GRL1A_MOUSE
ID GRL1A_MOUSE Reviewed; 366 AA.
AC Q6P6I6; Q8CG13; Q9CXJ7; Q9DCQ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA-directed RNA polymerase II subunit GRINL1A;
DE AltName: Full=DNA-directed RNA polymerase II subunit M;
DE AltName: Full=Glutamate receptor-like protein 1A;
GN Name=Polr2m; Synonyms=Grinl1a;
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, Embryonic eye, Embryonic head, and Kidney;
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=129, and Czech II; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-45, AND IDENTIFICATION.
RC STRAIN=C57BL/6J;
RX PubMed=12063408; DOI=10.1159/000059354;
RA Wydner K.S., Mohan Raj B.K., Sciorra L.J., Roginski R.S.;
RT "The mouse orthologue of the human ionotropic glutamate receptor-like gene
RT (GRINL1A) maps to mouse chromosome 9.";
RL Cytogenet. Cell Genet. 95:240-241(2001).
CC -!- FUNCTION: Isoform 1 appears to be stable component of the Pol II(G)
CC complex form of RNA polymerase II. Pol II synthesizes mRNA precursors
CC and many functional non-coding RNAs and is the central component of the
CC basal RNA polymerase II transcription machinery. Isoform 1 may play a
CC role in Mediator-dependent regulation of transcription activation.
CC Isoform 1 acts in vitro as negative regulator of transcriptional
CC activation; this repression is relieved by the Mediator complex, which
CC restores Pol II(G) activator-dependent transcription to a level
CC equivalent to that of Pol II (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Isoform 1 is a component of the Pol II(G) complex, which
CC contains the RNA polymerase II (Pol II) core complex subunits and
CC Polr2m isoform 1 and appears to be an abundant form of Pol II.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P6I6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P6I6-2; Sequence=VSP_032623;
CC -!- SIMILARITY: Belongs to the GRINL1 family. {ECO:0000305}.
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DR EMBL; AK002571; BAB22196.1; -; mRNA.
DR EMBL; AK014316; BAB29267.1; -; mRNA.
DR EMBL; AK051868; BAC34793.1; -; mRNA.
DR EMBL; AK052037; BAC34836.1; -; mRNA.
DR EMBL; AK079119; BAC37548.1; -; mRNA.
DR EMBL; AK159924; BAE35486.1; -; mRNA.
DR EMBL; AK166738; BAE38981.1; -; mRNA.
DR EMBL; BC018502; AAH18502.1; -; mRNA.
DR EMBL; BC062199; AAH62199.1; -; mRNA.
DR EMBL; AH012404; AAO15648.1; -; Genomic_DNA.
DR CCDS; CCDS23326.1; -. [Q6P6I6-1]
DR CCDS; CCDS52853.1; -. [Q6P6I6-2]
DR RefSeq; NP_001158265.1; NM_001164793.1. [Q6P6I6-2]
DR RefSeq; NP_848717.1; NM_178602.3. [Q6P6I6-1]
DR AlphaFoldDB; Q6P6I6; -.
DR SMR; Q6P6I6; -.
DR IntAct; Q6P6I6; 1.
DR MINT; Q6P6I6; -.
DR STRING; 10090.ENSMUSP00000034720; -.
DR iPTMnet; Q6P6I6; -.
DR PhosphoSitePlus; Q6P6I6; -.
DR EPD; Q6P6I6; -.
DR MaxQB; Q6P6I6; -.
DR PaxDb; Q6P6I6; -.
DR PeptideAtlas; Q6P6I6; -.
DR PRIDE; Q6P6I6; -.
DR ProteomicsDB; 271168; -. [Q6P6I6-1]
DR ProteomicsDB; 271169; -. [Q6P6I6-2]
DR Antibodypedia; 57855; 103 antibodies from 15 providers.
DR DNASU; 28015; -.
DR Ensembl; ENSMUST00000034720; ENSMUSP00000034720; ENSMUSG00000032199. [Q6P6I6-1]
DR Ensembl; ENSMUST00000163972; ENSMUSP00000132335; ENSMUSG00000032199. [Q6P6I6-2]
DR GeneID; 28015; -.
DR KEGG; mmu:28015; -.
DR UCSC; uc009qoy.2; mouse. [Q6P6I6-1]
DR CTD; 81488; -.
DR MGI; MGI:107282; Polr2m.
DR VEuPathDB; HostDB:ENSMUSG00000032199; -.
DR eggNOG; ENOG502S3HI; Eukaryota.
DR GeneTree; ENSGT00950000183065; -.
DR HOGENOM; CLU_051512_0_0_1; -.
DR InParanoid; Q6P6I6; -.
DR OMA; PRKQKFK; -.
DR OrthoDB; 1227717at2759; -.
DR PhylomeDB; Q6P6I6; -.
DR TreeFam; TF332945; -.
DR BioGRID-ORCS; 28015; 16 hits in 75 CRISPR screens.
DR ChiTaRS; Polr2m; mouse.
DR PRO; PR:Q6P6I6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P6I6; protein.
DR Bgee; ENSMUSG00000032199; Expressed in somite and 268 other tissues.
DR ExpressionAtlas; Q6P6I6; baseline and differential.
DR Genevisible; Q6P6I6; MM.
DR GO; GO:0043025; C:neuronal cell body; IMP:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISO:MGI.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0051685; P:maintenance of ER location; IMP:UniProtKB.
DR InterPro; IPR026213; GRINL1.
DR Pfam; PF15328; GCOM2; 1.
DR PRINTS; PR02085; POLR2GRINL1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1..366
FT /note="DNA-directed RNA polymerase II subunit GRINL1A"
FT /id="PRO_0000326230"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..39
FT /evidence="ECO:0000255"
FT COILED 299..333
FT /evidence="ECO:0000255"
FT COMPBIAS 101..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032623"
FT CONFLICT 112
FT /note="D -> V (in Ref. 2; AAH62199)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Q -> R (in Ref. 2; AAH62199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41237 MW; 1115E39921CF3561 CRC64;
MFSLPRGFEP PAPEDLGRQS SAELRERLRR QERLLRNEKF ICKLPDKGKK ISDTVAKLKA
AISEREEVRG RSELFHPVSV DCKLRQKATT RADTDVDKAQ SSDLMLDTSS LDPDCSSIDI
KSSKSTSETQ GPTHLTHRGN EETLEAGYTV NSSPAAHIRA RAPSSEVKEH LPQHSVSSQE
EEISSSIDSL FITKLQKITI ADQSEPSEEN TSTENFPELQ SETPKKPHYM KVLEMRARNP
VPPPHKFKTN VLPTQQSDSP SHCQRGQSPA SSEEQRRRAR QHLDDITAAR LLPLHHLPAQ
LLSIEESLAL QREQKQNYEE MQAKLAAQKL AERLNIKMQS YNPEGESSGR YREVRDEADA
QSSDEC
