CIRBP_LITCT
ID CIRBP_LITCT Reviewed; 164 AA.
AC Q9PTX2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Cold-inducible RNA-binding protein {ECO:0000303|PubMed:10817911};
DE Short=BFCIRP {ECO:0000312|EMBL:BAA88978.1};
DE AltName: Full=Glycine-rich RNA-binding protein CIRP {ECO:0000250|UniProtKB:Q14011};
GN Name=cirbp {ECO:0000250|UniProtKB:Q14011};
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA88978.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Liver {ECO:0000312|EMBL:BAA88978.1};
RX PubMed=10817911; DOI=10.1016/s0305-0491(99)00174-1;
RA Saito T., Sugimoto K., Adachi Y., Wu Q., Mori K.J.;
RT "Cloning and characterization of amphibian cold inducible RNA-binding
RT protein.";
RL Comp. Biochem. Physiol. 125:237-245(2000).
CC -!- FUNCTION: Cold-inducible mRNA binding protein. Acts cooperatively with
CC elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by
CC binding to them and inhibiting their deadenylation. Essential for
CC embryonic gastrulation and neural development, acting to maintain the
CC expression of a set of adhesion molecules, and cell movement during
CC embryogenesis. Required for pronephros development (By similarity). May
CC play a role in hibernation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with prmt1. Interacts with elavl1/elrA (via RRM3).
CC Associates with ribosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q9DED4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9DED4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9DED4}. Note=Shuttles between the nucleus and
CC cytoplasm. Predominantly cytoplasmic in oocytes. Translocates from the
CC nucleus to the cytoplasm upon arginine methylation (By similarity).
CC {ECO:0000250|UniProtKB:Q9DED4}.
CC -!- DEVELOPMENTAL STAGE: Expression is stronger in winter than in summer.
CC {ECO:0000269|PubMed:10817911}.
CC -!- DOMAIN: The arginine, glycine rich domain, which contains a number of
CC RGG motifs, is necessary to regulate nucleocytoplasmic localization.
CC {ECO:0000250|UniProtKB:Q9DED4}.
CC -!- PTM: Methylated on arginine residues within RGG motifs. Methylation by
CC prmt1 promotes cytoplasmic accumulation (By similarity).
CC {ECO:0000250|UniProtKB:Q9DED4}.
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DR EMBL; AB025351; BAA88978.1; -; mRNA.
DR AlphaFoldDB; Q9PTX2; -.
DR SMR; Q9PTX2; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme 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:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR GO; GO:0042750; P:hibernation; IEP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; 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; Developmental protein; Methylation; Nucleus; RNA-binding;
KW Stress response.
FT CHAIN 1..164
FT /note="Cold-inducible RNA-binding protein"
FT /id="PRO_0000390929"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 65..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 164 AA; 17608 MW; 160AC79D609AAA6D CRC64;
MSCDEGKLFV GGLSFDTDEQ CLETVFSKYG QIQEVVVVKD RETKRSRGFG FVTFENCEDA
KDAMAGMNGK TVDGRQIRVD QAGKSSNDRR GGYRGGSSGG GRGFFRGGRG RGGGGYGGSS
RFDNRSGGGY GGWIPDYYSS GRESSYGDRS AGGRSYRDSY DSYG
