Expressed in spermatocyte and 51 other tissues.
DR ExpressionAtlas; Q5VCS6; baseline and differential.
DR Genevisible; Q5VCS6; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0030719; P:P granule organization; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP: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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..1040
FT /note="Tudor domain-containing protein 5"
FT /id="PRO_0000281122"
FT DOMAIN 7..80
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 122..197
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 291..365
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 533..592
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 857..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 132..227
FT /note="SELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISV
FT EQTRAGSLLTLKKSVSEDKQRGWPAGKVFTQPFRMKQQGSYSTG -> R (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041054"
FT CONFLICT 662
FT /note="E -> G (in Ref. 4; AAU04873)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="K -> E (in Ref. 4; AAU04873)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="D -> N (in Ref. 4; AAU04873)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="G -> E (in Ref. 4; AAU04873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1040 AA; 116016 MW; 3A3D824431B2B04D CRC64;
MSEQERIQDC LRKEIRSLLI STKDGLTPQQ LEKEYLLMVG NHLPLRILGY RSTMELVLDM
PDVVSVCPGG DGTVILKAIP DESTKGIASL VAKQRRSHKV RNSMPKGRPS ICSGRVPYRG
RVPPILPAVV KSELKDLLAL SPVLLSDFEK AFARRFGRSF QYMQYGFLSM FEVLNAASDV
ISVEQTRAGS LLTLKKSVSE DKQRGWPAGK VFTQPFRMKQ QGSYSTGFPV MKAHFSQPIS
NMEPPKQVLS MAKTPTFNSV EASRLNHTEK LNQLESTFKS VIAQIGPGGT VDPELKRKIQ
FVVSKFPQGL FISKLLGEFE LTFKEQLSPK QLGFLNVTEL VGALSDILRV EFSEERQDLL
VFDADLKPLP SGGPLSSVRN SCLVQPDKKT EANPWTSSLS RNSLSTVAVK KTTWDCPLKN
QKEPEQKIYK KPNLVVKPLQ LQVETNKPQL SLSVANHDIP PDAVRAKKLC RLPPLDTSTL
VGVFVEYIIS PSQFYIRIYS RDSSELLEDM MIEMRRCYSN QLVSDRYIMP EYFIQPGHLC
CVKISEDKWW YRVIIHRILG KKEVEVFYPD FGNIGTVQKS SLRFLKCCYT KLPAQAIPCS
LAWVRPAEEH WTARAILHFQ KLCGLKPLVG VVDEYIDGIL NIFLCDTSSN EDVYFHHVLR
TEGHAIVCRE NAPSKGFRDF NPPALYTNAS SAGDMVLTDL GHPAQQHYLN EDQEILQQAQ
QDINDGKCIS YLKSAPKELL KDSKLSSLKT HKSCEEDPRW SILQPKDLKE ENEDEVPTGM
PCLESVTIGD DVWDENWLPL QAKMGKAGSP ASQLFTSNLV GKKQYQTGGE MAQKDWCFST
SKDIWDDSWQ PLGLANDVKG GIHTPEGPIA QEKNTSTTRI QQQPDLQYPL DSSTLPKLEE
FYISLIKSQQ SAERSQSEPA SIQTHAGRAA SKALSSTPAV GDSPENHSGS VESSPGSLKK
EDVSNSRAEA TAKDKSQGAI DQLSFILSPQ HQISQKLYIP RSTATAVLGA AARLATSRSL
LHWYPSVKGG KLEAERDGVK
