TNR6C_MOUSE
ID TNR6C_MOUSE Reviewed; 1690 AA.
AC Q3UHC0; Q3UZ61; Q80TB6; Q8BXF9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Trinucleotide repeat-containing gene 6C protein;
GN Name=Tnrc6c; Synonyms=Kiaa1582;
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, Cerebellum, and Thymus;
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 MRNA] OF 329-1690.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-313, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays a role in RNA-mediated gene silencing by micro-RNAs
CC (miRNAs). Required for miRNA-dependent translational repression of
CC complementary mRNAs by argonaute family proteins As scaffoldng protein
CC associates with argonaute proteins bound to partially complementary
CC mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase
CC complexes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with one or more of the argonaute family proteins
CC AGO1, AGO2, AGO3 and AGO4. Interacts with CNOT1; the interaction
CC mediates the association with the CCR4-NOT complex. Interacts with
CC PAN3; the interaction mediates the association with the PAN complex (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The silencing domain, also known as C-terminal effector domain
CC (CED), can act in autonomous repression, including both translational
CC inhibition and mRNA degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GW182 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK047249; BAC33005.1; -; mRNA.
DR EMBL; AK134064; BAE21997.1; -; mRNA.
DR EMBL; AK147471; BAE27937.1; ALT_INIT; mRNA.
DR EMBL; AK122529; BAC65811.1; -; mRNA.
DR RefSeq; NP_932139.2; NM_198022.2.
DR AlphaFoldDB; Q3UHC0; -.
DR SMR; Q3UHC0; -.
DR BioGRID; 229897; 3.
DR IntAct; Q3UHC0; 1.
DR STRING; 10090.ENSMUSP00000101951; -.
DR iPTMnet; Q3UHC0; -.
DR PhosphoSitePlus; Q3UHC0; -.
DR EPD; Q3UHC0; -.
DR MaxQB; Q3UHC0; -.
DR PaxDb; Q3UHC0; -.
DR PRIDE; Q3UHC0; -.
DR ProteomicsDB; 259483; -.
DR GeneID; 217351; -.
DR KEGG; mmu:217351; -.
DR CTD; 57690; -.
DR MGI; MGI:2443265; Tnrc6c.
DR eggNOG; ENOG502QWFQ; Eukaryota.
DR InParanoid; Q3UHC0; -.
DR OrthoDB; 50428at2759; -.
DR Reactome; R-MMU-426496; Post-transcriptional silencing by small RNAs.
DR BioGRID-ORCS; 217351; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Tnrc6c; mouse.
DR PRO; PR:Q3UHC0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UHC0; protein.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0001706; P:endoderm formation; IMP:MGI.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IEA:InterPro.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IMP:MGI.
DR CDD; cd12713; RRM_TNRC6C; 1.
DR CDD; cd14283; UBA_TNR6C; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019486; Argonaute_hook_dom.
DR InterPro; IPR026805; GW182_M_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR041917; TNR6C_UBA.
DR InterPro; IPR032226; TNRC6_PABC-bd.
DR InterPro; IPR033499; TNRC6C.
DR InterPro; IPR034927; TNRC6C_RRM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR13020:SF9; PTHR13020:SF9; 2.
DR Pfam; PF10427; Ago_hook; 1.
DR Pfam; PF12938; M_domain; 1.
