ID   FXR1B_XENLA             Reviewed;         675 AA.
AC   Q7ZTQ5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=RNA-binding protein fxr1-B {ECO:0000305};
DE   AltName: Full=xFxr1p-B;
GN   Name=fxr1-b; Synonyms=fxr1h;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH43638.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH43638.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding protein. Binds poly(G) and poly(U) but not
CC       poly(A) or poly(C). Regulates somite formation, probably by regulating
CC       gene expression (By similarity). {ECO:0000250|UniProtKB:P51115}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5BJ56}. Nucleus
CC       {ECO:0000250|UniProtKB:Q5BJ56}.
CC   -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC043638; AAH43638.1; -; mRNA.
DR   RefSeq; NP_001080422.1; NM_001086953.1.
DR   AlphaFoldDB; Q7ZTQ5; -.
DR   SMR; Q7ZTQ5; -.
DR   BioGRID; 98356; 1.
DR   IntAct; Q7ZTQ5; 1.
DR   DNASU; 380114; -.
DR   GeneID; 380114; -.
DR   KEGG; xla:380114; -.
DR   CTD; 380114; -.
DR   Xenbase; XB-GENE-1004715; fxr1.S.
DR   OrthoDB; 374073at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 380114; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0003723; F:RNA binding; 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; ISS:UniProtKB.
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; 1.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXMRP1_C_core; 1.
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   Cytoplasm; Developmental protein; Differentiation; Myogenesis; Nucleus;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..675
FT                   /note="RNA-binding protein fxr1-B"
FT                   /id="PRO_0000245324"
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..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..485
FT                   /note="RNA-binding RGG-box"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        437..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  76212 MW;  80EF72FACF7110D8 CRC64;
     MEDLTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRMP PLPDIKKEIT
     EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKS
     VTKNSFFKCT VDVPEDLRES CSNENVHKEF KKAVGACRVY FHAETNQLII LSASESTVKR
     VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLASAFH EEFDVREDLM GLAIGTHGSN
     IQQARKVPGI TAIELDEDSG TFRIYGESEE AVKKARSYLE FVEDFIQVPR NLVGKVIGKN
     GKVIQEIVDK SGVVRVRIEG DNETKLPRED GMVPFVFVGT KENIGNVQVL LEYHIAYLKE
     VEQLRMERLQ IDEQLRQIGM GFRPSSRGTE KEKGYVTDES AASSVRGSRS YSGRGRGRRG
     PNYTSGYGTN SELSNTSETE SERKEELSDW SLAGEDEREG RQQRDSRRRP GGRGRSGSAG
     RGRGGSRGGK SSISSVLKDP DSNPYSLLDN TESDQTADTD ASDSHHNANR RRRSRRRRTD
     EDSSLMDGMT ESDNASVNEN GLDDSEQKPQ RRNRSRRRRF RGQAEDRQPV TVADYISRAE
     SQSRQRNLPK ETLENGKKEK VKDVIEEHGP SEKVINGPRA TSADRALKPQ TTPTERNNAS
     CQDGSKQEAI LNGVS