RBMX_BOVIN
ID RBMX_BOVIN Reviewed; 396 AA.
AC Q29RT0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=RBMX; Synonyms=HNRPG;
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=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that plays several role in the regulation
CC of pre- and post-transcriptional processes. Implicated in tissue-
CC specific regulation of gene transcription and alternative splicing of
CC several pre-mRNAs. Binds to and stimulates transcription from the tumor
CC suppressor TXNIP gene promoter; may thus be involved in tumor
CC suppression. When associated with SAFB, binds to and stimulates
CC transcription from the SREBF1 promoter. Associates with nascent mRNAs
CC transcribed by RNA polymerase II. Component of the supraspliceosome
CC complex that regulates pre-mRNA alternative splice site selection. Can
CC either activate or suppress exon inclusion; acts additively with TRA2B
CC to promote exon 7 inclusion of the survival motor neuron SMN2.
CC Represses the splicing of MAPT/Tau exon 10. Binds preferentially to
CC single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
CC single-stranded conformation; probably binds RNA as a homodimer. Binds
CC non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic
CC TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated
CC inducible proteolytic cleavage of TNFR1 ectodomains and the release of
CC TNFR1 exosome-like vesicles to the extracellular compartment (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer. Found in the supraspliceosome complex.
CC Identified in the spliceosome C complex. Forms a complex with ILF2,
CC ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2,
CC KHDRBS3, SAFB/SAFB1, TRA2B and YTHDC1. Interacts with ERAP1; the
CC interaction is RNA-independent (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC Localizes in numerous small granules in the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for splice
CC site selection, indicating that its splicing activity does not require
CC direct binding to RNA. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Arg-185 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
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DR EMBL; BC114040; AAI14041.1; -; mRNA.
DR RefSeq; NP_001040075.1; NM_001046610.1.
DR AlphaFoldDB; Q29RT0; -.
DR SMR; Q29RT0; -.
DR STRING; 9913.ENSBTAP00000056096; -.
DR PaxDb; Q29RT0; -.
DR Ensembl; ENSBTAT00000066112; ENSBTAP00000056096; ENSBTAG00000047652.
DR GeneID; 617969; -.
DR KEGG; bta:617969; -.
DR CTD; 27288; -.
DR VEuPathDB; HostDB:ENSBTAG00000047652; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000162929; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; Q29RT0; -.
DR OMA; SARDECP; -.
DR OrthoDB; 1248417at2759; -.
DR TreeFam; TF331833; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000047652; Expressed in spermatocyte and 9 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Glycoprotein; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Transcription; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..396
FT /note="RNA-binding motif protein, X chromosome"
FT /id="PRO_0000240607"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CHAIN 2..396
FT /note="RNA-binding motif protein, X chromosome, N-
FT terminally processed"
FT /id="PRO_0000367118"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 84..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..236
FT /note="Necessary for the association to nascent RNAPII
FT transcripts and nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 336..396
FT /note="Necessary for RNA-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 144..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein G; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 2
FT /note="N-acetylvaline; in Heterogeneous nuclear
FT ribonucleoprotein G, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 122
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 141
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 162
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
SQ SEQUENCE 396 AA; 42369 MW; 2A81CE93A59F8118 CRC64;
MVEADRPGKL FIGGLNLETD EKSLEATFGK YGRISEVLLM KDRETNKSRG FAFITFESPA
DAKAAVRDMN GKSLDGKAIK VAQATKPAFE SGRRGPPLSR SRGRSRGLRG ARGGGPRRPP
SRGGPADDGG YAGDFDLRPS RAPLPMKRGP PPPRRAGPPP KRAAPSGPAR SGSGGGMRGR
APAARGRDGY EGPPRRDPPP PRRDPYLGSR EGGYSPRDGY SSRDYSSARD ARDFAPSPRE
YTYRDYGHSS ARDECPSRGY GDRDGYGGRD RDYADHPSGG SYRDPFESYG DPRSAAPARG
PPPSYGGGGG RYEEYRGCSP DAYGGGRDGY AGGRSERYSG GRDRVGRADR GLPQSVERGC
PPPRESYSRS GRKVPRGGGR LGSRSERGGG GGRSRY
