RBM4_RABIT
ID RBM4_RABIT Reviewed; 359 AA.
AC Q9BDY9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=RNA-binding protein 4;
DE AltName: Full=Lark homolog;
DE AltName: Full=RNA-binding motif protein 4;
GN Name=RBM4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang W., Guo X., Bhavanandan V.P.;
RT "Five domains in the RNA-binding protein lark.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding factor involved in multiple aspects of cellular
CC processes like alternative splicing of pre-mRNA and translation
CC regulation. Modulates alternative 5'-splice site and exon selection.
CC Acts as a muscle cell differentiation-promoting factor. Activates exon
CC skipping of the PTB pre-mRNA during muscle cell differentiation.
CC Antagonizes the activity of the splicing factor PTBP1 to modulate
CC muscle cell-specific exon selection of alpha tropomyosin. Binds to
CC intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs.
CC Required for the translational activation of PER1 mRNA in response to
CC circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts
CC a suppressive activity on Cap-dependent translation via binding to CU-
CC rich responsive elements within the 3'UTR of mRNAs, a process increased
CC under stress conditions or during myocytes differentiation. Recruits
CC EIF4A1 to stimulate IRES-dependent translation initiation in respons to
CC cellular stress. Associates to internal ribosome entry segment (IRES)
CC in target mRNA species under stress conditions. Plays a role for miRNA-
CC guided RNA cleavage and translation suppression by promoting
CC association of AGO2-containing miRNPs with their cognate target mRNAs.
CC Associates with miRNAs during muscle cell differentiation. Binds
CC preferentially to 5'-CGCGCG[GCA]-3' motif in vitro (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TNPO3; the interaction mediates nuclear import
CC of the protein and is disrupted by nuclear Ran bound to GTP. Interacts
CC with EIF4G1 and WT1. Interacts with EIF4A1; the interaction is
CC modulated under stress-induced conditions. Interacts with AGO1.
CC Interacts with AGO2; the interaction occurs under both cell
CC proliferation and differentiation conditions and in an RNA- and
CC phosphorylation-independent manner. Interacts with DDX5; the
CC interaction occurs in an RNA-independent manner (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasmic granule {ECO:0000250}. Note=Undergoes continuous
CC nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR
CC proteins in nuclear speckles. Arsenite stress-induced phosphorylation
CC increases its subcellular relocalization from the nucleus to the
CC cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK
CC signaling pathway. Primarily localized in nucleus and nucleoli under
CC cell growth conditions and accumulated in the cytoplasm and cytoplasm
CC perinuclear granules upon muscle cell differentiation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylated in vitro on Ser-304 by SRPK1.
CC Phosphorylation on Ser-304 is induced upon cell stress signaling, which
CC alters its subcellular localization and may modulate its activity on
CC IRES-mediated mRNA translation. Phosphorylation on Ser-304 is induced
CC upon cell muscle differentiation (By similarity). {ECO:0000250}.
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DR EMBL; AF233063; AAK14991.1; -; mRNA.
DR RefSeq; NP_001075548.1; NM_001082079.1.
DR AlphaFoldDB; Q9BDY9; -.
DR SMR; Q9BDY9; -.
DR STRING; 9986.ENSOCUP00000005783; -.
DR GeneID; 100008755; -.
DR KEGG; ocu:100008755; -.
DR CTD; 38811; -.
DR eggNOG; KOG0109; Eukaryota.
DR HOGENOM; CLU_045263_0_0_1; -.
DR InParanoid; Q9BDY9; -.
DR OMA; YGAFDYY; -.
DR OrthoDB; 1563362at2759; -.
DR TreeFam; TF320661; -.
DR Proteomes; UP000001811; Unplaced.
DR ExpressionAtlas; Q9BDY9; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR GO; GO:0097158; F:pre-mRNA intronic pyrimidine-rich binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002190; P:cap-independent translational initiation; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0097167; P:circadian regulation of translation; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0002192; P:IRES-dependent translational initiation of linear mRNA; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0032055; P:negative regulation of translation in response to stress; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISS:UniProtKB.
DR GO; GO:0046685; P:response to arsenic-containing substance; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12606; RRM1_RBM4; 1.
DR CDD; cd12607; RRM2_RBM4; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034897; RBM4_RRM1.
DR InterPro; IPR034898; RBM4_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Differentiation; Isopeptide bond; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="RNA-binding protein 4"
FT /id="PRO_0000081756"
FT DOMAIN 2..72
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 78..148
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 160..177
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 196..359
FT /note="Interaction with TNPO3"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWF3"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWF3"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BWF3"
SQ SEQUENCE 359 AA; 40060 MW; A5EDE2BF96725A0B CRC64;
MVKLFIGNLP REATEQEIRS LFEQYGKVLE CDIIKNYGFV HIEDKTAAED AIRNLHHYKL
HGVNINVEAS KNKSKASTKL HVGNISPTCT NQELRAKFEE YGPVIECDIV KDYAFVHMER
AEDAVEAIRG LDNTEFQGKR MHVQLSTSRL RTAPGMGDQS GCYRCGKEGH WSKECPVDRT
GRVADFTEQY NEQYGAVRTP YTMGYGESMY YNDAYGALDY YKRYRVRSYE AVAAAAAASA
YNYAEQTMSH LPQVQSTGVT SHLNSTSVDP YDRHLLQNSG AAATSAAMAA AAATSSSYYG
RDRSPLRRAA AVLPTVGEGY GYGPESELSQ ASAAARNSLY DMARYEREQY VDRARYSAF
