GRL1A_BOVIN
ID GRL1A_BOVIN Reviewed; 370 AA.
AC Q17QE3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA-directed RNA polymerase II subunit GRINL1A;
DE AltName: Full=DNA-directed RNA polymerase II subunit M;
DE AltName: Full=GRINL1A downstream protein 1;
DE Short=Gdown1;
DE AltName: Full=Glutamate receptor-like protein 1A;
GN Name=POLR2M; Synonyms=GRINL1A;
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].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 60-79 AND 323-349, FUNCTION, IDENTIFICATION IN THE POL
RP II(G) COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16769904; DOI=10.1073/pnas.0603702103;
RA Hu X., Malik S., Negroiu C.C., Hubbard K., Velalar C.N., Hampton B.,
RA Grosu D., Catalano J., Roeder R.G., Gnatt A.;
RT "A Mediator-responsive form of metazoan RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9506-9511(2006).
CC -!- FUNCTION: Appears to be a stable component of the Pol II(G) complex
CC form of RNA polymerase II (Pol 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. May play a role in
CC Mediator complex-dependent regulation of transcription activation. Acts
CC in vitro as a negative regulator of transcriptional activation; this
CC repression is relieved by the Mediator complex, which restores Pol
CC II(G) activator-dependent transcription to a level equivalent to that
CC of Pol II. {ECO:0000269|PubMed:16769904}.
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:0000269|PubMed:16769904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GRINL1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18413.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC118412; AAI18413.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001098947.1; NM_001105477.1.
DR RefSeq; XP_005211707.1; XM_005211650.3.
DR AlphaFoldDB; Q17QE3; -.
DR SMR; Q17QE3; -.
DR DIP; DIP-61185N; -.
DR IntAct; Q17QE3; 1.
DR STRING; 9913.ENSBTAP00000056555; -.
DR PaxDb; Q17QE3; -.
DR Ensembl; ENSBTAT00000002841; ENSBTAP00000002841; ENSBTAG00000040384.
DR GeneID; 100125877; -.
DR KEGG; bta:100125877; -.
DR CTD; 81488; -.
DR VEuPathDB; HostDB:ENSBTAG00000040384; -.
DR VGNC; VGNC:55134; POLR2M.
DR eggNOG; ENOG502S3HI; Eukaryota.
DR GeneTree; ENSGT00950000183065; -.
DR HOGENOM; CLU_051512_0_0_1; -.
DR InParanoid; Q17QE3; -.
DR OMA; PRKQKFK; -.
DR OrthoDB; 1227717at2759; -.
DR TreeFam; TF332945; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000040384; Expressed in gluteal muscle and 111 other tissues.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:Ensembl.
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; IBA:GO_Central.
DR InterPro; IPR026213; GRINL1.
DR Pfam; PF15328; GCOM2; 1.
DR PRINTS; PR02085; POLR2GRINL1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleus; Reference proteome; Transcription.
FT CHAIN 1..370
FT /note="DNA-directed RNA polymerase II subunit GRINL1A"
FT /id="PRO_0000326228"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..69
FT /evidence="ECO:0000255"
FT COILED 303..328
FT /evidence="ECO:0000255"
FT COMPBIAS 103..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41312 MW; 477C3B6607D6178A CRC64;
MSSLPRGFEP QTPEDLGQRS LAELREMLKR QERLLRNVKF ICKLPDKGKK ISDAVTKLKA
AIAEREEVRG RSELFYPVSL DCKERQKAIA VVDGDRDKAQ NSDQILDTSS PVPGCSSVAN
ITSSQTTSRQ QGLAHPTRGG DAEAAEAEHT VSEHPTSSSG APAPSSSQAS EGLPQHCALG
QVEDHPGSSD NLFIDRLQRI TIADPTEHHS EGNRNPENLA GLWSGPQKKP HYMEVLEMRA
KNPMPPPHKF KTNVLPSQPR DSSSACQRRG SPISSEERRR RDRKHLDDIT AARLLPLHHL
PTQLLSIEES LALQRQQKQS YEEIQAKLAA QKLAERLNIK MQSYNPEGES SRKYREVRDE
DDDQSSEDEF
