RFOX2_RAT
ID RFOX2_RAT Reviewed; 432 AA.
AC A1A5R1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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. Seems to act as a coregulatory factor of ER-alpha (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ER-alpha N-terminal activation domain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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DR EMBL; BC128766; AAI28767.1; -; mRNA.
DR RefSeq; NP_001073364.1; NM_001079895.1.
DR AlphaFoldDB; A1A5R1; -.
DR SMR; A1A5R1; -.
DR BioGRID; 263851; 1.
DR STRING; 10116.ENSRNOP00000063462; -.
DR PhosphoSitePlus; A1A5R1; -.
DR jPOST; A1A5R1; -.
DR PaxDb; A1A5R1; -.
DR PeptideAtlas; A1A5R1; -.
DR PRIDE; A1A5R1; -.
DR Ensembl; ENSRNOT00000066431; ENSRNOP00000063462; ENSRNOG00000004688.
DR GeneID; 362950; -.
DR KEGG; rno:362950; -.
DR UCSC; RGD:1311838; rat.
DR CTD; 23543; -.
DR RGD; 1311838; Rbfox2.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000157534; -.
DR HOGENOM; CLU_048440_0_1_1; -.
DR InParanoid; A1A5R1; -.
DR OrthoDB; 871288at2759; -.
DR PhylomeDB; A1A5R1; -.
DR TreeFam; TF315942; -.
DR Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR PRO; PR:A1A5R1; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004688; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; A1A5R1; baseline and differential.
DR Genevisible; A1A5R1; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; ISO:RGD.
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; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..432
FT /note="RNA binding protein fox-1 homolog 2"
FT /id="PRO_0000317116"
FT DOMAIN 163..239
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 164
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 202
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 206
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 230
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 240
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 339
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 371
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43251"
FT MOD_RES 423
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 423
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 428
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 428
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
SQ SEQUENCE 432 AA; 45550 MW; E7CA07BB0DBA16B1 CRC64;
MAEGGQAQQQ PPQLGPGAAA RGMKRESEVE LPVPGAGADG PEPGLSKRPR TEEAADEGMQ
GNQEPTTTPD AMVQPFTTIP FPPPPQNGIP TEYGVPHTQD YAGQTSEHNL TLYGSSQPHG
EQSSNSPSNQ NGSLTQTEGG AQTDGQQSQT QSSENSESKS TPKRLHVSNI PFRFRDPDLR
QMFGQFGKIL DVEIIFNERG SKGFGFVTFE NSADADRARE KLHGTVVEGR KIEVNNATAR
VMTNKKMVTP YANGWKLSPV VGAVYGPELY AASSFQADVS LGNEAAVPLS GRGGINTYIP
LISLPLVPGF PYPTAATTAA AFRGAHLRGR GRTVYGAVRA VPPTAIPAYP GVVYQDGFYG
ADLYGGYAAY RYAQPATATA ATAAAAAAAA YSDGYGRVYT ADPYHALAPA ASYGVGAVAS
LYRGGYSRFA PY
