TF3C1_RAT
ID TF3C1_RAT Reviewed; 2148 AA.
AC Q63505;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=General transcription factor 3C polypeptide 1;
DE AltName: Full=TF3C-alpha;
DE AltName: Full=TFIIIC box B-binding subunit;
DE AltName: Full=Transcription factor IIIC 220 kDa subunit;
DE Short=TFIIIC 220 kDa subunit;
DE Short=TFIIIC220;
DE AltName: Full=Transcription factor IIIC subunit alpha;
GN Name=Gtf3c1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 151-172; 360-385;
RP 686-713 AND 1338-1354.
RC TISSUE=Hepatocyte;
RX PubMed=8164661; DOI=10.1128/mcb.14.5.3053-3064.1994;
RA Lagna G., Kovelman R., Sukegawa J., Roeder R.G.;
RT "Cloning and characterization of an evolutionarily divergent DNA-binding
RT subunit of mammalian TFIIIC.";
RL Mol. Cell. Biol. 14:3053-3064(1994).
CC -!- FUNCTION: Required for RNA polymerase III-mediated transcription.
CC Component of TFIIIC that initiates transcription complex assembly on
CC tRNA and is required for transcription of 5S rRNA and other stable
CC nuclear and cytoplasmic RNAs. Binds to the box B promoter element (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC with IGHMBP2. Interacts with MAF1. {ECO:0000250|UniProtKB:Q12789}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 1 family. {ECO:0000305}.
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DR EMBL; L28801; AAA42032.1; -; mRNA.
DR PIR; A56011; A56011.
DR AlphaFoldDB; Q63505; -.
DR BioGRID; 251080; 1.
DR STRING; 10116.ENSRNOP00000022271; -.
DR iPTMnet; Q63505; -.
DR PhosphoSitePlus; Q63505; -.
DR PaxDb; Q63505; -.
DR PRIDE; Q63505; -.
DR UCSC; RGD:621048; rat.
DR RGD; 621048; Gtf3c1.
DR eggNOG; KOG4560; Eukaryota.
DR InParanoid; Q63505; -.
DR PhylomeDB; Q63505; -.
DR Reactome; R-RNO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-RNO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:Q63505; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISO:RGD.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IBA:GO_Central.
DR CDD; cd16169; Tau138_eWH; 1.
DR InterPro; IPR044210; Tfc3-like.
DR InterPro; IPR035625; Tfc3_eWH.
DR InterPro; IPR007309; TFIIIC_Bblock-bd.
DR PANTHER; PTHR15180; PTHR15180; 1.
DR Pfam; PF04182; B-block_TFIIIC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription; Ubl conjugation.
FT CHAIN 1..2148
FT /note="General transcription factor 3C polypeptide 1"
FT /id="PRO_0000209712"
FT REGION 473..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1823..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2127..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1231
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT MOD_RES 1195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K284"
