FXR1A_XENLA
ID FXR1A_XENLA Reviewed; 676 AA.
AC P51115; Q4PJJ9; Q6GNP7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RNA-binding protein fxr1-A {ECO:0000305};
DE AltName: Full=xFxr1p-A;
GN Name=fxr1-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND RNA-BINDING.
RC TISSUE=Ovary;
RX PubMed=7781595; DOI=10.1002/j.1460-2075.1995.tb07237.x;
RA Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L.,
RA Dreyfuss G.;
RT "FXR1, an autosomal homolog of the fragile X mental retardation gene.";
RL EMBO J. 14:2401-2408(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic tail;
RX PubMed=16000371; DOI=10.1091/mbc.e05-04-0304;
RA Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T.,
RA Khandjian E.W.;
RT "The RNA-binding protein Fragile X-related 1 regulates somite formation in
RT Xenopus laevis.";
RL Mol. Biol. Cell 16:4350-4361(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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. {ECO:0000269|PubMed:16000371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P51115-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51115-2; Sequence=VSP_019707;
CC Name=3;
CC IsoId=P51115-3; Sequence=VSP_019706, VSP_019708;
CC -!- TISSUE SPECIFICITY: During embryogenesis, isoform 2 is present from
CC fertilization (stage 0) whereas isoform 1 is first present after stage
CC 30. In the tadpole (stage 36), isoform 1 shows high expression in
CC somites forming the caudal muscle and low expression in the eye. In
CC adults, isoform 1 is expressed in heart and muscle, whereas isoform 2
CC is expressed in the brain, liver and kidney.
CC {ECO:0000269|PubMed:16000371}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR EMBL; U25163; AAC59682.1; -; mRNA.
DR EMBL; DQ083374; AAY79165.1; -; mRNA.
DR EMBL; DQ083375; AAY79166.1; -; mRNA.
DR EMBL; BC073457; AAH73457.1; -; mRNA.
DR RefSeq; NP_001081786.1; NM_001088317.1. [P51115-1]
DR RefSeq; XP_018117202.1; XM_018261713.1. [P51115-1]
DR AlphaFoldDB; P51115; -.
DR SMR; P51115; -.
DR MaxQB; P51115; -.
DR PRIDE; P51115; -.
DR DNASU; 398050; -.
DR GeneID; 398050; -.
DR KEGG; xla:398050; -.
DR CTD; 398050; -.
DR Xenbase; XB-GENE-6252042; fxr1.L.
DR OMA; DQQQRGY; -.
DR OrthoDB; 374073at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398050; 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; IDA: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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Myogenesis; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..676
FT /note="RNA-binding protein fxr1-A"
FT /id="PRO_0000050108"
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..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..486
FT /note="RNA-binding RGG-box"
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 596..610
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 642..676
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|PubMed:16000371,
FT ECO:0000303|PubMed:7781595"
FT /id="VSP_019707"
FT VAR_SEQ 564..574
FT /note="DDSEQKPQRRN -> GQYMRTIVHYR (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019706"
FT VAR_SEQ 575..676
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019708"
FT CONFLICT 84
FT /note="V -> A (in Ref. 1; AAC59682)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> R (in Ref. 1; AAC59682)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="G -> R (in Ref. 1; AAC59682)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> L (in Ref. 1; AAC59682)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="Missing (in Ref. 1; AAC59682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 76213 MW; 87B3394379AD5F60 CRC64;
MEDMTVEVRG SNGAFYKGFV KDVHEDSLTV VFENNWQPER QVPFDEVRMP PLPDIKKEIT
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
VTKNSFFKCT VDVPEDLRES CSNENVHKEF KKAVGACRVY FHAETNQLII LSACESTVKR
VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLASAFH EEFIVREDLM GLAIGTHGSN
IQQARKVPGI TAIELDEDSG TFRIYGESAE AVKKARSYLE FVEDFIQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNETKLPRED GMVPFVFVGT KENIGNVQVL 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 KETLAKGKKE KVKDVIEEHG PSEKVINGPR ASSADKASNP QTASTERNQA
SCQDGSKQEA IMNGVS
