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RFOX1_PONAB
ID   RFOX1_PONAB             Reviewed;         382 AA.
AC   Q5NVN8; Q5R948;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=RNA binding protein fox-1 homolog 1;
DE   AltName: Full=Ataxin-2-binding protein 1;
DE   AltName: Full=Fox-1 homolog A;
GN   Name=RBFOX1; Synonyms=A2BP1, FOX1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. 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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the C-terminus of ATXN2. {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=Q5NVN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5NVN8-2; Sequence=VSP_030885, VSP_030886;
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DR   EMBL; CR859547; CAH91712.1; -; mRNA.
DR   EMBL; CR925977; CAI29625.1; -; mRNA.
DR   RefSeq; NP_001125995.1; NM_001132523.1.
DR   AlphaFoldDB; Q5NVN8; -.
DR   BMRB; Q5NVN8; -.
DR   SMR; Q5NVN8; -.
DR   STRING; 9601.ENSPPYP00000008003; -.
DR   GeneID; 100172936; -.
DR   KEGG; pon:100172936; -.
DR   CTD; 54715; -.
DR   eggNOG; KOG0125; Eukaryota.
DR   InParanoid; Q5NVN8; -.
DR   OrthoDB; 871288at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..382
FT                   /note="RNA binding protein fox-1 homolog 1"
FT                   /id="PRO_0000317111"
FT   DOMAIN          117..193
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            118
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            126
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            127
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            151
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            156
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            160
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            184
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         317
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JJ43"
FT   VAR_SEQ         1
FT                   /note="M -> METGQRTHASGTYSFLDRTQHSDIKADCSTCVEIEDRKVSRQQM
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_030885"
FT   VAR_SEQ         332..382
FT                   /note="SYGRVYAADPYHHALAPAPTYGVGAMPQGSSPSTDFRGAKLHTSRPLLSGS
FT                   -> RNQFVFVAADEISCNTSAVTDEFMLPTPTTTHLLQPPPTALVPCPKVPAPAQTSEE
FT                   LSCTLPGLCCQAAENLTASPPLLQFMFKVIVAQERK (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_030886"
FT   CONFLICT        152
FT                   /note="E -> G (in Ref. 1; CAH91712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  41024 MW;  5832284AA1B2C006 CRC64;
     MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPE
     HTLNLYPPAQ THSEQSPADT SAQTVSGTAT QTDDAAPTDG QPQTQPSENT ENKSQPKRLH
     VSNIPFRFRD PDLRQMFGQF GKILDVEIIF NERGSKGFGF VTFENSADAD RAREKLHGTV
     VEGRKIEVNN ATARVMTNKK TVNPYTNGWK LNPVVGAVYS PEFYAGTVLL CQANQEGSSM
     YSAPSSLVYT SAMPGFPYPA ATAAAAYRGA HLRGRGRTVY NTFRAAAPPP PIPAYGGVVY
     QDGFYGADIY GGYAAYRYAQ PTPATAAAYS DSYGRVYAAD PYHHALAPAP TYGVGAMPQG
     SSPSTDFRGA KLHTSRPLLS GS
 
 
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