ID   CIRBP_XENTR             Reviewed;         166 AA.
AC   Q28IQ9;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Cold-inducible RNA-binding protein {ECO:0000312|EMBL:CAJ83306.1};
DE   AltName: Full=Glycine-rich RNA-binding protein CIRP {ECO:0000250|UniProtKB:Q14011};
GN   Name=cirbp {ECO:0000312|EMBL:CAJ83306.1}; ORFNames=TNeu081o03.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:CAJ83306.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:CAJ83306.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 themm 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).
CC       {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   -!- DOMAIN: The glycine-rich domain, which contains a number of RGG motifs,
CC       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; CR760272; CAJ83306.1; -; mRNA.
DR   RefSeq; NP_001017228.1; NM_001017228.3.
DR   AlphaFoldDB; Q28IQ9; -.
DR   SMR; Q28IQ9; -.
DR   GeneID; 549982; -.
DR   KEGG; xtr:549982; -.
DR   CTD; 1153; -.
DR   Xenbase; XB-GENE-492781; cirbp.
DR   InParanoid; Q28IQ9; -.
DR   OrthoDB; 1579773at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003281; Expressed in neurula embryo and 36 other tissues.
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:0005681; C:spliceosomal complex; IBA:GO_Central.
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:0003723; F:RNA binding; IBA:GO_Central.
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: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: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: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; Reference proteome;
KW   RNA-binding; Stress response.
FT   CHAIN           1..166
FT                   /note="Cold-inducible RNA-binding protein"
FT                   /id="PRO_0000390931"
FT   DOMAIN          6..84
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          68..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   166 AA;  18002 MW;  8B749CFF5395956D CRC64;
     MSCDEGKLFV GGLNFETTEE SLEQVFSKYG QVAEVVVVKD RESKRSRGFG FVTFENPEDA
     KDAMMAMNGK SVDGRQIRVD QAGKSSNDRR GGYRGGSSGG RGFFRGGRGR GGGGDRGYGG
     SSRFENRSGG YQSSGSRDYY GRSHGSYGDR SGGSYRDSYD SYTTQE