RPB3_BOVIN
ID RPB3_BOVIN Reviewed; 275 AA.
AC Q3T0Q3; A7E3Q9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB3 {ECO:0000305};
DE Short=RNA polymerase II subunit 3;
DE Short=RNA polymerase II subunit B3;
DE AltName: Full=DNA-directed RNA polymerase II subunit C;
GN Name=POLR2C {ECO:0000250|UniProtKB:P19387};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB3 is part of the
CC core element with the central large cleft and the clamp element that
CC moves to open and close the cleft (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB11/POLR2J and RPB3/POLR2C subunits interact with
CC each other (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; BT030680; ABS44996.1; -; mRNA.
DR EMBL; BC102301; AAI02302.1; -; mRNA.
DR RefSeq; NP_001029384.1; NM_001034212.2.
DR PDB; 5FLM; EM; 3.40 A; C=1-275.
DR PDB; 5OIK; EM; 3.70 A; C=1-275.
DR PDBsum; 5FLM; -.
DR PDBsum; 5OIK; -.
DR AlphaFoldDB; Q3T0Q3; -.
DR SMR; Q3T0Q3; -.
DR DIP; DIP-61186N; -.
DR IntAct; Q3T0Q3; 2.
DR STRING; 9913.ENSBTAP00000002420; -.
DR PaxDb; Q3T0Q3; -.
DR PRIDE; Q3T0Q3; -.
DR Ensembl; ENSBTAT00000002420; ENSBTAP00000002420; ENSBTAG00000001856.
DR GeneID; 504452; -.
DR KEGG; bta:504452; -.
DR CTD; 5432; -.
DR VEuPathDB; HostDB:ENSBTAG00000001856; -.
DR VGNC; VGNC:33137; POLR2C.
DR eggNOG; KOG1522; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR HOGENOM; CLU_038421_1_0_1; -.
DR InParanoid; Q3T0Q3; -.
DR OMA; PENIVMM; -.
DR OrthoDB; 834009at2759; -.
DR TreeFam; TF103038; -.
DR Reactome; R-BTA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-BTA-674695; RNA Polymerase II Pre-transcription Events.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000001856; Expressed in adenohypophysis and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..275
FT /note="DNA-directed RNA polymerase II subunit RPB3"
FT /id="PRO_0000290351"
FT REGION 203..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19387"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19387"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 76..81
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 241..270
FT /evidence="ECO:0007829|PDB:5FLM"
SQ SEQUENCE 275 AA; 31429 MW; FAB3E2F670E1B352 CRC64;
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH
DEFIAHRLGL IPLTSDDIVD KLQYSRDCTC EEFCPECSVE FTLDVRCNED QTRHVTSRDL
ISNSPRVIPV TSRNRDNDPN DYVEQDDILI VKLRKGQELR LRAYAKKGFG KEHAKWNPTA
GVAFEYDPDN ALRHTVYPKP EEWPKSEYSE LDEDESQAPY DPNGKPERFY YNVESCGSLR
PETIVLSALS GLKKKLSDLQ TQLSHEIQSD VLTIN