RFOX1_MOUSE
ID RFOX1_MOUSE Reviewed; 396 AA.
AC Q9JJ43; Q3UYA8; Q537C9; Q537D0; Q537D1; Q537D2; Q6PD12; Q8R4Z7; Q9JJB5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RNA binding protein fox-1 homolog 1;
DE AltName: Full=Ataxin-2-binding protein 1;
DE AltName: Full=Fox-1 homolog A;
GN Name=Rbfox1; Synonyms=A2bp, A2bp1, Fox1; ORFNames=MNCb-3035;
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] (ISOFORM 2).
RX PubMed=10814712; DOI=10.1093/hmg/9.9.1303;
RA Shibata H., Huynh D.P., Pulst S.-M.;
RT "A novel protein with RNA-binding motifs interacts with ataxin-2.";
RL Hum. Mol. Genet. 9:1303-1313(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 5; 6 AND 7), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Muscle;
RX PubMed=15824060; DOI=10.1093/nar/gki338;
RA Nakahata S., Kawamoto S.;
RT "Tissue-dependent isoforms of mammalian Fox-1 homologs are associated with
RT tissue-specific splicing activities.";
RL Nucleic Acids Res. 33:2078-2089(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Skeletal muscle;
RA Chen W., Winkelmann J.C.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12574126; DOI=10.1093/emboj/cdg089;
RA Jin Y., Suzuki H., Maegawa S., Endo H., Sugano S., Hashimoto K., Yasuda K.,
RA Inoue K.;
RT "A vertebrate RNA-binding protein Fox-1 regulates tissue-specific splicing
RT via the pentanucleotide GCAUG.";
RL EMBO J. 22:905-912(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16260614; DOI=10.1128/mcb.25.22.10005-10016.2005;
RA Underwood J.G., Boutz P.L., Dougherty J.D., Stoilov P., Black D.L.;
RT "Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal
RT splicing regulators in mammals.";
RL Mol. Cell. Biol. 25:10005-10016(2005).
RN [9]
RP FUNCTION.
RX PubMed=17101796; DOI=10.1128/mcb.01015-06;
RA Zhou H.-L., Baraniak A.P., Lou H.;
RT "Role for Fox-1/Fox-2 in mediating the neuronal pathway of
RT calcitonin/calcitonin gene-related peptide alternative RNA processing.";
RL Mol. Cell. Biol. 27:830-841(2007).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-316 AND ARG-387, METHYLATION
RP [LARGE SCALE ANALYSIS] AT ARG-337 (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: RNA-binding protein that regulates alternative splicing
CC events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2
CC to the 3'-splice site. Regulates alternative splicing of tissue-
CC specific exons and of differentially spliced exons during
CC erythropoiesis. {ECO:0000269|PubMed:12574126,
CC ECO:0000269|PubMed:15824060, ECO:0000269|PubMed:16260614,
CC ECO:0000269|PubMed:17101796}.
CC -!- SUBUNIT: Binds to the C-terminus of ATXN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=A016;
CC IsoId=Q9JJ43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJ43-2; Sequence=VSP_030879;
CC Name=3; Synonyms=A713;
CC IsoId=Q9JJ43-3; Sequence=VSP_030880, VSP_030883;
CC Name=4;
CC IsoId=Q9JJ43-4; Sequence=VSP_030882;
CC Name=5; Synonyms=2, A030;
CC IsoId=Q9JJ43-5; Sequence=VSP_030884;
CC Name=6; Synonyms=4, A715;
CC IsoId=Q9JJ43-6; Sequence=VSP_030880, VSP_030883, VSP_030884;
CC Name=7; Synonyms=5, A704;
CC IsoId=Q9JJ43-7; Sequence=VSP_030880, VSP_030881, VSP_030883,
CC VSP_030884;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Detected in
CC heart, brain, neurons, skeletal muscle and embryo.
CC {ECO:0000269|PubMed:12574126, ECO:0000269|PubMed:15824060,
CC ECO:0000269|PubMed:16260614}.
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DR EMBL; AF107204; AAF78292.1; -; mRNA.
DR EMBL; AY659954; AAV74337.1; -; mRNA.
DR EMBL; AY659955; AAV74338.1; -; mRNA.
DR EMBL; AY659956; AAV74339.1; -; mRNA.
DR EMBL; AY659957; AAV74340.1; -; mRNA.
DR EMBL; AY659958; AAV74341.1; -; mRNA.
DR EMBL; AF191501; AAL83425.1; -; mRNA.
DR EMBL; AB041596; BAA95079.1; -; mRNA.
DR EMBL; AK134833; BAE22304.1; -; mRNA.
DR EMBL; BC059002; AAH59002.1; -; mRNA.
DR CCDS; CCDS27936.1; -. [Q9JJ43-3]
DR CCDS; CCDS37245.1; -. [Q9JJ43-1]
DR RefSeq; NP_067452.2; NM_021477.5. [Q9JJ43-1]
DR RefSeq; NP_899011.2; NM_183188.2. [Q9JJ43-3]
DR RefSeq; XP_006522251.1; XM_006522188.1.
DR RefSeq; XP_006522252.1; XM_006522189.3.
DR RefSeq; XP_006522253.1; XM_006522190.1. [Q9JJ43-4]
DR RefSeq; XP_006522255.1; XM_006522192.3.
DR RefSeq; XP_011244213.1; XM_011245911.2.
DR RefSeq; XP_011244218.1; XM_011245916.1.
DR RefSeq; XP_017172487.1; XM_017316998.1.
DR RefSeq; XP_017172491.1; XM_017317002.1.
DR AlphaFoldDB; Q9JJ43; -.
DR BMRB; Q9JJ43; -.
