ID A0A2R8Y872_HUMAN Unreviewed; 1335 AA.
AC A0A2R8Y872;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=TDRD12 {ECO:0000313|Ensembl:ENSP00000496698.1};
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 {ECO:0000313|Ensembl:ENSP00000496698.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000496698.1, ECO:0000313|Proteomes:UP000005640}
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] {ECO:0000313|Ensembl:ENSP00000496698.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR EMBL; AC008736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011525773.1; XM_011527471.2.
DR SMR; A0A2R8Y872; -.
DR MassIVE; A0A2R8Y872; -.
DR PeptideAtlas; A0A2R8Y872; -.
DR Antibodypedia; 47944; 46 antibodies from 12 providers.
DR DNASU; 91646; -.
DR Ensembl; ENST00000647536.1; ENSP00000496698.1; ENSG00000173809.18.
DR GeneID; 91646; -.
DR CTD; 91646; -.
DR HGNC; HGNC:25044; TDRD12.
DR VEuPathDB; HostDB:ENSG00000173809; -.
DR GeneTree; ENSGT00420000029847; -.
DR OMA; KMHKEVV; -.
DR OrthoDB; 5351296at2759; -.
DR ChiTaRS; TDRD12; human.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000173809; Expressed in primordial germ cell in gonad and 125 other cell types or tissues.
DR ExpressionAtlas; A0A2R8Y872; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd20434; Tudor_TDRD12_rpt1; 1.
DR CDD; cd20435; Tudor_TDRD12_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.40.50.90; -; 2.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047390; Tudor_TDRD12_rpt1.
DR PANTHER; PTHR22655:SF2; ATP-DEPENDENT RNA HELICASE TDRD12-RELATED; 1.
DR PANTHER; PTHR22655; UNCHARACTERIZED; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00567; TUDOR; 2.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|MaxQB:A0A2R8Y872,
KW ECO:0007829|PeptideAtlas:A0A2R8Y872};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 1190..1276
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 1103..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 151151 MW; 54B2041E02187A2E 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 NHFIFRDKRI CPDRHRINPE TDLPRKLSSQ ALPSFGYIKI IPFYILNATN
YFGRIVDKHM DLYATLNAEM NEYFKDSNKT TVEKVEKFGL YGLAEKTLFH RVQVLEVNQK
EDAWALDDIL VEFIDEGRTG LVTRDQLLHL PEHFHTLPPQ AVEFIVCRVK PADNEIEWNP
KVTRYIHHKI VGKLHDAKVI LALGNTVWID PMVHITNLSS LKTSVIDYNV RAEILSMGMG
IDNPEHIEQL KKLREDAKIP ACEESLSQTP PRVTGTSPAQ DQDHPSEEQG GQGTPPAEDA
ACLQSPQPED TGAEGGAESK TSSENQKPET LSGNTEGAFI SRTAQPPLKS FHPQIKWFQK
EDVVILKIRI RNVKDYKCQY LRDRVVFSAW VGDKFYLADL ELRGNIRKDD CQCVIRNDEP
VITLAKERRE AWCHLLRQRN PNVAFDFDHW EDCEEDSHFP KVVNSKNLPY TVTEVVEDSS
STSEDDDSES EREGE
//
