TDR12_HUMAN
ID TDR12_HUMAN Reviewed; 1177 AA.
AC Q587J7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative ATP-dependent RNA helicase TDRD12;
DE EC=3.6.4.13;
DE AltName: Full=ES cell-associated transcript 8 protein;
DE AltName: Full=Tudor domain-containing protein 12;
GN Name=TDRD12; Synonyms=ECAT8;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-1177 (ISOFORM 2).
RX PubMed=12787504; DOI=10.1016/s0092-8674(03)00393-3;
RA Mitsui K., Tokuzawa Y., Itoh H., Segawa K., Murakami M., Takahashi K.,
RA Maruyama M., Maeda M., Yamanaka S.;
RT "The homeoprotein Nanog is required for maintenance of pluripotency in
RT mouse epiblast and ES cells.";
RL Cell 113:631-642(2003).
CC -!- FUNCTION: Probable ATP-binding RNA helicase required during
CC spermatogenesis to repress transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons. Involved in the secondary piRNAs metabolic
CC process. Acts via the PET complex, a multiprotein complex required
CC during the secondary piRNAs metabolic process for the PIWIL2 slicing-
CC triggered loading of PIWIL4 piRNAs. {ECO:0000250|UniProtKB:Q9CWU0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Component of a mRNP complex containing PIWIL2, TDRD1 and
CC piRNAs. Component of the PET complex, at least composed of EXD1,
CC PIWIL2, TDRD12 and piRNAs. {ECO:0000250|UniProtKB:Q9CWU0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q587J7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q587J7-2; Sequence=VSP_029675, VSP_029676;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049000; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB211063; BAD95490.1; ALT_INIT; mRNA.
DR CCDS; CCDS46038.1; -. [Q587J7-2]
DR RefSeq; NP_001104292.1; NM_001110822.1. [Q587J7-2]
DR AlphaFoldDB; Q587J7; -.
DR SMR; Q587J7; -.
DR BioGRID; 124857; 1.
DR IntAct; Q587J7; 3.
DR MINT; Q587J7; -.
DR STRING; 9606.ENSP00000390621; -.
DR CarbonylDB; Q587J7; -.
DR iPTMnet; Q587J7; -.
DR PhosphoSitePlus; Q587J7; -.
DR BioMuta; TDRD12; -.
DR DMDM; 162416281; -.
DR EPD; Q587J7; -.
DR MassIVE; Q587J7; -.
DR PaxDb; Q587J7; -.
DR PeptideAtlas; Q587J7; -.
DR PRIDE; Q587J7; -.
DR ProteomicsDB; 62600; -. [Q587J7-1]
DR ProteomicsDB; 62601; -. [Q587J7-2]
DR Antibodypedia; 47944; 46 antibodies from 12 providers.
DR DNASU; 91646; -.
DR Ensembl; ENST00000421545.2; ENSP00000390621.2; ENSG00000173809.18. [Q587J7-2]
DR Ensembl; ENST00000444215.6; ENSP00000416248.2; ENSG00000173809.18. [Q587J7-1]
DR GeneID; 91646; -.
DR KEGG; hsa:91646; -.
DR UCSC; uc002ntq.3; human. [Q587J7-1]
DR CTD; 91646; -.
DR DisGeNET; 91646; -.
DR GeneCards; TDRD12; -.
DR HGNC; HGNC:25044; TDRD12.
DR HPA; ENSG00000173809; Group enriched (epididymis, testis).
DR neXtProt; NX_Q587J7; -.
DR OpenTargets; ENSG00000173809; -.
DR PharmGKB; PA162405542; -.
DR VEuPathDB; HostDB:ENSG00000173809; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00420000029847; -.
DR HOGENOM; CLU_008124_0_0_1; -.
DR InParanoid; Q587J7; -.
DR OrthoDB; 231240at2759; -.
DR PhylomeDB; Q587J7; -.
DR TreeFam; TF332354; -.
DR PathwayCommons; Q587J7; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q587J7; -.
DR BioGRID-ORCS; 91646; 8 hits in 1060 CRISPR screens.
DR ChiTaRS; TDRD12; human.
DR GenomeRNAi; 91646; -.