DR SMR; Q9JJ43; -.
DR BioGRID; 234568; 4.
DR IntAct; Q9JJ43; 1.
DR STRING; 10090.ENSMUSP00000049970; -.
DR iPTMnet; Q9JJ43; -.
DR PhosphoSitePlus; Q9JJ43; -.
DR MaxQB; Q9JJ43; -.
DR PaxDb; Q9JJ43; -.
DR PeptideAtlas; Q9JJ43; -.
DR PRIDE; Q9JJ43; -.
DR ProteomicsDB; 255300; -. [Q9JJ43-1]
DR ProteomicsDB; 255301; -. [Q9JJ43-2]
DR ProteomicsDB; 255302; -. [Q9JJ43-3]
DR ProteomicsDB; 255303; -. [Q9JJ43-4]
DR ProteomicsDB; 255304; -. [Q9JJ43-5]
DR ProteomicsDB; 255305; -. [Q9JJ43-6]
DR ProteomicsDB; 255306; -. [Q9JJ43-7]
DR Antibodypedia; 24505; 389 antibodies from 32 providers.
DR DNASU; 268859; -.
DR Ensembl; ENSMUST00000056416; ENSMUSP00000049970; ENSMUSG00000008658. [Q9JJ43-1]
DR Ensembl; ENSMUST00000115841; ENSMUSP00000111507; ENSMUSG00000008658. [Q9JJ43-1]
DR Ensembl; ENSMUST00000229741; ENSMUSP00000155364; ENSMUSG00000008658. [Q9JJ43-3]
DR GeneID; 268859; -.
DR KEGG; mmu:268859; -.
DR UCSC; uc007ycb.2; mouse. [Q9JJ43-1]
DR UCSC; uc007ycc.2; mouse. [Q9JJ43-4]
DR UCSC; uc007ycf.2; mouse. [Q9JJ43-3]
DR UCSC; uc007ycg.2; mouse. [Q9JJ43-6]
DR UCSC; uc007ych.2; mouse. [Q9JJ43-7]
DR UCSC; uc007yci.2; mouse. [Q9JJ43-5]
DR CTD; 54715; -.
DR MGI; MGI:1926224; Rbfox1.
DR VEuPathDB; HostDB:ENSMUSG00000008658; -.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000160685; -.
DR HOGENOM; CLU_048440_0_0_1; -.
DR InParanoid; Q9JJ43; -.
DR OMA; DXNAFAP; -.
DR PhylomeDB; Q9JJ43; -.
DR TreeFam; TF315942; -.
DR BioGRID-ORCS; 268859; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Rbfox1; mouse.
DR PRO; PR:Q9JJ43; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JJ43; protein.
DR Bgee; ENSMUSG00000008658; Expressed in caudate-putamen and 195 other tissues.
DR ExpressionAtlas; Q9JJ43; baseline and differential.
DR Genevisible; Q9JJ43; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0097165; C:nuclear stress granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12407; RRM_FOX1_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025670; Fox-1_C_dom.
DR InterPro; IPR034237; FOX1_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR017325; RNA-bd_Fox-1.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF12414; Fox-1_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037932; Ataxin_2_bd_A2BP; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..396
FT /note="RNA binding protein fox-1 homolog 1"
FT /id="PRO_0000081481"
FT DOMAIN 116..192
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 316
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 387
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10814712"
FT /id="VSP_030879"
FT VAR_SEQ 1..9
FT /note="MNCEREQLR -> MLASQGVLLHSYGVPMIVPAAPYFPGLMQ (in
FT isoform 3, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_030880"
FT VAR_SEQ 156..186
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15824060"
FT /id="VSP_030881"
FT VAR_SEQ 207..224
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030882"
FT VAR_SEQ 301..309
FT /note="DGFYGADIY -> EPVYGNKLLQ (in isoform 3, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_030883"
FT VAR_SEQ 331..396
FT /note="SYGRVYAADPYHHTLAPAPTYGVGAMNAFAPLTDAKTRSHADDVGLVLSSLQ
FT ASIYRGGYNRFAPY -> RNQFVFVATDEISCNTSAVTDEFMLPTPTTTHLLQPPPTAL
FT VP (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10814712,
FT ECO:0000303|PubMed:15824060, ECO:0000303|PubMed:16141072"
FT /id="VSP_030884"
FT CONFLICT 60
FT /note="D -> G (in Ref. 4; BAA95079)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="P -> PFR (in Ref. 1; AAF78292)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="F -> FS (in Ref. 1; AAF78292)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="T -> S (in Ref. 3; AAL83425)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="V -> G (in Ref. 3; AAL83425)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="F -> L (in Ref. 3; AAL83425)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="S -> G (in Ref. 4; BAA95079)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9JJ43-3:337
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 396 AA; 42678 MW; E64DBA6FE6A062ED CRC64;
MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPD
HTLNLYPPTQ THSEQSADTS AQTVSGTATQ TDDAAPTDGQ PQTQPSENTE SKSQPKRLHV
SNIPFRFRDP DLRQMFGQFG KILDVEIIFN ERGSKGFGFV TFENSADADR AREKLHGTVV
EGRKIEVNNA TARVMTNKKT VNPYTNGWKL NPVVGAVYSP DFYAGTVLLC QANQEGSSMY
SGPSSLVYTS AMPGFPYPAA TAAAAYRGAH LRGRGRTVYN TFRAAAPPPP IPAYGGVVYQ
DGFYGADIYG GYAAYRYAQP TPATAAAYSD SYGRVYAADP YHHTLAPAPT YGVGAMNAFA
PLTDAKTRSH ADDVGLVLSS LQASIYRGGY NRFAPY
