CIRBB_XENLA
ID CIRBB_XENLA Reviewed; 166 AA.
AC Q9DED4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cold-inducible RNA-binding protein B;
DE AltName: Full=Cold-inducible RNA-binding protein 2 {ECO:0000312|EMBL:BAB19129.1};
DE Short=xCIRP2 {ECO:0000303|PubMed:11095679};
DE AltName: Full=Glycine-rich RNA-binding protein CIRP-B;
GN Name=cirbp-b; Synonyms=cirbp, cirp2 {ECO:0000312|EMBL:AAH54250.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB19129.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, RNA-BINDING, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:11095679};
RX PubMed=11095679; DOI=10.1093/nar/28.23.4689;
RA Matsumoto K., Aoki K., Dohmae N., Takio K., Tsujimoto M.;
RT "CIRP2, a major cytoplasmic RNA-binding protein in Xenopus oocytes.";
RL Nucleic Acids Res. 28:4689-4697(2000).
RN [2] {ECO:0000312|EMBL:AAH54250.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH54250.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, DOMAIN, AND METHYLATION.
RX PubMed=12466543; DOI=10.1093/nar/gkf638;
RA Aoki K., Ishii Y., Matsumoto K., Tsujimoto M.;
RT "Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich
RT region-mediated nucleocytoplasmic distribution.";
RL Nucleic Acids Res. 30:5182-5192(2002).
RN [4] {ECO:0000305}
RP FUNCTION, RNA-BINDING, AND INTERACTION WITH ELAVL1.
RX PubMed=13679363; DOI=10.1074/jbc.m308328200;
RA Aoki K., Matsumoto K., Tsujimoto M.;
RT "Xenopus cold-inducible RNA-binding protein 2 interacts with ElrA, the
RT Xenopus homolog of HuR, and inhibits deadenylation of specific mRNAs.";
RL J. Biol. Chem. 278:48491-48497(2003).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16600183; DOI=10.1016/j.bbrc.2006.03.086;
RA Peng Y., Yang P.H., Tanner J.A., Huang J.D., Li M., Lee H.F., Xu R.H.,
RA Kung H.F., Lin M.C.;
RT "Cold-inducible RNA binding protein is required for the expression of
RT adhesion molecules and embryonic cell movement in Xenopus laevis.";
RL Biochem. Biophys. Res. Commun. 344:416-424(2006).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18687117; DOI=10.1186/1471-213x-8-77;
RA van Venrooy S., Fichtner D., Kunz M., Wedlich D., Gradl D.;
RT "Cold-inducible RNA binding protein (CIRP), a novel XTcf-3 specific target
RT gene regulates neural development in Xenopus.";
RL BMC Dev. Biol. 8:77-77(2008).
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.
CC {ECO:0000269|PubMed:13679363, ECO:0000269|PubMed:16600183,
CC ECO:0000269|PubMed:18687117}.
CC -!- SUBUNIT: Interacts with prmt1. Interacts with elavl1/elrA (via RRM3).
CC Associates with ribosomes. {ECO:0000269|PubMed:11095679,
CC ECO:0000269|PubMed:12466543, ECO:0000269|PubMed:13679363}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:12466543}. Cytoplasm
CC {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:12466543}.
CC Note=Shuttles between the nucleus and cytoplasm. Predominantly
CC cytoplasmic in oocytes. Translocates from the nucleus to the cytoplasm
CC upon arginine methylation. {ECO:0000269|PubMed:11095679,
CC ECO:0000269|PubMed:12466543}.
CC -!- TISSUE SPECIFICITY: In adults, most abundant in testis, ovary, brain
CC and liver, with lower expression in kidney and heart.
CC {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:18687117}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Levels
CC accumulate during oogenesis (at protein level).
CC {ECO:0000269|PubMed:11095679}.
CC -!- INDUCTION: By tcf7l1/tcf-3. {ECO:0000269|PubMed:18687117}.
CC -!- DOMAIN: The glycine-rich domain, which contains a number of RGG motifs,
CC is necessary to regulate nucleocytoplasmic localization.
CC {ECO:0000269|PubMed:12466543}.
CC -!- PTM: Methylated on arginine residues within RGG motifs. Methylation by
CC prmt1 promotes cytoplasmic accumulation. {ECO:0000269|PubMed:12466543}.
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DR EMBL; AB044535; BAB19129.1; -; mRNA.
DR EMBL; BC054250; AAH54250.1; -; mRNA.
DR RefSeq; NP_001079794.1; NM_001086325.1.
DR AlphaFoldDB; Q9DED4; -.
DR SMR; Q9DED4; -.
DR BioGRID; 97727; 1.
DR IntAct; Q9DED4; 1.
DR MINT; Q9DED4; -.
DR DNASU; 379484; -.
DR GeneID; 379484; -.
DR KEGG; xla:379484; -.
DR CTD; 379484; -.
DR Xenbase; XB-GENE-492785; cirbp.S.
DR OMA; GWEDRSY; -.
DR OrthoDB; 1579773at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 379484; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP: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 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Direct protein sequencing; Methylation;
KW Nucleus; Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..166
FT /note="Cold-inducible RNA-binding protein B"
FT /id="PRO_0000390930"
FT DOMAIN 5..83
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 124..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 166 AA; 17855 MW; 809B4B247447AEAF CRC64;
MSDEGKLFIG GLNFDTNEES LEQVFSKYGQ ISEVVVVKDR ETKRSRGFGF VTFENPDDAK
DAMMAMNGKA VDGRQIRVDQ AGKSSGDRRG GYRGGSSGGR GFFRGGRGRG GGDRGYGSSR
FDNRSGGYGG SSGSRDYYSS GRSQGSYGDR AGGSYRDSYD SYATHE
