RBM3_RAT
ID RBM3_RAT Reviewed; 155 AA.
AC Q925G0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RNA-binding protein 3;
DE AltName: Full=RNA-binding motif protein 3;
GN Name=Rbm3;
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 MRNA].
RA Beck A.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127.
RC STRAIN=Sprague-Dawley;
RA Long X., Bigsby R.M., Nephew K.P.;
RT "Rat RNA-binding motif protein 3 (RBM3).";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH RPL4, 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 [4]
RP FUNCTION, METHYLATION, ASSOCIATION WITH RIBOSOMES, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RX PubMed=17403028; DOI=10.1111/j.1471-4159.2007.04521.x;
RA Smart F., Aschrafi A., Atkins A., Owens G.C., Pilotte J., Cunningham B.A.,
RA Vanderklish P.W.;
RT "Two isoforms of the cold-inducible mRNA-binding protein RBM3 localize to
RT dendrites and promote translation.";
RL J. Neurochem. 101:1367-1379(2007).
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 (By similarity). Enhances phosphorylation of translation
CC initiation factors and active polysome formation. {ECO:0000250,
CC ECO:0000269|PubMed:17403028}.
CC -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC subunits. {ECO:0000269|PubMed:15684048}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17403028}. Cytoplasm
CC {ECO:0000269|PubMed:17403028}. Cell projection, dendrite
CC {ECO:0000269|PubMed:17403028}. Note=Localizes in mRNA granules in
CC dendrites. Isoform 1 shows a much higher dendritic localization than
CC isoform 2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RBM3 Arg-;
CC IsoId=Q925G0-1; Sequence=Displayed;
CC Name=2; Synonyms=RBM3 Arg+;
CC IsoId=Q925G0-2; Sequence=VSP_038576;
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain. Highly expressed in
CC the cerebellum and olfactory bulb (at protein level). Expressed in
CC neurons and glial cells. {ECO:0000269|PubMed:17403028}.
CC -!- PTM: Arg-105 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. Isoform 2 is methylated.
CC {ECO:0000269|PubMed:17403028}.
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DR EMBL; FM093406; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF355190; AAK39523.1; -; mRNA.
DR RefSeq; NP_446148.1; NM_053696.1.
DR AlphaFoldDB; Q925G0; -.
DR SMR; Q925G0; -.
DR IntAct; Q925G0; 1.
DR MINT; Q925G0; -.
DR STRING; 10116.ENSRNOP00000007367; -.
DR jPOST; Q925G0; -.
DR PaxDb; Q925G0; -.
DR PRIDE; Q925G0; -.
DR GeneID; 114488; -.
DR KEGG; rno:114488; -.
DR UCSC; RGD:620145; rat. [Q925G0-1]
DR CTD; 5935; -.
DR RGD; 620145; Rbm3.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q925G0; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; Q925G0; -.
DR PRO; PR:Q925G0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035196; P:miRNA processing; ISO:RGD.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0006412; P:translation; ISO:RGD.
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 Alternative splicing; Cell projection; Cytoplasm; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..155
FT /note="RNA-binding protein 3"
FT /id="PRO_0000390775"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 79..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O89086"
FT MOD_RES 105
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 105
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 120
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 130
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89086"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT MOD_RES 153
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P98179"
FT VAR_SEQ 136
FT /note="G -> GA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038576"
FT CONFLICT 63
FT /note="V -> A (in Ref. 2; AAK39523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 16855 MW; 9BD4118495D60411 CRC64;
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
SDVMRAMNGE SLDGRQIRVD HAGKSARGTR GGAFGAHGRG RSYSRGGGDQ GYGSGRYDSR
PGGYGYGYGR SRDYSGSQGG YDRYSGGNYR DNYDN
