CIRBA_XENLA
ID CIRBA_XENLA Reviewed; 166 AA.
AC O93235; Q7ZYU7; Q9DFG5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cold-inducible RNA-binding protein A;
DE AltName: Full=Cold-inducible RNA-binding protein;
DE Short=XCIRP;
DE AltName: Full=Cold-inducible RNA-binding protein 1;
DE Short=XCIRP-1;
DE AltName: Full=Glycine-rich RNA-binding protein CIRP-A;
GN Name=cirbp-a; Synonyms=cirbp, cirp, cirp-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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9602141; DOI=10.1016/s0378-1119(98)00102-4;
RA Uochi T., Asashima M.;
RT "XCIRP (Xenopus homolog of cold-inducible RNA-binding protein) is expressed
RT transiently in developing pronephros and neural tissue.";
RL Gene 211:245-250(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND LACK OF COLD-INDUCTION IN EMBRYOS.
RC TISSUE=Neurula;
RX PubMed=11018519; DOI=10.1016/s0014-5793(00)02019-6;
RA Peng Y., Kok K.H., Xu R.H., Kwok K.H., Tay D., Fung P.C., Kung H.F.,
RA Lin M.C.;
RT "Maternal cold inducible RNA binding protein is required for embryonic
RT kidney formation in Xenopus laevis.";
RL FEBS Lett. 482:37-43(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 28-35.
RC TISSUE=Oocyte;
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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
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).
RN [6]
RP FUNCTION, AND RNA-BINDING.
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 [7]
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 sequence (ARE)-containing mRNAs by
CC binding to them and inhibiting their deadenylation (By similarity).
CC Essential for embryonic gastrulation and neural development, acting to
CC maintain the expression of a set of adhesion molecules and cell
CC movement during embryogenesis. Plays a role in the specification and
CC migration of pronephros cells during embryonic kidney development.
CC {ECO:0000250, ECO:0000269|PubMed:11018519, ECO:0000269|PubMed:16600183,
CC ECO:0000269|PubMed:18687117}.
CC -!- SUBUNIT: Interacts with prmt1. Interacts with elavl1/elrA (via RRM3).
CC Associates with ribosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm.
CC Predominantly cytoplasmic in oocytes. Translocates from the nucleus to
CC the cytoplasm upon arginine methylation (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O93235-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O93235-2; Sequence=VSP_038656;
CC -!- TISSUE SPECIFICITY: Initially localizes to the animal half of the late
CC blastula embryo, then to the neural crest and neural tube from late
CC neurula stage through to larval stages, and finally in the neural
CC tissues and developing pronephros of tailbud stages. Expressed in a
CC range of adult tissues including kidney, brain, lung, liver, heart,
CC muslce, stomach, small and large intestine, and skin.
CC {ECO:0000269|PubMed:10817911, ECO:0000269|PubMed:11018519,
CC ECO:0000269|PubMed:18687117, ECO:0000269|PubMed:9602141}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at a low level in the mature oocyte, with expression
CC increasing rapidly during gastrulation, and is maintained throughout
CC organogenesis. {ECO:0000269|PubMed:11018519,
CC ECO:0000269|PubMed:9602141}.
CC -!- INDUCTION: By cold stress in adult brain. Cold-induction may be adult-
CC specific since cold-induction is not observed during embryonic
CC development. Induced by tcf7l1/tcf-3. {ECO:0000269|PubMed:10817911,
CC ECO:0000269|PubMed:18687117}.
CC -!- DOMAIN: The glycine-rich domain, which contains a number of RGG motifs,
CC is necessary to regulate nucleocytoplasmic localization. {ECO:0000250}.
CC -!- PTM: Methylated on arginine residues within RGG motifs. Methylation by
CC prmt1 promotes cytoplasmic accumulation (By similarity). {ECO:0000250}.
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DR EMBL; AB007597; BAA31861.1; -; mRNA.
DR EMBL; AF278702; AAG09816.1; -; mRNA.
DR EMBL; BC041204; AAH41204.1; -; mRNA.
DR RefSeq; NP_001080069.1; NM_001086600.1. [O93235-1]
DR RefSeq; XP_018121719.1; XM_018266230.1. [O93235-1]
DR AlphaFoldDB; O93235; -.
DR SMR; O93235; -.
DR BioGRID; 98003; 1.
DR DNASU; 379761; -.
DR GeneID; 379761; -.
DR KEGG; xla:379761; -.
DR CTD; 379761; -.
DR Xenbase; XB-GENE-6256647; cirbp.L.
DR OMA; HYRRDYH; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379761; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; 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; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
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: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:0072004; P:kidney field specification; IMP: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; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein;
KW Direct protein sequencing; Nucleus; Reference proteome; RNA-binding;
KW Stress response.
FT CHAIN 1..166
FT /note="Cold-inducible RNA-binding protein A"
FT /id="PRO_0000081507"
FT DOMAIN 5..83
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 67..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 163..166
FT /note="ATHE -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9602141"
FT /id="VSP_038656"
FT CONFLICT 19
FT /note="D -> G (in Ref. 2; AAG09816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 17903 MW; DB87F2183FE9B371 CRC64;
MSDEGKLFIG GLNFETNEDC LEQAFTKYGR ISEVVVVKDR ETKRSRGFGF VTFENVDDAK
DAMMAMNGKS VDGRQIRVDQ AGKSSGERRG GYRGGSSGGR GFFRGGRGRG GGDRGYGSSR
FDNRSGGYGG SSGSRDYYGS GRSQGSYGDR SGGSYRDSYD SYATHE