DR Pharos; Q587J7; Tdark.
DR PRO; PR:Q587J7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q587J7; protein.
DR Bgee; ENSG00000173809; Expressed in right testis and 123 other tissues.
DR ExpressionAtlas; Q587J7; baseline and differential.
DR GO; GO:1990923; C:PET complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00567; TUDOR; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Developmental protein; Differentiation;
KW Helicase; Hydrolase; Meiosis; Nucleotide-binding; Reference proteome;
KW Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1177
FT /note="Putative ATP-dependent RNA helicase TDRD12"
FT /id="PRO_0000311968"
FT DOMAIN 56..118
FT /note="Tudor 1"
FT DOMAIN 447..635
FT /note="Helicase ATP-binding"
FT DOMAIN 900..999
FT /note="Tudor 2"
FT REGION 1098..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 574..577
FT /note="DEAH box"
FT COMPBIAS 1102..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 395
FT /note="L -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12787504"
FT /id="VSP_029675"
FT VAR_SEQ 396..1177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12787504"
FT /id="VSP_029676"
FT CONFLICT 8
FT /note="K -> Q (in Ref. 3; BAD95490)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> S (in Ref. 3; BAD95490)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="K -> E (in Ref. 2; BC049000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1177 AA; 132578 MW; 35C6C813A228132F CRC64;
MLQLLVLKIE DPGCFWVIIK GCSPFLDHDV DYQKLNSAMN DFYNSTCQDI EIKPLTLEEG
QVCVVYCEEL KCWCRAIVKS ITSSADQYLA ECFLVDFAKN IPVKSKNIRV VVESFMQLPY
RAKKFSLYCT KPVTLHIDFC RDSTDIVPAK KWDNAAIQYF QNLLKATTQV EARLCAVEED
TFEVYLYVTI KDEKVCVNDD LVAKNYACYM SPTKNKNLDY LEKPRLNIKS APSFNKLNPA
LTLWPMFLQG KDVQGMEDSH GVNFPAQSLQ HTWCKGIVGD LRPTATAQDK AVKCNMDSLR
DSPKDKSEKK HHCISLKDTN KRVESSVYWP AKRGITIYAD PDVPEASALS QKSNEKPLRL
TEKKEYDEKN SCVKLLQFLN PDPLRADGIS DLQQLQKLKG LQPPVVVLRN KIKPCLTIDS
SPLSADLKKA LQRNKFPGPS HTESYSWPPI ARGCDVVVIS HCESNPLLYL LPVLTVLQTG
ACYKSLPSRN GPLAVIVCPG WKKAQFIFEL LGEYSMSSRP LHPVLLTIGL HKEEAKNTKL
PRGCDVIVTT PYSLLRLLAC QSLLFLRLCH LILDEVEVLF LEANEQMFAI LDNFKKNIEV
EERESAPHQI VAVGVHWNKH IEHLIKEFMN DPYIVITAME EAALYGNVQQ VVHLCLECEK
TSSLLQALDF IPSQAQKTLI FTCSVAETEI VCKVVESSSI FCLKMHKEMI FNLQNVLEQW
KKKLSSGSQI ILALTDDCVP LLAITDATCV IHFSFPASPK VFGGRLYCMS DHFHAEQGSP
AEQGDKKAKS VLLLTEKDAS HAVGVLRYLE RADAKVPAEL YEFTAGVLEA KEDKKAGRPL
CPYLKAFGFC KDKRICPDRH RINPETDLPR KLSSQALPSF GYIKIIPFYI LNATNYFGRI
VDKHMDLYAT LNAEMNEYFK DSNKTTVEKV EKFGLYGLAE KTLFHRVQVL EVNQKEDAWA
LDDILVEFID EGRTGLVTRD QLLHLPEHFH TLPPQAVEFI VCRVKPADNE IEWNPKVTRY
IHHKIVGKLH DAKVILALGN TVWIDPMVHI TNLSSLKTSV IDYNVRAEIL SMGMGIDNPE
HIEQLKKLRE DAKIPACEES LSQTPPRVTG TSPAQDQDHP SEEQGGQGTP PAEDAACLQS
PQPEDTGAEG GAESKTSSEN QKPGGYLVFK RWLSSNR
