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RPC5_MOUSE
ID   RPC5_MOUSE              Reviewed;         710 AA.
AC   Q9CZT4; Q8CI35; Q9DBD1;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC5;
DE            Short=RNA polymerase III subunit 5;
DE            Short=RNA polymerase III subunit C5;
DE   AltName: Full=Sex-lethal interactor homolog;
DE            Short=Sxl interactor;
GN   Name=Polr3e; Synonyms=Sin;
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=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-162 AND SER-503, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Specific periphjeric component of RNA polymerase III which synthesizes
CC       small RNAs, such as 5S rRNA and tRNAs. Essential for efficient
CC       transcription from both the type 2 VAI and type 3 U6 RNA polymerase III
CC       promoters. Plays a key role in sensing and limiting infection by
CC       intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic
CC       DNA sensor involved in innate immune response. Can sense non-self dsDNA
CC       that serves as template for transcription into dsRNA. The non-self RNA
CC       polymerase III transcripts induce type I interferon and NF- Kappa-B
CC       through the RIG-I pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. Interacts with RPC4 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CZT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZT4-2; Sequence=VSP_007066;
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DR   EMBL; AK005034; BAB23761.1; -; mRNA.
DR   EMBL; AK012184; BAB28084.1; -; mRNA.
DR   EMBL; BC037637; AAH37637.1; -; mRNA.
DR   CCDS; CCDS21797.1; -. [Q9CZT4-1]
DR   CCDS; CCDS52383.1; -. [Q9CZT4-2]
DR   RefSeq; NP_001157568.1; NM_001164096.1. [Q9CZT4-2]
DR   RefSeq; NP_079574.2; NM_025298.3. [Q9CZT4-1]
DR   AlphaFoldDB; Q9CZT4; -.
DR   SMR; Q9CZT4; -.
DR   BioGRID; 205075; 2.
DR   IntAct; Q9CZT4; 2.
DR   STRING; 10090.ENSMUSP00000033173; -.
DR   iPTMnet; Q9CZT4; -.
DR   PhosphoSitePlus; Q9CZT4; -.
DR   EPD; Q9CZT4; -.
DR   MaxQB; Q9CZT4; -.
DR   PaxDb; Q9CZT4; -.
DR   PRIDE; Q9CZT4; -.
DR   ProteomicsDB; 299866; -. [Q9CZT4-1]
DR   ProteomicsDB; 299867; -. [Q9CZT4-2]
DR   Antibodypedia; 25851; 134 antibodies from 23 providers.
DR   DNASU; 26939; -.
DR   Ensembl; ENSMUST00000033173; ENSMUSP00000033173; ENSMUSG00000030880. [Q9CZT4-1]
DR   Ensembl; ENSMUST00000106483; ENSMUSP00000102092; ENSMUSG00000030880. [Q9CZT4-1]
DR   Ensembl; ENSMUST00000207481; ENSMUSP00000146970; ENSMUSG00000030880. [Q9CZT4-2]
DR   GeneID; 26939; -.
DR   KEGG; mmu:26939; -.
DR   UCSC; uc009jnf.2; mouse. [Q9CZT4-1]
DR   UCSC; uc009jnh.2; mouse. [Q9CZT4-2]
DR   CTD; 55718; -.
DR   MGI; MGI:1349452; Polr3e.
DR   VEuPathDB; HostDB:ENSMUSG00000030880; -.
DR   eggNOG; KOG2354; Eukaryota.
DR   GeneTree; ENSGT00390000016123; -.
DR   HOGENOM; CLU_021012_1_0_1; -.
DR   InParanoid; Q9CZT4; -.
DR   OMA; MDTSACD; -.
DR   OrthoDB; 1110776at2759; -.
DR   PhylomeDB; Q9CZT4; -.
DR   TreeFam; TF103050; -.
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; 26939; 24 hits in 74 CRISPR screens.
DR   ChiTaRS; Polr3e; mouse.
DR   PRO; PR:Q9CZT4; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9CZT4; protein.
DR   Bgee; ENSMUSG00000030880; Expressed in right kidney and 260 other tissues.
DR   Genevisible; Q9CZT4; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR006886; RNA_pol_III_Rpc5.
DR   InterPro; IPR045576; RPC5_C.
DR   PANTHER; PTHR12069; PTHR12069; 1.
DR   Pfam; PF04801; RPC5; 1.
DR   Pfam; PF19725; RPC5_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiviral defense; DNA-directed RNA polymerase;
KW   Immunity; Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Ubl conjugation.
FT   CHAIN           1..710
FT                   /note="DNA-directed RNA polymerase III subunit RPC5"
FT                   /id="PRO_0000073971"
FT   REGION          146..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   MOD_RES         224
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        171
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   CROSSLNK        432
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   CROSSLNK        498
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   CROSSLNK        498
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   CROSSLNK        661
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU0"
FT   VAR_SEQ         30..55
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007066"
FT   CONFLICT        238
FT                   /note="L -> F (in Ref. 1; BAB28084)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675
FT                   /note="T -> A (in Ref. 1; BAB28084)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   710 AA;  79854 MW;  97A9E8B877157A51 CRC64;
     MANEEDDPVI QEIDVYLAKS LAEKLYLFQY PVRPASMTYD DIPHLSAKIK PKQQKVELEM
     AIDTLNPNYC RSKGEQIALN VDGACADETS TYSSKLMDKQ TFCSSQTTSN TARYAAALYR
     QGELHLTPLH GILQLRPSFS YLDKADAKHR EREAANEAGD SSQDEAEEDV KQITVRFSRP
     ESEQARQRRV QSYEFLQKKH AEEPWVHLHY YGMRDSRSEH ERQYLLCQGS SGVENTELVK
     SPSEYLMMLM PPSPEEEKDK PVAPSNVLSM AQLRTLPLAD QIKVLMKNVK VMPFANLMSL
     LGPSVDSVAV LRGIQKVAML VQGNWVVKSD ILYPKDSSSP HSGMPAEVLC RGRDFVMWKF
     TQSRWVVRKE VAAVTKLCAE DVKDFLEHMA VVRINKGWEF LLPYDLEFIK KHPDVVQRQH
     MLWSGIQAKL EKVYNLVKET MPKKPDGQSA PVGLVSGEQR VQTAKTKAQQ NHAFLERELQ
     RRKEQMRAAT VLPSVQIKEE PLSEEEADGA ELEAEEEEPM DTAPSTCLST KLANGLPAGR
     AVGGDSLNGH PVPGCASNPV ACELKAFVEA TFQRQFVLTL SELKRLFNLH LAGLPPGHIL
     FSGVSDRMLQ DTVLAAGCKQ ILVPFPPQTA ASPDEQKVFA LWESGDMSDQ HRQVLLEIFS
     KNYRVRRNLI QSRLTQECGE ELSKQEVDKV LKDCCVSCGG MWYLKGTVQS
 
 
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