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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
 
 
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