RFX1L_DANRE
ID RFX1L_DANRE Reviewed; 382 AA.
AC Q7ZT82;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RNA binding protein fox-1 homolog 1-like;
DE AltName: Full=Ataxin 2-binding protein 1-like;
DE AltName: Full=Fox-1 homolog-like protein 1;
GN Name=rbfox1l; Synonyms=a2bp1l, fox1, fox1l; ORFNames=si:ch211-57k11.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-190, AND TISSUE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: RNA-binding protein that regulates alternative splicing
CC events by binding to 5'-GCAUG-3' elements. Regulates alternative
CC splicing of tissue-specific exons. {ECO:0000269|PubMed:12574126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12574126}.
CC -!- TISSUE SPECIFICITY: Expressed during muscle development in adaxial
CC cells, somites, cardiac precursors, finbuds and jaw muscle cells.
CC {ECO:0000269|PubMed:12574126}.
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DR EMBL; AB074763; BAC65158.1; -; mRNA.
DR EMBL; BX511250; CAM56520.1; -; Genomic_DNA.
DR RefSeq; NP_999940.1; NM_214775.1.
DR AlphaFoldDB; Q7ZT82; -.
DR SMR; Q7ZT82; -.
DR STRING; 7955.ENSDARP00000016637; -.
DR PaxDb; Q7ZT82; -.
DR Ensembl; ENSDART00000027364; ENSDARP00000016637; ENSDARG00000021184.
DR GeneID; 407613; -.
DR KEGG; dre:407613; -.
DR CTD; 407613; -.
DR ZFIN; ZDB-GENE-040923-2; rbfox1l.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000166165; -.
DR HOGENOM; CLU_048440_0_0_1; -.
DR InParanoid; Q7ZT82; -.
DR OMA; PQTASCY; -.
DR OrthoDB; 871288at2759; -.
DR PhylomeDB; Q7ZT82; -.
DR TreeFam; TF315942; -.
DR PRO; PR:Q7ZT82; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000021184; Expressed in muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q7ZT82; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:ZFIN.
DR GO; GO:0003015; P:heart process; IMP:ZFIN.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:ZFIN.
DR GO; GO:0008380; P:RNA splicing; IDA:ZFIN.
DR GO; GO:0048741; P:skeletal muscle fiber development; IGI:ZFIN.
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 mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..382
FT /note="RNA binding protein fox-1 homolog 1-like"
FT /id="PRO_0000317113"
FT DOMAIN 147..223
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 34..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 148
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 224
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MUTAGEN 190
FT /note="F->A: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:12574126"
SQ SEQUENCE 382 AA; 40271 MW; 3880D190028BC6DF CRC64;
MLSSPTVILQ PYGLPVYPQT ASCYPGIVQG AAAQEAGPGN GDPSLPQVYA PPPSYPPPGQ
APPTPAARLP PLDFSAAHPN SEYADHHQLR VYQGPQHDGT ESITASNTDD SLAPVTSDPQ
SLSVSVASGS GAAGGSDEEG GGKAQPKRLH VSNIPFRFRD PDLRQMFGQF GKILDVEIIF
NERGSKGFGF VTFESAVEAD RAREKLNGTI VEGRKIEVNN ATARVVTKKP QTPLVNAAGW
KINPVMGAMY APELYTVASF PYPVPTPTLA YRGSGLRGRG RAVYNTIRSA AAAATPAAVP
AYPGVVYQEG LYGAEVYGGY PATYRVAQSA SAAATATYSD GYGRVYATAT DPYHHSVGPT
TTYGVGTMAS LYRGGYNRFT PY