DR Pfam; PF16608; TNRC6-PABC_bdg; 2.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..1690
FT /note="Trinucleotide repeat-containing gene 6C protein"
FT /id="PRO_0000278527"
FT DOMAIN 928..973
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1565..1632
FT /note="RRM"
FT REGION 1..921
FT /note="Sufficient for interaction with argonaute family
FT proteins"
FT /evidence="ECO:0000250"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1690
FT /note="Silencing domain; interaction with CNOT1 and PAN3"
FT /evidence="ECO:0000250"
FT REGION 1351..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1690
FT /note="Sufficient for translational repression when
FT tethered to a target mRNA"
FT /evidence="ECO:0000250"
FT REGION 1371..1417
FT /note="Required for interaction with PABPC1"
FT /evidence="ECO:0000250"
FT REGION 1381..1399
FT /note="PABPC1-interacting motif-2 (PAM2)"
FT /evidence="ECO:0000250"
FT REGION 1397..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1690
FT /note="Interaction with the CCR4-NOT complex"
FT /evidence="ECO:0000250"
FT REGION 1600..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1156..1214
FT /evidence="ECO:0000255"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCJ0"
FT MOD_RES 776
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCJ0"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCJ0"
FT CONFLICT 1521
FT /note="L -> P (in Ref. 1; BAE21997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1690 AA; 175775 MW; 4788764371891904 CRC64;
MATGSAQSSF PSHLKKTNGS HGTNGALVQS PSNQSALGAG GTNGNGGVAR VWGVATSSSS
GLAHCSVGGG DGKMDNMIGD GRSQNCWGAS NSNAGINLNL NPNANPAAWP VLGHEGTVAT
GNPSSICSPV SAIGQNMGSQ NGNPVGALGA WGNLLPQESA EPQTSTSQNV SFSVQPQNLN
TDGPNNTNPM NSSPNPINAM QTNGLPNWGM AVGMGAIIPP HLQGLPGANG SSVSQGSGSG
GEGMGSSVWG LSPGNPATGS TNCGFSQGNG DTVNSALSAK QNGSSSAVQK EGNGGNAWDS
GPPAGPGILA WGRGSGTNGI GNIHSGAWGH PSRSSSNGVN GEWGKPPNQH SSSDISGKGS
TGWDSASAAS QTPALQPGSE HMNSWAKATS SGTTASEGSS DGSGNHNEGS TGREGTGEGR
RRDKGVLDQG HIQLPRNDLD PRVLSNSGWG QTPVKQNTAW EFEESPRSER KNDNGTEAWG
SIATQPSNSG GKTDGSIMNS TNTSSVSGWV SSPPAAVPAN TSWGDSNNKA PSGPGVWGDS
ISSTAVNNAA ATKSGHAWSG TVNQEDKSPT WGEPQKPKSQ NWGDGQRANP AWSTGAGDWA
DSSSVLGHLG DGKKNGSGWD ADGNRSGSGW NDATRCGTSG WGSGTNAKVN PGTNWGESLK
PGPQQNWAHK PQDNNVSNWG GAASVKQTGT GWIGGPLPVK QKDSSEATGW EEPSPPSIRR
KMEIDDGTSA WGDPSTYNNK TVNMWDRNNP VIQSSTTAPA TPTTPTSSST THRAETPPSH
QAGTQLNRSP LLGPVSSGWG EMPSVHSKAE NSWGEPSSPC TLVDNGTAAW GKPPSSGSGW
DHPAEPVVPF GRASAPAAAP ALCKPASKSM QEGWGSGADE MNLGTSQWED EDGDMWNNAA
SQESSSSCSS WGNTSKKGLQ KGMKTPGKQD EAWIMSRLIK QLTDMGFPRE PAEEALKSNS
MNLDQAMSAL LEKKVDMDKR GLGMTDYNGM VTKPLGCRPP ISKESSMDRP TFLDKLTLSF
SNQDGGLVEE PTTSPFLPSP SLKLPLSNSA LPSQALGGVA SGLGMQNLNS SRQIPSGNLG
VFGNSGAAQA RTMQQPPVQP LNSSQPSLRA QVPQFLSPQV QAQLLQFAAK NIGLSPALLT
SPINPQHMTM LNQLYQLQLA YQRLQIQQQM LQAQRNVSGP MRQQEQQVAR TITNLQQQIQ
QHQRQLAQAL LVKQPPPPPP PPHLSLHPSA GKSGMESFPP PPQAPGLPDL QTKEQQSSPN
TFAPYPLAGL NPNMNVNSID MSSGLSVKDP SQSQSRLPQW THPNSMGNLS SAASPLDQNP
SKHGAIPGGL SIGPPGKSSI DDSYGRYDLI QNSESPASPP VAVPHSWSRA KSDSDKISNG
SSISWPPEFH PGVPWKGLQN IDPENDPDVT PGSVPTGPTI NTTIQDVNRY LLKSGGKLSD
IKSTWSSGPA SHTQASLSHE LWKVPRNTTA PTRPPPGLAN PKPSSTWGTS PLGWTSSYSS
GSAWSTDTSG RTSSWLVLRN LTPQIDGSTL RTLCLQHGPL ITFHLNLTQG NAVVRYSSKE
EAAKAQKSLH MCVLGNTTIL AEFAGEEEVN RFLAQGQALP PTSSWQSSSG GSQPRLGTSG
STHGLVRSDT AHWNTPCLSG KGSSELLWGG VPQYSSSLWG PPSAEDARVI GSPTPLNTLL
PGDLLSGESI
