ID RPC1_BOVIN Reviewed; 1390 AA.
AC A4IF62;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC1;
DE Short=RNA polymerase III subunit C1;
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:O14802};
DE AltName: Full=DNA-directed RNA polymerase III subunit A;
GN Name=POLR3A {ECO:0000250|UniProtKB:O14802};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic core component of RNA polymerase III (Pol III), a
CC DNA-dependent RNA polymerase which synthesizes small non-coding RNAs
CC using the four ribonucleoside triphosphates as substrates. Synthesizes
CC 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic
CC loci (By similarity). Pol III-mediated transcription cycle proceeds
CC through transcription initiation, transcription elongation and
CC transcription termination stages. During transcription initiation, Pol
CC III is recruited to DNA promoters type I, II or III with the help of
CC general transcription factors and other specific initiation factors.
CC Once the polymerase has escaped from the promoter it enters the
CC elongation phase during which RNA is actively polymerized, based on
CC complementarity with the template DNA strand. Transcription termination
CC involves the release of the RNA transcript and polymerase from the DNA
CC (By similarity). Forms Pol III active center together with the second
CC largest subunit POLR3B/RPC2. Appends one nucleotide at a time to the 3'
CC end of the nascent RNA, with POLR3A/RPC1 contributing a Mg(2+)-
CC coordinating DxDGD motif, and POLR3B/RPC2 participating in the
CC coordination of a second Mg(2+) ion and providing lysine residues
CC believed to facilitate Watson-Crick base pairing between the incoming
CC nucleotide and template base. Typically, Mg(2+) ions direct a 5'
CC nucleoside triphosphate to form a phosphodiester bond with the 3'
CC hydroxyl of the preceding nucleotide of the nascent RNA, with the
CC elimination of pyrophosphate (By similarity). Pol III plays a key role
CC in sensing and limiting infection by intracellular bacteria and DNA
CC viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate
CC immune response. Can sense non-self dsDNA that serves as template for
CC transcription into dsRNA. The non-self RNA polymerase III transcripts,
CC such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I
CC interferon and NF-kappa-B through the RIG-I pathway (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O14802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:O14802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:O14802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O14802};
CC Note=Two Mg(2+) ions are coordinated by both the catalytic residues and
CC the nucleic acid substrate to enhance substrate recognition and
CC catalytic efficiency. {ECO:0000250|UniProtKB:O14802,
CC ECO:0000250|UniProtKB:P24928};
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits: a ten-subunit catalytic core composed of
CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10,
CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and
CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and
CC CRCP/RPC9, protruding from the core and functioning primarily in
CC transcription initiation; and additional subunits homologous to general
CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3-
CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription
CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both
CC transcription initiation and termination (By similarity). As part of
CC the RNA polymerase III complex, interacts with PKP2 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O14802}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14802}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:O14802}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; BC134422; AAI34423.1; -; mRNA.
DR RefSeq; NP_001077219.1; NM_001083750.1.
DR AlphaFoldDB; A4IF62; -.
DR SMR; A4IF62; -.
DR STRING; 9913.ENSBTAP00000017638; -.
DR PaxDb; 9913-ENSBTAP00000017638; -.
DR Ensembl; ENSBTAT00000017638.6; ENSBTAP00000017638.5; ENSBTAG00000013259.6.
DR GeneID; 540308; -.
DR KEGG; bta:540308; -.
DR CTD; 11128; -.
DR VEuPathDB; HostDB:ENSBTAG00000013259; -.
DR VGNC; VGNC:33145; POLR3A.
DR eggNOG; KOG0261; Eukaryota.
DR GeneTree; ENSGT00930000151028; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; A4IF62; -.
DR TreeFam; TF103054; -.
DR Reactome; R-BTA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-BTA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-BTA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000013259; Expressed in spermatocyte and 108 other cell types or tissues.
DR ExpressionAtlas; A4IF62; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IEA:GOC.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antiviral defense; Cytoplasm; DNA-directed RNA polymerase;
KW Immunity; Innate immunity; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1390
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000330752"
FT REGION 844..856
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 144
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="nontemplate strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 167
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="nontemplate strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 326
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 348
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 353
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 360
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 366
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 464
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with POLR3B/RPC2"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with POLR3B/RPC2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 503
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 1159
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="nontemplate strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 1305
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT BINDING 1323
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_label="template strand"
FT /evidence="ECO:0000250|UniProtKB:O14802"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14802"
SQ SEQUENCE 1390 AA; 155791 MW; ECF9B3A1FA466284 CRC64;
MVKEQFRETD VAKKISHICF GMKSAEEMRQ QAHIQVVSKN LYSQDNNHSP LLYGVLDHRM
GTSEKDRPCE TCGKNLADCL GHYGYIDLEL PCFHVGYFRA VIGILQMICK TCCHIMLSQE
EKKQFLDYLK RPGLTYLQKR GLKKKISDKC RKKNTCHHCG AFNGTVKKCG LLKIIHEKYK
TNKKVVDPIV SSFLQSFETA IEHNKEVEPL LGKAQENLNP LVVLNLFKRI PAEDIPLLLM
NPEAGKPSDL ILTRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRISG
AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG RFRGNLSGKR
VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TFPEKVNKAN INFLRKLVRN GPEVHPGANF
IQQRHTQMKR FLKYGNREKM AQELKFGDIV ERHLIDGDVV LFNRQPSLHK LSIMAHLARV
KPHRTFRFNE CVCTPYNADF DGDEMNLHLP QTEEAKAEAL VLMGTKANLV TPRNGEPLIA
AIQDFLTGAY LLTLKDTFFD RAKACQIIAS ILVGKDEKIK VRLPPPTILK PVTLWTGKQI
FSVILRPSDD NPVRANLRTK GKQYCGRGED LCVNDSYVTI QNSELMSGSM DKGTLGSGSK
NNIFYILLRD WGQNEAADAM SRLARLAPVY LSNRGFSIGI GDVTPGQGLL KAKYELLNAG
YKKCDEYIEA LNTGKLQQQP GCTAEETLEA LILKELSVIR DHAGSACLRE LDKSNSPLTM
ALCGSKGSFI NISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVANSFYS
GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF
IYGGDGLDPA AMEGKDEPLE FKRVLDNIKA VFPCRSEPAL SKNELLLSAE SIMKKNEFLC
CQDSFLQEIK KFIKEVSEKI KKTRDKYGIN DNGTTEPRVL YQLDRITPTQ IEKFLETCRD
KYMRAQMEPG SAVGALCAQS IGEPGTQMTL KTFHFAGVAS MNITLGVPRI KEIINASKAI
STPIITAQLD KDDDADYARL VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL
RLEVNAETVR YSICMSKLRV KPGDVAVHGE AVVCVTPREN SKSSMYYVLQ FLKEDLPKVV
VQGIPEVSRA VIHIDEQSGK EKYKLLVEGD NLRAVMATHG VKGTRTTSNN TYEVEKTLGI
EAARTTIINE IQYTMVNHGM SIDRRHVMLL SDLMTYKGEV LGITRFGLAK MKESVLMLAS
FEKTADHLFD AAYFGQKDSV CGVSECIIMG IPMNIGTGLF KLLHKANRDP SPPRRPLIFD
TNEFHIPLVT
//
