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RFOX2_XENTR
ID   RFOX2_XENTR             Reviewed;         380 AA.
AC   Q66JB7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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DR   EMBL; BC080984; AAH80984.1; -; mRNA.
DR   RefSeq; NP_001008085.1; NM_001008084.1.
DR   AlphaFoldDB; Q66JB7; -.
DR   SMR; Q66JB7; -.
DR   STRING; 8364.ENSXETP00000043659; -.
DR   DNASU; 493447; -.
DR   Ensembl; ENSXETT00000000477; ENSXETP00000000477; ENSXETG00000000231.
DR   GeneID; 493447; -.
DR   KEGG; xtr:493447; -.
DR   CTD; 23543; -.
DR   Xenbase; XB-GENE-489991; rbfox2.
DR   eggNOG; KOG0125; Eukaryota.
DR   HOGENOM; CLU_048440_0_1_1; -.
DR   InParanoid; Q66JB7; -.
DR   OrthoDB; 871288at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000231; Expressed in neurula embryo and 12 other tissues.
DR   ExpressionAtlas; Q66JB7; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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: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   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..380
FT                   /note="RNA binding protein fox-1 homolog 2"
FT                   /id="PRO_0000317118"
FT   DOMAIN          110..186
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            111
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            119
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            120
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            153
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            177
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            187
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40211 MW;  51EC40877A41BADB CRC64;
     MEKNKMVSQG NQEPTATPDT MVQPFAAIPF PPPPQNGLST DYGSQHTQEY ATQSTEHGIP
     LYGGGQSHAE HSTPATSTAN ASSTTDGSQT EGQQSQTQNS ENSESKPTPK RLHVSNIPFR
     FRDPDLRQMF GQFGKILDVE IIFNERGSKG FGFVTFETSA DADRAREKLH STVVEGRKIE
     VNNATARVMT NKKSVTPYGN GWKLSPVVGA VYGPELYAAA PGLQADVSLA TEAGVPLPGP
     RGVNTYIPLI IPGFPYPTAA AAATTAAAFR GAHLRGRGRT VYGAVRAVPP TAIPTYPGVL
     YQDGFYGTEL YGGYAAYRYT QPATAATAAT AAAAAAAAYS DGYGRVYTAD PYHALAPATS
     YGVGAVASLY RGGYSRFAPY
 
 
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