CIRBP_RAT
ID CIRBP_RAT Reviewed; 172 AA.
AC P60825; O09069; O09148; Q61413;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cold-inducible RNA-binding protein;
DE AltName: Full=A18 hnRNP;
DE AltName: Full=Glycine-rich RNA-binding protein CIRP;
GN Name=Cirbp; Synonyms=Cirp;
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 [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA Xue J., Nishiyama H., Fujita J.;
RT "Expression of cold inducible-RNA-binding protein (CIRP) in the rat
RT brain.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cold-inducible mRNA binding protein that plays a protective
CC role in the genotoxic stress response by stabilizing transcripts of
CC genes involved in cell survival. Acts as a translational activator.
CC Seems to play an essential role in cold-induced suppression of cell
CC proliferation. Binds specifically to the 3'-untranslated regions (3'-
CC UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a
CC translational repressor. Promotes assembly of stress granules (SGs),
CC when overexpressed (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EIF4G1. Associates with ribosomes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
CC Note=Translocates from the nucleus to the cytoplasm after exposure to
CC UV radiation. Translocates from the nucleus to the cytoplasm into
CC stress granules upon various cytoplasmic stresses, such as osmotic and
CC heat shocks. Its recruitment into stress granules occurs in the absence
CC of TIAR proteins (By similarity). {ECO:0000250}.
CC -!- INDUCTION: By cold stress.
CC -!- DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich domain
CC are necessary for binding to the TXN 3'-untranslated region. Both the
CC RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats)
CC are necessary for optimal recruitment into SGs upon cellular stress.
CC The C-terminal domain containing RGG repeats is necessary for
CC translational repression (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated on arginine residues. Methylation of the RGG motifs is
CC a prerequisite for recruitment into SGs (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B
CC increases RNA-binding activity to the TXN 3'-UTR transcript upon
CC exposure to UV radiation (By similarity). {ECO:0000250}.
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DR EMBL; AB000362; BAA19092.1; -; mRNA.
DR RefSeq; NP_112409.2; NM_031147.2.
DR RefSeq; XP_006241076.1; XM_006241014.3.
DR RefSeq; XP_006241077.3; XM_006241015.3.
DR AlphaFoldDB; P60825; -.
DR SMR; P60825; -.
DR IntAct; P60825; 1.
DR STRING; 10116.ENSRNOP00000021648; -.
DR jPOST; P60825; -.
DR PaxDb; P60825; -.
DR PRIDE; P60825; -.
DR Ensembl; ENSRNOT00000021648; ENSRNOP00000021648; ENSRNOG00000031387.
DR GeneID; 81825; -.
DR KEGG; rno:81825; -.
DR UCSC; RGD:620756; rat.
DR CTD; 1153; -.
DR RGD; 620756; Cirbp.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000156757; -.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; P60825; -.
DR OMA; GWEDRSY; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; P60825; -.
DR TreeFam; TF354331; -.
DR PRO; PR:P60825; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000015999; Expressed in thymus and 20 other tissues.
DR Genevisible; P60825; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; ISS:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; 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; ISS:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISO:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
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 InterPro; IPR003954; RRM_dom_euk.
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 Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Stress response.
FT CHAIN 1..172
FT /note="Cold-inducible RNA-binding protein"
FT /id="PRO_0000081506"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 70..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14011"
SQ SEQUENCE 172 AA; 18607 MW; DA0E53088FBED4C8 CRC64;
MASDEGKLFV GGLSFDTNEQ ALEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA
KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRSR GRGFSRGGGD
RGYGGGRFES RSGGYGGSRD YYASRSQGGS YGYRSSGGSY RDSYDSYATH NE
