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RPC7_MOUSE
ID   RPC7_MOUSE              Reviewed;         223 AA.
AC   Q6NXY9; Q8K0W5; Q9CV05;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC7;
DE            Short=RNA polymerase III subunit C7;
DE   AltName: Full=DNA-directed RNA polymerase III subunit G;
GN   Name=Polr3g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-113 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=21898682; DOI=10.1002/stem.714;
RA   Wong R.C., Pollan S., Fong H., Ibrahim A., Smith E.L., Ho M., Laslett A.L.,
RA   Donovan P.J.;
RT   "A novel role for an RNA polymerase III subunit POLR3G in regulating
RT   pluripotency in human embryonic stem cells.";
RL   Stem Cells 29:1517-1527(2011).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=24107381; DOI=10.1101/gr.161570.113;
RA   Renaud M., Praz V., Vieu E., Florens L., Washburn M.P., l'Hote P.,
RA   Hernandez N.;
RT   "Gene duplication and neofunctionalization: POLR3G and POLR3GL.";
RL   Genome Res. 24:37-51(2014).
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. May direct with other members of
CC       the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G subcomplex RNA Pol III binding
CC       to the TFIIIB-DNA complex via the interactions between TFIIIB and
CC       POLR3F. May be involved either in the recruitment and stabilization of
CC       the subcomplex within RNA polymerase III, or in stimulating catalytic
CC       functions of other subunits during initiation. Plays a key role in
CC       sensing and limiting infection by intracellular bacteria and DNA
CC       viruses. Acts as 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       induce type I interferon and NF- Kappa-B through the RIG-I pathway.
CC       {ECO:0000250|UniProtKB:O15318}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G
CC       form a Pol III subcomplex. Directly interacts with POLR3C/RPC62. Also
CC       found a trimeric complex with POLR3C and POLR3GL.
CC       {ECO:0000250|UniProtKB:O15318}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21898682}. Cytoplasm
CC       {ECO:0000269|PubMed:21898682}. Note=In zygotes and the 2-cell stage
CC       embryos, mainly in the cytoplasm. Starts to localize to the nucleus in
CC       the 8-16 cell stage embryo and early blastocysts.
CC       {ECO:0000269|PubMed:21898682}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NXY9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NXY9-2; Sequence=VSP_012672, VSP_012673;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in the liver.
CC       {ECO:0000269|PubMed:24107381}.
CC   -!- DEVELOPMENTAL STAGE: Not detectable in unfertilized oocytes. First
CC       detected in zygotes and the 2-cell stage embryos. Expressed until at
CC       least the early blastocyst stage. {ECO:0000269|PubMed:21898682}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit
CC       family. {ECO:0000305}.
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DR   EMBL; BC030063; AAH30063.1; -; mRNA.
DR   EMBL; BC066818; AAH66818.1; -; mRNA.
DR   EMBL; AK010126; BAB26717.3; -; mRNA.
DR   CCDS; CCDS36738.1; -. [Q6NXY9-1]
DR   RefSeq; NP_001074645.1; NM_001081176.1. [Q6NXY9-1]
DR   AlphaFoldDB; Q6NXY9; -.
DR   STRING; 10090.ENSMUSP00000035289; -.
DR   iPTMnet; Q6NXY9; -.
DR   PhosphoSitePlus; Q6NXY9; -.
DR   EPD; Q6NXY9; -.
DR   MaxQB; Q6NXY9; -.
DR   PaxDb; Q6NXY9; -.
DR   PeptideAtlas; Q6NXY9; -.
DR   PRIDE; Q6NXY9; -.
DR   ProteomicsDB; 299869; -. [Q6NXY9-1]
DR   ProteomicsDB; 299870; -. [Q6NXY9-2]
DR   Ensembl; ENSMUST00000048993; ENSMUSP00000035289; ENSMUSG00000035834. [Q6NXY9-1]
DR   Ensembl; ENSMUST00000161920; ENSMUSP00000125054; ENSMUSG00000035834. [Q6NXY9-2]
DR   GeneID; 67486; -.
DR   KEGG; mmu:67486; -.
DR   UCSC; uc007rhx.1; mouse. [Q6NXY9-1]
DR   UCSC; uc007rhz.1; mouse. [Q6NXY9-2]
DR   CTD; 10622; -.
DR   MGI; MGI:1914736; Polr3g.
DR   VEuPathDB; HostDB:ENSMUSG00000035834; -.
DR   eggNOG; ENOG502RY1A; Eukaryota.
DR   GeneTree; ENSGT00990000204076; -.
DR   HOGENOM; CLU_084309_0_0_1; -.
DR   InParanoid; Q6NXY9; -.
DR   OMA; HKDWREK; -.
DR   OrthoDB; 1403784at2759; -.
DR   PhylomeDB; Q6NXY9; -.
DR   TreeFam; TF103052; -.
DR   Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR   BioGRID-ORCS; 67486; 6 hits in 76 CRISPR screens.
DR   ChiTaRS; Polr3g; mouse.
DR   PRO; PR:Q6NXY9; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q6NXY9; protein.
DR   Bgee; ENSMUSG00000035834; Expressed in lumbar dorsal root ganglion and 162 other tissues.
DR   Genevisible; Q6NXY9; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEP:MGI.
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; ISS:UniProtKB.
DR   InterPro; IPR024661; RNA_pol_III_Rpc31.
DR   PANTHER; PTHR15367; PTHR15367; 1.
DR   Pfam; PF11705; RNA_pol_3_Rpc31; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Antiviral defense; Cytoplasm; Immunity;
KW   Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription.
FT   CHAIN           1..223
FT                   /note="DNA-directed RNA polymerase III subunit RPC7"
FT                   /id="PRO_0000073979"
FT   REGION          111..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..202
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..223
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         134
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O15318"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15318"
FT   VAR_SEQ         83..160
FT                   /note="DDIERYSKRYMKVYKEEWVPDWRRLPREMMPRKKCKKGDPKSKPSKAAAKAT
FT                   SLINSADVLKTIEELEKRGEGERSDE -> GTHARQALPEAGSSVFTEGAVDAGTCDHV
FT                   TQPITQLEKTLLTRIVRKEKHLYFIVLFFFFFFLQLTHNTLCLPFVIQY (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012672"
FT   VAR_SEQ         161..223
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012673"
SQ   SEQUENCE   223 AA;  25947 MW;  AFC5A5305ABEF9F0 CRC64;
     MAGNKGRGRA AYTFNIEAVG FSRGEKLPDV VLKPPPLFPD TDYKPVPLKT GEDEDYMLAL
     KQELRETVKR LPYFIEPPEE KQDDIERYSK RYMKVYKEEW VPDWRRLPRE MMPRKKCKKG
     DPKSKPSKAA AKATSLINSA DVLKTIEELE KRGEGERSDE ENEEKEGSKE KDKDDEEDGE
     EDAEQEDYDE EEQEEENDYI NSYFDNGDDF GVDSDDNMDE ATY
 
 
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