FMR1_XENTR
ID FMR1_XENTR Reviewed; 590 AA.
AC Q6GLC9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Fragile X messenger ribonucleoprotein 1 homolog {ECO:0000250|UniProtKB:Q06787};
DE AltName: Full=XtFmrp {ECO:0000305};
GN Name=fmr1 {ECO:0000250|UniProtKB:Q06787, ECO:0000303|PubMed:15968590};
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:AAH74570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP 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: Multifunctional polyribosome-associated RNA-binding protein
CC that plays a central role in neuronal development and synaptic
CC plasticity through the regulation of alternative mRNA splicing, mRNA
CC stability, mRNA dendritic transport and postsynaptic local protein
CC synthesis of a subset of mRNAs. Binds poly(G) and poly(U), and to a
CC lower extent poly(A) and poly(C). {ECO:0000250|UniProtKB:P35922,
CC ECO:0000250|UniProtKB:P51113, ECO:0000250|UniProtKB:Q06787,
CC ECO:0000250|UniProtKB:Q80WE1}.
CC -!- SUBUNIT: Homodimer. Heterodimer. {ECO:0000250|UniProtKB:Q06787}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P35922}. Chromosome
CC {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip
CC {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic
CC cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane
CC {ECO:0000250|UniProtKB:P35922}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q06787}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6GLC9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15968590};
CC IsoId=Q6GLC9-2; Sequence=VSP_052084;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously throughout the embryo. Shows
CC tissue-specific expression in adults, being abundant in most neurons of
CC the central nervous system (CNS) and in all spermatogenic cells of the
CC testis. {ECO:0000269|PubMed:15968590}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
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DR EMBL; BC074570; AAH74570.1; -; mRNA.
DR RefSeq; NP_001005454.1; NM_001005454.1. [Q6GLC9-1]
DR AlphaFoldDB; Q6GLC9; -.
DR SMR; Q6GLC9; -.
DR STRING; 8364.ENSXETP00000015179; -.
DR PaxDb; Q6GLC9; -.
DR DNASU; 448049; -.
DR GeneID; 448049; -.
DR KEGG; xtr:448049; -.
DR CTD; 2332; -.
DR Xenbase; XB-GENE-977113; fmr1.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR HOGENOM; CLU_020699_4_0_1; -.
DR InParanoid; Q6GLC9; -.
DR OMA; WKAIIKM; -.
DR OrthoDB; 374073at2759; -.
DR PhylomeDB; Q6GLC9; -.
DR TreeFam; TF105427; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000019647; Expressed in brain and 12 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0010369; C:chromocenter; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:1902737; C:dendritic filopodium; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0044326; C:dendritic spine neck; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:1990812; C:growth cone filopodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
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:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0021905; P:forebrain-midbrain boundary formation; IEA:Ensembl.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0014036; P:neural crest cell fate specification; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0090365; P:regulation of mRNA modification; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0060538; P:skeletal muscle organ development; ISS:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR032196; FXMR_C2.
DR InterPro; IPR022034; FXMRP1_C_core.
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; PF16098; FXMR_C2; 1.
DR Pfam; PF12235; FXMRP1_C_core; 2.
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 Alternative splicing; Cell membrane; Cell projection; Centromere;
KW Chromosome; Cytoplasm; Membrane; mRNA processing; mRNA splicing;
KW mRNA transport; Neurogenesis; Nucleus; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
KW Synapse; Synaptosome; Translation regulation; Transport.
FT CHAIN 1..590
FT /note="Fragile X messenger ribonucleoprotein 1 homolog"
FT /id="PRO_0000245323"
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 376..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..507
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000255"
FT COMPBIAS 400..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 425..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15968590"
FT /id="VSP_052084"
SQ SEQUENCE 590 AA; 67130 MW; 3C6F9A2B0A33D0E8 CRC64;
MEELAVEVRG SNGAFYKAFV KDVHEDSITV TFENNWQQER QIPFHDVRFP PPSGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKNSFHKVK LDVPEDLRQM CAKDSAHKDF KKAVGAFSVS YDSENYQLVI LSVNEVTIKR
ANMLSDMHFR SLRTKLSLML RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQE AVKKARTYLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENDKNISPEE GMVPFVFVGT KDSITNATVL LDYHLNYLKE
VDQLRLERLQ IDEQLRQIGA SSRPPPNRPD KEKGYQSEDL SGTGRGSRPY NNRGRSRRGT
GYASDIRYGD PDYRKTTYPE YPRSQAFWIK GTNSEASNAS ETESDHRDEL SDWSLAPAED
DRDNYHRRGD GRRRGGPRGQ GMRGRGGFKG NDDQPRPDNR QRNSRETKAR TSDGSLQIRI
DCNNERSVHT KTLQNASVEG SRLRTGKDRV QKKEKSEVVD GPQVVVNGIP