FT MOD_RES 1624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT MOD_RES 1853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT MOD_RES 1893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K284"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT CROSSLNK 769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
FT CROSSLNK 832
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12789"
SQ SEQUENCE 2148 AA; 242306 MW; 886849CDC7A47822 CRC64;
MDALESLLDE VALEGLDGLC LPALWSRLES RSPAFPLPLE PYTQEFLWRA LVTHPGISFY
EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVTLEDVYPI HMILENKDGI QGSCRYFKER
KDITSSIRSK CLQPRCTMVE AFSRWGKKLI IVASQDMRYR ALIGLEGDPD LKLPDFSYCI
LERLGRSRWQ GELQRDLHTT AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI
LLLLNRFHVD RRSKYDILME KLSMMLSTRS NQIETLGKLR EELGLCERTF KRLYQYMLNA
GLAKVVSLPL QEIHPECGPC KTKKGTDVMV RCLKLLKEFR RKMEDDHDDD DDEEAISKAV
PPVDIVFERD MLTQTYELIE RRGTKGISQA EIRVAMNVGK LEARMLCRLL QRFKVVKGFM
EDEGRQRTTK YISCVFAEES DLSRQYAREK ARGELLTTVS LASVQDESLM PEGEEAFLSD
SESEEESSCS GKRRGRGSRG HSRASGDAGP GSRPHHSTPA KGGWKVLNLH PLKKPKSAAV
ERSRRSSACR DGLDTSSSSE LNIPFDPHSM DSHSGDIAVI EEVRLDNPKE GGGSQKGGRH
GSGQDKPHKT YRLLKRRNLI IEAVTNLRLI ESLFTIQKMI MDQEKQEGVS TKCCKKSIIR
LVRNLSEEGL LRLYRTTVIQ DGIKKKVDLV VHPSMDQNDP LVRSAIEQVR FRISNSSTAN
RVKVPPAPAP QEEAEEGNQE PEVPSRSADS EANTSSKPES TRVKKTDEKM GITPLKNYKP
VIVPGLGRSI GFLPKMPRLR VMHLFLWYLV YGHPASHTGE QPTFHSERKT GKQEPSRPGV
QPSSGDDWDS SEAKNSTESS SWEAEMELST ERVYVDEISW MRYVPPIPIH RDFGFGWALV
SDILLCLPLS IFVQVVQVSY KVDNLEDFLN DPLKKHTLIR FLPRHIRQQL LYKRRYIFSV
VENLQRLCYM GLLQFGPTEK FQDKDQVFVF LKKNAVIVDT TICDPHYNLA HSSRPFERRL
YVLDSMQDVE SYWFDLQCIC LNTPLGVVRC PCAQKICPDP GSDPEGSLRK EQESAMDKHN
LERKCAMLEY TTGSREVVDE GLVPGDGLGA AGLDSSFYAH LKRNWVWTSY IINKARKNNT
SENGLTGRLQ TFLSKRPMPL GSGGSGRLPL WSEGKADAEL CADKEEHFEL DREPTPGRNR
KVRGGKSQKR KRLKKEPIRK TKRRRRGEHP EAKSKKLRYQ DEADQNALRM MTRLRVSWSM
QEDGLLMLCR IASNVLNTKV KGPFVTWQVV RDILHATFEE SLDKTSHSVG RRARYIVKNP
QAFMNYKVCL AEVYQDKALV GDFMSRKDNY EDPKVCAKEF KEFVEKLKEK FSSGLRNPNL
EIPDTLQELF AKYRVLAIGD EKDRVRKEDE LNSVEDIHFL VLQNLIQSTL SLSNSQSNSC
QSFQIFRLYR EFREPVLVRA FMECQKRSLV NRRRVSHSQG PKKNRAVPFV PMSYQLSQSY
YKLFTWRFPT TVCTESFQFY DRLRANGILD QPDHFSFKDM DSNDPSSDLV AFSLDSPGGH
CVTALALFSL GLLSVDVRIP EQIVVVDSSM VESEVMKSLG KDGGLDDDDE EEDLDEGSGT
KRQSVEVKAH QASHTKYLLM RGYYTVPGMV STRNLNPNDS IVVNSCQVKF RLRNTPAPTH
LGPTGPTATP LEELQAGPSC LPASFTSLVD PQLHTRCPEE FAHQMAQSGY SPEDVAASLE
ILQAVAAADC FGVDREKLSR QFSALEKIAD KRTRTFLDYI QDLLEQQQVM EVGGNTVRLV
AMASAQPWLL PSVRLKDVEI DTKASGDDSQ SRLPAGSSIE DHTSEGAPIP PVSSNGTKKR
PYCSIQSPET DAEEATRLPA KKPTLQDVCV AASPRPGTEE QTEAQAQFAA PEDAGAEGPR
QESQESVGVS GLEQLGCEFQ LPENSEDPRG LTESNMAQVA WESGCERVCF VGRPWRGVDG
RLNMPVCKGM MEAVLYHIMS RPGVPESCLL QYYQGVLQPV AVLELLRGLE SLGCIQKRML
KKPASVSLFS RPVVEGLGQA SEAEALSCQG STVTFYEPTL DCTIRLGRVF PHDINWKQSG
SIYRCVPGQQ RSLCPCLIVP PGLSQEPRPS HSCYQSSAQP STGVATSR
