ID   RFOX2_XENLA             Reviewed;         411 AA.
AC   A4F5G6; A4F5G7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=RNA binding protein fox-1 homolog 2;
DE   AltName: Full=Fox-1 homolog B;
DE   AltName: Full=RNA-binding motif protein 9;
DE   AltName: Full=RNA-binding protein 9;
GN   Name=rbfox2; Synonyms=fox2, rbm9;
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] (ISOFORMS 1 AND 2), AND INTERACTION WITH PAPD4.
RC   TISSUE=Oocyte;
RX   PubMed=18177378; DOI=10.1111/j.1742-4658.2007.06216.x;
RA   Papin C., Rouget C., Mandart E.;
RT   "Xenopus Rbm9 is a novel interactor of XGld2 in the cytoplasmic
RT   polyadenylation complex.";
RL   FEBS J. 275:490-503(2008).
CC   -!- FUNCTION: RNA-binding protein that regulates alternative splicing
CC       events by binding to 5'-UGCAUGU-3' elements. Regulates alternative
CC       splicing of tissue-specific exons (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with papd4/gld2. {ECO:0000269|PubMed:18177378}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A4F5G6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A4F5G6-2; Sequence=VSP_030901;
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DR   EMBL; AM419007; CAL91350.1; -; mRNA.
DR   EMBL; AM419008; CAL91351.1; -; mRNA.
DR   RefSeq; NP_001085103.2; NM_001091634.2. [A4F5G6-1]
DR   AlphaFoldDB; A4F5G6; -.
DR   SMR; A4F5G6; -.
DR   DNASU; 432174; -.
DR   GeneID; 432174; -.
DR   KEGG; xla:432174; -.
DR   CTD; 432174; -.
DR   Xenbase; XB-GENE-6255985; rbfox2.L.
DR   OrthoDB; 871288at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 432174; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043484; P:regulation of RNA splicing; IEA:InterPro.
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; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..411
FT                   /note="RNA binding protein fox-1 homolog 2"
FT                   /id="PRO_0000317117"
FT   DOMAIN          173..249
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          16..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            174
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            182
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            183
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            207
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            212
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            216
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            240
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            250
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         281..282
FT                   /note="AV -> AAAPGLQADVSLATEAGVPLPGPRGVNTYIPLII (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:18177378"
FT                   /id="VSP_030901"
SQ   SEQUENCE   411 AA;  43566 MW;  32FCB46A2F1DED6F CRC64;
     MADAVMSDAH LLGFNTRGTK RESDQQLHLG SSGASGAGVK RQRVEPEQQE PGNPMSMPVS
     QAYQGFAPLN SQGNQEPTAT PDTMVQPFAA IPFPPPPQNG LSTDYGSQHT QDYATQSTEH
     GIPLYGGGQS LAEHSAPATS TANASSTTDG SQTEGQQSQS QNNENSETKA SPKRLHVSNI
     PFRFRDPDLR QMFGQFGKIL DVEIIFNERG SKGFGFVTFE TSADADRARE KLHSTVVEGR
     KIEVNNATAR VMTNKKSVTP YGNGWKLSPV VGAVYGPELY AVPGFPYPTA AAAATTAAAF
     RGAHLRGRGR TVYGAVRAVP PTAIPTYPGV LYQDGFYGTE LYGGYAAYRY AQPATAATAA
     TAAAAAAAAY SDGYGRVYTA DPYHTLAPAT SYGVGAVASL YRGGYSRFAP Y