FXR1_XENTR
ID FXR1_XENTR Reviewed; 674 AA.
AC Q5BJ56; Q28C19;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=RNA-binding protein fxr1 {ECO:0000305};
DE AltName: Full=XtFxr1p;
GN Name=fxr1 {ECO:0000250|UniProtKB:P51115}; ORFNames=TEgg078n09.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ81473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAJ81473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-674 (ISOFORM 2).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH91614.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP IDENTIFICATION (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15968590; DOI=10.1387/ijdb.051974lb;
RA Blonden L., van 't Padje S., Severijnen L.-A., Destree O., Oostra B.A.,
RA Willemsen R.;
RT "Two members of the Fxr gene family, Fmr1 and Fxr1, are differentially
RT expressed in Xenopus tropicalis.";
RL Int. J. Dev. Biol. 49:437-441(2005).
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:0000269|PubMed:15968590}. Nucleus
CC {ECO:0000269|PubMed:15968590}. Note=Nuclear very early in embryonic
CC development (at two hours post-fertilization), becoming cytoplasmic in
CC later embryonic stages through to adulthood.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15968590};
CC IsoId=Q5BJ56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BJ56-2; Sequence=VSP_052085;
CC -!- TISSUE SPECIFICITY: Shows tissue-specific expression during embryonic
CC development. At stage 23, expressed preferentially in structures that
CC will develop into muscle (mesodermal) and neural (ectodermal) tissue.
CC From stage 37 onwards, highly expressed in neurons and skeletal muscle
CC tissue. Expression remains tissue-specific in adults, being localized
CC to neurons of the central nervous system (CNS), all spermatogenic cells
CC of the testis and skeletal muscle. Within skeletal muscle, expression
CC appears to be localized to costameres. {ECO:0000269|PubMed:15968590}.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ81473.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; CR942504; CAJ81473.1; ALT_SEQ; mRNA.
DR EMBL; BC091614; AAH91614.1; -; mRNA.
DR RefSeq; NP_001263426.1; NM_001276497.1.
DR RefSeq; NP_001263427.1; NM_001276498.1.
DR AlphaFoldDB; Q5BJ56; -.
DR SMR; Q5BJ56; -.
DR STRING; 8364.ENSXETP00000042154; -.
DR PaxDb; Q5BJ56; -.
DR GeneID; 594894; -.
DR KEGG; xtr:594894; -.
DR CTD; 8087; -.
DR Xenbase; XB-GENE-1004708; fxr1.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR InParanoid; Q5BJ56; -.
DR OrthoDB; 374073at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:1902737; C:dendritic filopodium; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0044326; C:dendritic spine neck; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
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:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
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; 1.
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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Myogenesis; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..674
FT /note="RNA-binding protein fxr1"
FT /id="PRO_0000245325"
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 380..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..486
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000255"
FT COMPBIAS 438..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 564..590
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052085"
SQ SEQUENCE 674 AA; 75903 MW; 5903EF9A5A34AC7A CRC64;
MEDLAVEVRG SNGAYYKGFV KDVHEDSLTV VFENNWQPER QVPFHEVRMP PLPDIKKEIT
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPGNQNKS
VTKSSFFKCT VDVPEDLREP CSNENVHKEF KKAVGACRVY FHAETNQLII LSACESTVKR
VTILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
IQQARKVPGI TAIELDEDSG TFRIYGESAE AVKKARSYLE FVEDFIQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNETKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
VEQLRMERLQ IDEQLRQIGM GFRPSSSRGT EKEKGYATDE STASSVRGSR SYSGRGRGRR
GPNYTSGYGT NSELSNPSET ESERKEELSD WSLAGEDERE SRQQRDSRRR PGGRGRSGSA
GRGRGGSRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHNTN RRRRSRRRRT
DEDSSLMDGM TESDNASVNE NGLDDSEQKP QRRNRSRRRR FRGQAEDRQP VTVADYISRA
ESQSRQRNLP KEPLAKGKKE KVKDVIEEHG PSEKVINGPR AASADKALKP QTTERNKASC
QDGSKQEAIL NGVS
