RBM3_MOUSE
ID RBM3_MOUSE Reviewed; 153 AA.
AC O89086;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein 3;
DE AltName: Full=RNA-binding motif protein 3;
GN Name=Rbm3;
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 [MRNA].
RX PubMed=10793079; DOI=10.1016/s0002-9440(10)65039-0;
RA Danno S., Itoh K., Matsuda T., Fujita J.;
RT "Decreased expression of mouse Rbm3, a cold-shock protein, in Sertoli cells
RT of cryptorchid testis.";
RL Am. J. Pathol. 156:1685-1692(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR;
RX PubMed=11470798; DOI=10.1074/jbc.m106008200;
RA Chappell S.A., Owens G.C., Mauro V.P.;
RT "A 5' leader of Rbm3, a cold stress-induced mRNA, mediates internal
RT initiation of translation with increased efficiency under conditions of
RT mild hypothermia.";
RL J. Biol. Chem. 276:36917-36922(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=15684048; DOI=10.1073/pnas.0409764102;
RA Dresios J., Aschrafi A., Owens G.C., Vanderklish P.W., Edelman G.M.,
RA Mauro V.P.;
RT "Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters
RT microRNA levels, and enhances global protein synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1865-1870(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-47; ARG-103; ARG-118 AND ARG-128,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Cold-inducible mRNA binding protein that enhances global
CC protein synthesis at both physiological and mild hypothermic
CC temperatures. Reduces the relative abundance of microRNAs, when
CC overexpressed. Enhances phosphorylation of translation initiation
CC factors and active polysome formation. {ECO:0000269|PubMed:15684048}.
CC -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC subunits in an RNA-independent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA
CC granules in dentrites. {ECO:0000250}.
CC -!- PTM: Arg-103 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; AB016424; BAA32060.1; -; mRNA.
DR EMBL; AY052560; AAL10707.1; -; mRNA.
DR EMBL; BC006580; AAH06580.1; -; mRNA.
DR CCDS; CCDS52988.1; -.
DR RefSeq; NP_001159882.1; NM_001166410.2.
DR RefSeq; NP_001159883.1; NM_001166411.2.
DR AlphaFoldDB; O89086; -.
DR SMR; O89086; -.
DR BioGRID; 202821; 11.
DR IntAct; O89086; 4.
DR MINT; O89086; -.
DR STRING; 10090.ENSMUSP00000038964; -.
DR iPTMnet; O89086; -.
DR PhosphoSitePlus; O89086; -.
DR REPRODUCTION-2DPAGE; IPI00130883; -.
DR EPD; O89086; -.
DR PaxDb; O89086; -.
DR PeptideAtlas; O89086; -.
DR PRIDE; O89086; -.
DR ProteomicsDB; 300267; -.
DR DNASU; 19652; -.
DR Ensembl; ENSMUST00000115615; ENSMUSP00000111277; ENSMUSG00000031167.
DR Ensembl; ENSMUST00000115619; ENSMUSP00000111282; ENSMUSG00000031167.
DR Ensembl; ENSMUST00000115621; ENSMUSP00000111284; ENSMUSG00000031167.
DR GeneID; 19652; -.
DR KEGG; mmu:19652; -.
DR UCSC; uc009sob.3; mouse.
DR CTD; 5935; -.
DR MGI; MGI:1099460; Rbm3.
DR VEuPathDB; HostDB:ENSMUSG00000031167; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153524; -.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; O89086; -.
DR PhylomeDB; O89086; -.
DR BioGRID-ORCS; 19652; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm3; mouse.
DR PRO; PR:O89086; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O89086; protein.
DR Bgee; ENSMUSG00000031167; Expressed in ventricular zone and 215 other tissues.
DR ExpressionAtlas; O89086; baseline and differential.
DR Genevisible; O89086; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IPI:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035196; P:miRNA processing; IDA:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IDA:MGI.
DR GO; GO:0006412; P:translation; IDA:MGI.
DR CDD; cd12449; RRM_CIRBP_RBM3; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034278; RBM3/CIRBP_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..153
FT /note="RNA-binding protein 3"
FT /id="PRO_0000081753"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 103
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 103
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 103
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 118
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 128
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
SQ SEQUENCE 153 AA; 16605 MW; C54A66A1A9E4FF3D CRC64;
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
SDAMRAMNGE SLDGRQIRVD HAGKSARGSR GGAFGGRGRS YSRGGGDQGY GSGRYDSRPG
GYGYGYGRSR DYSGSQGGYD RYSGGNYRDN YDN
