CIRBP_MOUSE
ID CIRBP_MOUSE Reviewed; 172 AA.
AC P60824; O09069; O09148; Q3V1A6; Q61413;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION BY COLD-SHOCK.
RC STRAIN=DDY/STD; TISSUE=Testis;
RX PubMed=9151692; DOI=10.1083/jcb.137.4.899;
RA Nishiyama H., Itoh K., Kaneko Y., Kishishita M., Yoshida O., Fujita J.;
RT "A glycine-rich RNA-binding protein mediating cold-inducible suppression of
RT mammalian cell growth.";
RL J. Cell Biol. 137:899-908(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, METHYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-91;
RP ARG-94; ARG-101; ARG-105; ARG-108; ARG-110; ARG-112; ARG-116; ARG-121;
RP ARG-127 AND ARG-131.
RX PubMed=17967451; DOI=10.1016/j.yexcr.2007.09.017;
RA De Leeuw F., Zhang T., Wauquier C., Huez G., Kruys V., Gueydan C.;
RT "The cold-inducible RNA-binding protein migrates from the nucleus to
RT cytoplasmic stress granules by a methylation-dependent mechanism and acts
RT as a translational repressor.";
RL Exp. Cell Res. 313:4130-4144(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Promotes assembly of stress granules
CC (SGs), when overexpressed. Seems to play an essential role in cold-
CC induced suppression of cell proliferation. Acts as a translational
CC repressor. Acts as a translational activator. Binds specifically to the
CC 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2
CC and TXN. {ECO:0000269|PubMed:17967451, ECO:0000269|PubMed:9151692}.
CC -!- SUBUNIT: Interacts with EIF4G1. Associates with ribosomes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17967451}. Cytoplasm {ECO:0000269|PubMed:17967451}.
CC Note=Translocates from the nucleus to the cytoplasm after exposure to
CC UV radiation (By similarity). Translocates from the nucleus to the
CC cytoplasm into stress granules upon various cytoplasmic stresses, such
CC as osmotic and heat shocks. Its recruitment into stress granules occurs
CC in the absence of TIAR proteins. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Up-regulated upon mild cold-shock and hypoxia.
CC {ECO:0000269|PubMed:9151692}.
CC -!- DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich domain
CC are necessary for binding to the TXN 3'-untranslated region (By
CC similarity). Both the RRM domain and the arginine, glycine (RGG) rich
CC domain (RGG repeats) are necessary for optimal recruitment into SGs
CC upon cellular stress. The C-terminal domain containing RGG repeats is
CC necessary for translational repression. {ECO:0000250}.
CC -!- PTM: Methylated on arginine residues. Methylation of the RGG motifs is
CC a prerequisite for recruitment into SGs. {ECO:0000269|PubMed:17967451}.
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; D78135; BAA11213.1; -; mRNA.
DR EMBL; AK014655; BAB29491.1; -; mRNA.
DR EMBL; AK132584; BAE21245.1; -; mRNA.
DR EMBL; BC075699; AAH75699.1; -; mRNA.
DR CCDS; CCDS35975.1; -.
DR RefSeq; NP_031731.1; NM_007705.2.
DR AlphaFoldDB; P60824; -.
DR SMR; P60824; -.
DR BioGRID; 198716; 22.
DR IntAct; P60824; 2.
DR MINT; P60824; -.
DR STRING; 10090.ENSMUSP00000101004; -.
DR iPTMnet; P60824; -.
DR PhosphoSitePlus; P60824; -.
DR EPD; P60824; -.
DR MaxQB; P60824; -.
DR PaxDb; P60824; -.
DR PeptideAtlas; P60824; -.
DR PRIDE; P60824; -.
DR ProteomicsDB; 283563; -.
DR Antibodypedia; 22628; 362 antibodies from 37 providers.
DR DNASU; 12696; -.
DR Ensembl; ENSMUST00000105365; ENSMUSP00000101004; ENSMUSG00000045193.
DR GeneID; 12696; -.
DR KEGG; mmu:12696; -.
DR UCSC; uc007gce.1; mouse.
DR CTD; 1153; -.
DR MGI; MGI:893588; Cirbp.
DR VEuPathDB; HostDB:ENSMUSG00000045193; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153524; -.
DR InParanoid; P60824; -.
DR OMA; GWEDRSY; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; P60824; -.
DR TreeFam; TF354331; -.
DR BioGRID-ORCS; 12696; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cirbp; mouse.
DR PRO; PR:P60824; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P60824; protein.
DR Bgee; ENSMUSG00000045193; Expressed in retinal neural layer and 241 other tissues.
DR ExpressionAtlas; P60824; baseline and differential.
DR Genevisible; P60824; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; ISS:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IDA:MGI.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:MGI.
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; IDA:MGI.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; IDA: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 Activator; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Stress response.
FT CHAIN 1..172
FT /note="Cold-inducible RNA-binding protein"
FT /id="PRO_0000081504"
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"
FT MUTAGEN 91
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 94
FT /note="R->K: Inhibits stress granules localization and
FT translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 101
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 105
FT /note="R->K: Inhibits stress granules localization and
FT translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 108
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 110
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 112
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 116
FT /note="R->K: Inhibits stress granules localization and
FT translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 121
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 127
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
FT MUTAGEN 131
FT /note="R->K: Inhibits translational repression."
FT /evidence="ECO:0000269|PubMed:17967451"
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
