ID   GRL1A_RAT               Reviewed;         364 AA.
AC   Q91XQ4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 116.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11474202; DOI=10.1159/000056971;
RA   Roginski R.S., Mohan Raj B.K., Finkernagel S.W., Sciorra L.J.;
RT   "Assignment of an ionotropic glutamate receptor-like gene (GRINL1A) to
RT   human chromosome 15q22.1 by in situ hybridization.";
RL   Cytogenet. Cell Genet. 93:143-144(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Appears to be stable component of the Pol II(G) complex form
CC       of RNA polymerase II. Pol II synthesizes mRNA precursors and many
CC       functional non-coding RNAs and is the central component of the basal
CC       RNA polymerase II transcription machinery. May play a role in Mediator-
CC       dependent regulation of transcription activation. In vitro, acts as
CC       negative regulator of transcriptional activation; this repression is
CC       relieved by the Mediator complex, which restores Pol II(G) activator-
CC       dependent transcription to a level equivalent to that of Pol II (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Pol II(G) complex, which contains the RNA
CC       polymerase II (Pol II) core complex subunits and Polr2m and appears to
CC       be an abundant form of Pol II. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GRINL1 family. {ECO:0000305}.
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DR   EMBL; AF326772; AAK92283.2; -; mRNA.
DR   EMBL; BC079379; AAH79379.1; -; mRNA.
DR   RefSeq; NP_899652.1; NM_183402.1.
DR   AlphaFoldDB; Q91XQ4; -.
DR   SMR; Q91XQ4; -.
DR   STRING; 10116.ENSRNOP00000065670; -.
DR   PhosphoSitePlus; Q91XQ4; -.
DR   PaxDb; Q91XQ4; -.
DR   PRIDE; Q91XQ4; -.
DR   Ensembl; ENSRNOT00000085843; ENSRNOP00000072186; ENSRNOG00000057676.
DR   GeneID; 192147; -.
DR   KEGG; rno:192147; -.
DR   UCSC; RGD:619847; rat.
DR   CTD; 81488; -.
DR   RGD; 619847; Polr2m.
DR   eggNOG; ENOG502S3HI; Eukaryota.
DR   GeneTree; ENSGT00950000183065; -.
DR   HOGENOM; CLU_051512_0_0_1; -.
DR   InParanoid; Q91XQ4; -.
DR   OrthoDB; 1227717at2759; -.
DR   PhylomeDB; Q91XQ4; -.
DR   TreeFam; TF332945; -.
DR   PRO; PR:Q91XQ4; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000057676; Expressed in heart and 20 other tissues.
DR   ExpressionAtlas; Q91XQ4; baseline and differential.
DR   Genevisible; Q91XQ4; RN.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; ISO:RGD.
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; ISO:RGD.
DR   InterPro; IPR026213; GRINL1.
DR   Pfam; PF15328; GCOM2; 1.
DR   PRINTS; PR02085; POLR2GRINL1.
PE   2: Evidence at transcript level;
KW   Coiled coil; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW   Transcription.
FT   CHAIN           1..364
FT                   /note="DNA-directed RNA polymerase II subunit GRINL1A"
FT                   /id="PRO_0000326232"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          15..39
FT                   /evidence="ECO:0000255"
FT   COILED          297..331
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        200..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  40874 MW;  5EC07061B9F917EC CRC64;
     MCSLPRGFEP PAPEDLGRQS SAELRERLRR QERLLRNEKF ICKLPDKGKK ISDTIAKLKA
     AISEREEVRG RTELFHPVSV DCKLRHKATT RVDTDIDKAQ NSDLMLDTSS LVPECSSVDI
     ESSKTTSETQ GPTHLTHKGN EETLATGCTV NTCPSARITT QDPSSEVNEH LPQHSSQVEE
     ISSSVDSLFI TKLQKITIAD QTEPSEENTS TENFPGLQSE TPKKPHYMKV LEMRAKNPVP
     PPHKFKTNVL PTQQSDSSSH CHKGQSPASS EEHRRRARQH LDDVTAARLL PLHHLPAQLL
     SIEESLALQK EQKQNYEEMQ AKLAAQKLAE RLNIKMQSFN PEGESSGRYR EVRDEDDAQS
     SDEC