RFOX2_BOVIN
ID RFOX2_BOVIN Reviewed; 394 AA.
AC A6QPR6; Q0V8B8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 61.
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 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] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-279 (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6QPR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6QPR6-2; Sequence=VSP_030887, VSP_030888;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49448.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC149447; AAI49448.1; ALT_INIT; mRNA.
DR EMBL; BT026301; ABG81457.1; -; mRNA.
DR AlphaFoldDB; A6QPR6; -.
DR SMR; A6QPR6; -.
DR STRING; 9913.ENSBTAP00000026808; -.
DR PaxDb; A6QPR6; -.
DR PRIDE; A6QPR6; -.
DR eggNOG; KOG0125; Eukaryota.
DR InParanoid; A6QPR6; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
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: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 Alternative splicing; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..394
FT /note="RNA binding protein fox-1 homolog 2"
FT /id="PRO_0000317114"
FT DOMAIN 129..205
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 130
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 139
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 163
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 206
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 301
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 333
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43251"
FT MOD_RES 385
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 385
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 390
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 390
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT VAR_SEQ 102
FT /note="T -> TQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_030887"
FT VAR_SEQ 268..269
FT /note="II -> ISLPLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_030888"
FT CONFLICT 1..10
FT /note="MGRLQMLKHK -> MSSDSMDQPRNPCE (in Ref. 1; AAI49448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 41972 MW; A7E599538D1F2214 CRC64;
MGRLQMLKHK NEPLTPGYHG FPTRDSQGNQ EPTTTPDAMV QPFTTIPFPP PPQNGIPTEY
GVPHTQDYAG QTSEHNLTLY GSTQAHGEQS SNSPSTQNGS LTTEGGAQTD GQQSQTQSSE
NSESKSTPKR LHVSNIPFRF RDPDLRQMFG QFGKILDVEI IFNERGSKGF GFVTFENSAD
ADRAREKLHG TVVEGRKIEV NNATARVMTN KKMVTPYANG WKLSPVVGAV YGPELYAASS
FQADVSLGND AAVPLSGRGG INTYIPLIIP GFPYPTAATT AAAFRGAHLR GRGRTVYGAV
RAVPPAAIPA YPGVVYQDGF YGADLYGGYA AYRYAQPATA TAATAAAAAA AAYSDGYGRV
YTADPYHALA PAASYGVGAV ASLYRGGYSR FAPY
