位置:首页 > 蛋白库 > RPC4_BOVIN
RPC4_BOVIN
ID   RPC4_BOVIN              Reviewed;         398 AA.
AC   Q5E9Z7; Q17QS2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC4;
DE            Short=RNA polymerase III subunit C4;
DE   AltName: Full=DNA-directed RNA polymerase III subunit D;
GN   Name=POLR3D;
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=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) 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       Specific peripheric component of RNA polymerase III which synthesizes
CC       small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and
CC       limiting infection by intracellular bacteria and DNA viruses. Acts as
CC       nuclear and cytosolic DNA sensor involved in innate immune response.
CC       Can sense non-self dsDNA that serves as template for transcription into
CC       dsRNA. The non-self RNA polymerase III transcripts induce type I
CC       interferon and NF- Kappa-B through the RIG-I pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. Interacts with RPC5 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPC4/POLR3D RNA polymerase
CC       subunit family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT020772; AAX08789.1; -; mRNA.
DR   EMBL; BC118212; AAI18213.1; -; mRNA.
DR   RefSeq; XP_005210298.1; XM_005210241.3.
DR   RefSeq; XP_005210299.1; XM_005210242.3.
DR   AlphaFoldDB; Q5E9Z7; -.
DR   STRING; 9913.ENSBTAP00000013251; -.
DR   PaxDb; Q5E9Z7; -.
DR   PRIDE; Q5E9Z7; -.
DR   GeneID; 508049; -.
DR   CTD; 661; -.
DR   eggNOG; KOG3122; Eukaryota.
DR   InParanoid; Q5E9Z7; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045089; P:positive regulation of 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:InterPro.
DR   InterPro; IPR007811; RPC4.
DR   PANTHER; PTHR13408; PTHR13408; 1.
DR   Pfam; PF05132; RNA_pol_Rpc4; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Antiviral defense; DNA-directed RNA polymerase; Immunity;
KW   Innate immunity; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CHAIN           2..398
FT                   /note="DNA-directed RNA polymerase III subunit RPC4"
FT                   /id="PRO_0000239118"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   MOD_RES         95
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   MOD_RES         97
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   MOD_RES         99
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        78
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        152
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        160
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        199
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        206
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
FT   CROSSLNK        302
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05423"
SQ   SEQUENCE   398 AA;  44549 MW;  0D757880454CA4CD CRC64;
     MSEGNAAGEP SAPGGPRPLL SGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP
     NIISRKIKEE PKEEVTVKKE KRERDRDRQR DSHGRGRGRP EVIQSHSIFE QGPAEMMKKK
     GNWDKTVDMS DVGPSHIINI KKEKRETDEE TKQILRMLEK DDFIDDPGLR NDIRNMPVQL
     PLAHSGWLFK EENEETDVKP RLAGPKEEDM EVDMPAVKVK EEPRDEDEEA KMKAPLRAAR
     KIPGLPKDVS VAELLRELSL TQEEELLFLQ LPDSLPGQPP TQDIKPIKTE VQSEDGQMVV
     IKQEKDREAR LAENTCTLAD LTEGQVGKLL IRKSGKVQLL LGKVTLDVTM GTTCSFLQEL
     VSVGLGDSRT GDMTVLGHIK HKLVCSPNFE SLLDHRHR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024