ID   FXR1_CRIGR              Reviewed;         621 AA.
AC   O70523;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RNA-binding protein FXR1 {ECO:0000305};
GN   Name=FXR1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9642279; DOI=10.1074/jbc.273.27.17122;
RA   Bolivar J., Guelman S., Iglesias C., Ortiz M., Valdivia M.M.;
RT   "The fragile-X-related gene FXR1 is a human autoantigen processed during
RT   apoptosis.";
RL   J. Biol. Chem. 273:17122-17127(1998).
CC   -!- FUNCTION: RNA-binding protein required for embryonic and postnatal
CC       development of muscle tissue. May regulate intracellular transport and
CC       local translation of certain mRNAs (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FMR1. Interacts with FRX2. Interacts with
CC       TDRD3. Interacts with HABP4. Interacts with CYFIP2 but not with CYFIP1.
CC       {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC       trimethylated histone peptides. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR   EMBL; Y12837; CAA73358.1; -; mRNA.
DR   RefSeq; NP_001233685.1; NM_001246756.1.
DR   AlphaFoldDB; O70523; -.
DR   SMR; O70523; -.
DR   STRING; 10029.NP_001233685.1; -.
DR   PRIDE; O70523; -.
DR   GeneID; 100689323; -.
DR   KEGG; cge:100689323; -.
DR   CTD; 8087; -.
DR   eggNOG; ENOG502QPKJ; Eukaryota.
DR   OrthoDB; 374073at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:InterPro.
DR   Gene3D; 3.30.1370.10; -; 2.
DR   InterPro; IPR008395; Agenet-like_dom.
DR   InterPro; IPR040148; FMR1.
DR   InterPro; IPR040472; FMRP_KH0.
DR   InterPro; IPR022034; FXMRP1_C_core.
DR   InterPro; IPR032172; FXR_C1.
DR   InterPro; IPR032177; FXR_C3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR041560; Tudor_FRX1.
DR   PANTHER; PTHR10603; PTHR10603; 2.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXMRP1_C_core; 2.
DR   Pfam; PF16096; FXR_C1; 1.
DR   Pfam; PF16097; FXR_C3; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF17904; KH_9; 1.
DR   Pfam; PF18336; Tudor_FRX1; 1.
DR   SMART; SM00322; KH; 2.
DR   SUPFAM; SSF54791; SSF54791; 2.
DR   PROSITE; PS51641; AGENET_LIKE; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW   Isopeptide bond; Methylation; Myogenesis; Phosphoprotein; Repeat;
KW   RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   CHAIN           2..621
FT                   /note="RNA-binding protein FXR1"
FT                   /id="PRO_0000050105"
FT   DOMAIN          4..50
FT                   /note="Agenet-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT   DOMAIN          63..115
FT                   /note="Agenet-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT   DOMAIN          222..251
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          285..314
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          381..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..457
FT                   /note="RNA-binding RGG-box"
FT   REGION          545..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         68
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61584"
FT   MOD_RES         401
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XI81"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         447
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         447
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         453
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         453
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         455
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         455
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P35922"
FT   MOD_RES         483
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61584"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51116"
FT   MOD_RES         587
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   MOD_RES         611
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
FT   CROSSLNK        56
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P51114"
SQ   SEQUENCE   621 AA;  69706 MW;  5BA1CC62BD1061B1 CRC64;
     MADVTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
     EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
     VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
     VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
     IQQARKVPGV TAIELDEDTG TFRIYGESAE AVKKARGFME FVEDFIQVPR NLVGKVIGKN
     GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
     VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS
     DWSLAGEDDR ETRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL
     DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY
     ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDE IPNVPRTPGE
     EKTKNLKEES TQEAAVLNGV S