ID   RFOX1_MACFA             Reviewed;         376 AA.
AC   Q95KI0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 80.
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; ORFNames=QtrA-11594;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) 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}.
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DR   EMBL; AB060859; BAB46877.1; -; mRNA.
DR   AlphaFoldDB; Q95KI0; -.
DR   BMRB; Q95KI0; -.
DR   SMR; Q95KI0; -.
DR   STRING; 9541.XP_005591232.1; -.
DR   eggNOG; KOG0125; Eukaryota.
DR   eggNOG; KOG2346; Eukaryota.
DR   Proteomes; UP000233100; 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   Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..376
FT                   /note="RNA binding protein fox-1 homolog 1"
FT                   /id="PRO_0000317110"
FT   DOMAIN          119..195
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            120
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            128
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            129
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            153
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            158
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            162
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            186
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            196
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         319
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JJ43"
SQ   SEQUENCE   376 AA;  40565 MW;  DAA7A4D0D7B1030A CRC64;
     MEEKGSRMVQ QGNQEAAAAP DTMAQPYASA QFAPPQNGIP AEYTAPHPHP APEYTGQTTV
     PEHTLNLYPP AQTHSEQSPA DTNAQTVSGT ATQTDDAAPT DGQPQTQPSE NTENKSQPKR
     LHVSNIPFRF RDPDLRQMFG QFGKILDVEI IFNERGSKGF GFVTFENSAD ADRAREKLHG
     TVVEGRKIEV NNATARVMTN KKTVNPYTNG WKLNPVVGAV YSPEFYAGTV LLCQANQEGS
     SMYSAPSSLV YTSAMPGFPY PAATAAAAYR GAHLRGRGRT VYNTFRAAAP PPPIPAYGGV
     VYQDGFYGAD IYGGYAAYRY AQPTPATAAA YSDRNQFVFV AADEISCNTS AVTDEFMLPT
     PTTTHLLQPP PTALVP