THA11_MOUSE
ID THA11_MOUSE Reviewed; 305 AA.
AC Q9JJD0; Q3TCZ5; Q99KZ0;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=THAP domain-containing protein 11;
DE AltName: Full=Ronin;
GN Name=Thap11; ORFNames=MNCb-2032;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND INTERACTION WITH HCFC1.
RX PubMed=18585351; DOI=10.1016/j.cell.2008.05.047;
RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA Songyang Z., Thomson J.A., Zwaka T.P.;
RT "Ronin is essential for embryogenesis and the pluripotency of mouse
RT embryonic stem cells.";
RL Cell 133:1162-1174(2008).
RN [6]
RP ERRATUM OF PUBMED:18585351.
RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA Songyang Z., Thomson J.A., Zwaka T.P.;
RL Cell 134:692-692(2008).
CC -!- FUNCTION: Transcriptional repressor that plays a central role for
CC embryogenesis and the pluripotency of embryonic stem (ES) cells.
CC Sequence-specific DNA-binding factor that represses gene expression in
CC pluripotent ES cells by directly binding to key genetic loci and
CC recruiting epigenetic modifiers. {ECO:0000269|PubMed:18585351}.
CC -!- SUBUNIT: Interacts (via coiled coil domain) with HCFC1.
CC {ECO:0000269|PubMed:18585351}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18585351}. Cytoplasm
CC {ECO:0000269|PubMed:18585351}. Note=May be regulated by shuttling of
CC the protein between the cytoplasm and nucleus.
CC -!- TISSUE SPECIFICITY: Mainly restricted to pluripotent cells of the
CC developing embryo, to oocytes, and to certain regions of the adult
CC brain. {ECO:0000269|PubMed:18585351}.
CC -!- DEVELOPMENTAL STAGE: First appears at the 2-cell stage, intensifies
CC during the 8-cell and compact morula stages, but subsides in the
CC blastocyst. {ECO:0000269|PubMed:18585351}.
CC -!- DISRUPTION PHENOTYPE: Mice show periimplantational lethality and have
CC defects in the inner cell mass. Conditional knockout prevents the
CC growth of ES cells while forced expression allows ES cells to
CC proliferate without differentiation under conditions that normally do
CC not promote self-renewal. {ECO:0000269|PubMed:18585351}.
CC -!- MISCELLANEOUS: Was named 'Ronin' (a masterless Japanese samurai) by
CC PubMed:18585351 because of its lack of apparent relationship to known
CC 'master' regulator of pluripotency.
CC -!- SIMILARITY: Belongs to the THAP11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB041579; BAA95063.1; -; mRNA.
DR EMBL; AK165981; BAE38498.1; -; mRNA.
DR EMBL; AK170457; BAE41810.1; -; mRNA.
DR EMBL; CH466525; EDL11318.1; -; Genomic_DNA.
DR EMBL; BC003949; AAH03949.1; ALT_INIT; mRNA.
DR EMBL; BC138966; AAI38967.1; -; mRNA.
DR EMBL; BC138987; AAI38988.1; -; mRNA.
DR CCDS; CCDS22616.1; -.
DR RefSeq; NP_067488.1; NM_021513.2.
DR AlphaFoldDB; Q9JJD0; -.
DR BMRB; Q9JJD0; -.
DR SMR; Q9JJD0; -.
DR BioGRID; 208487; 3.
DR ELM; Q9JJD0; -.
DR STRING; 10090.ENSMUSP00000048994; -.
DR iPTMnet; Q9JJD0; -.
DR PhosphoSitePlus; Q9JJD0; -.
DR EPD; Q9JJD0; -.
DR MaxQB; Q9JJD0; -.
DR PaxDb; Q9JJD0; -.
DR PeptideAtlas; Q9JJD0; -.
DR PRIDE; Q9JJD0; -.
DR ProteomicsDB; 263172; -.
DR Antibodypedia; 29649; 286 antibodies from 34 providers.
DR DNASU; 59016; -.
DR Ensembl; ENSMUST00000040445; ENSMUSP00000048994; ENSMUSG00000036442.
DR GeneID; 59016; -.
DR KEGG; mmu:59016; -.
DR UCSC; uc009nei.2; mouse.
DR CTD; 57215; -.
DR MGI; MGI:1930964; Thap11.
DR VEuPathDB; HostDB:ENSMUSG00000036442; -.
DR eggNOG; ENOG502QQ1Z; Eukaryota.
DR GeneTree; ENSGT00390000006585; -.
DR HOGENOM; CLU_090879_1_0_1; -.
DR InParanoid; Q9JJD0; -.
DR OMA; NSHRDKD; -.
DR OrthoDB; 1177412at2759; -.
DR PhylomeDB; Q9JJD0; -.
DR TreeFam; TF331359; -.
DR BioGRID-ORCS; 59016; 32 hits in 76 CRISPR screens.
DR ChiTaRS; Thap11; mouse.
DR PRO; PR:Q9JJD0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JJD0; protein.
DR Bgee; ENSMUSG00000036442; Expressed in dorsal pancreas and 253 other tissues.
DR Genevisible; Q9JJD0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0022900; P:electron transport chain; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:2000825; P:positive regulation of androgen receptor activity; IMP:MGI.
DR GO; GO:1903108; P:regulation of mitochondrial transcription; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006612; THAP_Znf.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..305
FT /note="THAP domain-containing protein 11"
FT /id="PRO_0000068654"
FT ZN_FING 1..80
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 85..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..296
FT /evidence="ECO:0000255"
FT MOTIF 234..237
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250"
FT COMPBIAS 101..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33276 MW; 8586597DABC8601A CRC64;
MPGFTCCVPG CYNNSHRDKA LHFYTFPKDA ELRRLWLKNV SRAGVSGCFS TFQPTTGHRL
CSVHFQGGRK TYTVRVPTIF PLRGVNERKV ARRPAGAAAA RRRQQQQQQQ QQQQQQQQLQ
QQQPSPSSST AQTTQLQPNL VSASAAVLLT LQAAVDSNQA PGSVVPVSTT PSGDDVKPID
LTVQVEFAAA EGAAAAAAAS ELEAATAGLE AAECTLGPQL VVVGEEGFPD TGSDHSYSLS
SGTTEEELLR KLNEQRDILA LMEVKMKEMK GSIRHLRLTE AKLREELREK DRLLAMAVIR
KKHGM
