ID   RFOX3_BOVIN             Reviewed;         328 AA.
AC   Q0VD23;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=RNA binding protein fox-1 homolog 3;
DE   AltName: Full=Fox-1 homolog C;
GN   Name=RBFOX3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pre-mRNA alternative splicing regulator. Regulates
CC       alternative splicing of RBFOX2 to enhance the production of mRNA
CC       species that are targeted for nonsense-mediated decay (NMD).
CC       {ECO:0000250|UniProtKB:Q8BIF2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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DR   EMBL; BC119875; AAI19876.1; -; mRNA.
DR   RefSeq; NP_001069005.1; NM_001075537.1.
DR   RefSeq; XP_005221252.1; XM_005221195.3.
DR   AlphaFoldDB; Q0VD23; -.
DR   SMR; Q0VD23; -.
DR   Ensembl; ENSBTAT00000008241; ENSBTAP00000008241; ENSBTAG00000006280.
DR   GeneID; 511773; -.
DR   KEGG; bta:511773; -.
DR   CTD; 146713; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006280; -.
DR   VGNC; VGNC:33779; RBFOX3.
DR   GeneTree; ENSGT00940000159924; -.
DR   HOGENOM; CLU_048440_0_0_1; -.
DR   InParanoid; Q0VD23; -.
DR   OMA; MLAWHPA; -.
DR   OrthoDB; 871288at2759; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000006280; Expressed in prefrontal cortex and 74 other tissues.
DR   ExpressionAtlas; Q0VD23; 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   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR025670; Fox-1_C_dom.
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   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..328
FT                   /note="RNA binding protein fox-1 homolog 3"
FT                   /id="PRO_0000349206"
FT   DOMAIN          99..172
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            100
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            108
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            133
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            138
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            145
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         192
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIF2"
FT   MOD_RES         192
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIF2"
FT   MOD_RES         288
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIF2"
SQ   SEQUENCE   328 AA;  35468 MW;  2DCE0793DFEA58C5 CRC64;
     MAQPYPPAQY PPPPQNGIPA EYAPPPPHPT PDYSGQTPVP PEHGMTLYTP AQTHPEQPSS
     DTSTQPITGA QTVPQTDEAA QTDSQPLHPS DPTEKQQPKR LHVSNIPFRF RDPDLRQMFG
     QFGKILDVEI IFNERGSKVN NATARVMTNK KTANPYTNGW KLNPVVGAVY GPEFYAVTGF
     PYPTTGTAVA YRGAHLRGRG RAVYNTFRAA PPPPPIPTYG AALEQTLVKM PVPWAGLAPC
     PLPPQQTPEP AYPTSPAFPP LSCPFASRVV YQDGFYGAEI YGGYAAYRYA QPAAAAAAYS
     DSYGRVYAAA DPYHHTIGPA ATYSIGTM