RBMX_RAT
ID RBMX_RAT Reviewed; 390 AA.
AC Q4V898;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE AltName: Full=RNA-binding motif protein, X chromosome retrogene;
DE AltName: Full=RNA-binding motif protein, X chromosome retrogene-like;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=Rbmx; Synonyms=Rbmxrt;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PROTEIN SEQUENCE OF 10-17 AND 348-355.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [5]
RP FUNCTION, AND SREBF1 TRANSACTIVATION.
RX PubMed=17188681; DOI=10.1016/j.febslet.2006.12.014;
RA Takemoto T., Nishio Y., Sekine O., Ikeuchi C., Nagai Y., Maeno Y.,
RA Maegawa H., Kimura H., Kashiwagi A.;
RT "RBMX is a novel hepatic transcriptional regulator of SREBP-1c gene
RT response to high-fructose diet.";
RL FEBS Lett. 581:218-222(2007).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX,
RP HOMOMULTIMERIZATION, INTERACTION WITH CLK2; KHDRBS2; SAFB; TRA2B AND
RP YTHDC1, RNA-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
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 SMN. Represses
CC the splicing of MAPT/Tau exon 10. Binds preferentially to single-
CC stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-
CC stranded conformation; probably binds RNA as a homodimer. Binds non-
CC specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1
CC trafficking pathways; promotes both the IL-1-beta-mediated inducible
CC proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1
CC exosome-like vesicles to the extracellular compartment.
CC {ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:17188681,
CC ECO:0000269|PubMed:19282290}.
CC -!- SUBUNIT: Homomultimer (By similarity). Found in the supraspliceosome
CC complex (PubMed:19282290) Identified in the spliceosome C complex (By
CC similarity). Interacts with KHDRBS3 (By similarity). Forms a complex
CC with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA (By similarity).
CC Interacts with SAFB/SAFB1 (By similarity). Interacts with ERAP1; the
CC interaction is RNA-independent (By similarity). Interacts with CLK2,
CC KHDRBS2, SAFB, TRA2B and YTHDC1 (PubMed:19282290). Interacts with
CC PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:P38159,
CC ECO:0000250|UniProtKB:Q9WV02, ECO:0000269|PubMed:19282290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC ribonucleosomes (By similarity). Localizes in numerous small granules
CC in the nucleus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, spleen, lung, liver, kidney,
CC testis and heart. Weakly expressed in skeletal muscle (at protein
CC level). {ECO:0000269|PubMed:19282290}.
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.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Arg-182 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
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DR EMBL; CH474106; EDL75123.1; -; Genomic_DNA.
DR EMBL; BC097479; AAH97479.1; -; mRNA.
DR RefSeq; NP_001020834.1; NM_001025663.1.
DR RefSeq; XP_006257742.1; XM_006257680.3.
DR RefSeq; XP_006257743.1; XM_006257681.3.
DR RefSeq; XP_006257744.1; XM_006257682.3.
DR RefSeq; XP_006257745.1; XM_006257683.3.
DR AlphaFoldDB; Q4V898; -.
DR SMR; Q4V898; -.
DR BioGRID; 257324; 3.
DR CORUM; Q4V898; -.
DR STRING; 10116.ENSRNOP00000001154; -.
DR iPTMnet; Q4V898; -.
DR PhosphoSitePlus; Q4V898; -.
DR jPOST; Q4V898; -.
DR PaxDb; Q4V898; -.
DR PRIDE; Q4V898; -.
DR Ensembl; ENSRNOT00000097092; ENSRNOP00000089402; ENSRNOG00000000866.
DR GeneID; 302855; -.
DR KEGG; rno:302855; -.
DR CTD; 27316; -.
DR RGD; 1565256; Rbmx.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; Q4V898; -.
DR OMA; AKYHEGF; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; Q4V898; -.
DR TreeFam; TF331833; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:Q4V898; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000000866; Expressed in thymus and 20 other tissues.
DR Genevisible; Q4V898; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0006376; P:mRNA splice site selection; IMP:RGD.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Glycoprotein; Isopeptide bond;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Transcription; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..390
FT /note="RNA-binding motif protein, X chromosome"
FT /id="PRO_0000413089"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CHAIN 2..390
FT /note="RNA-binding motif protein, X chromosome, N-
FT terminally processed"
FT /id="PRO_0000413017"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 58..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..336
FT /note="Polar 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 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 125
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 352
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"
FT CONFLICT 12
FT /note="I -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="G -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 42258 MW; 55DFD2163C9D4A9E CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGLPPPP RSRGPPRGLR GGRGGSGGTR
GPPSRGGHMD DGGYSMNFTL SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR
APVSRGRDGY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY SDRDGYGRER DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYTSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP
RDSYSSSSRG APRGGGRGGS RSDRGGRSRY
