FMR1B_XENLA
ID FMR1B_XENLA Reviewed; 564 AA.
AC Q2KHP9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Fragile X messenger ribonucleoprotein 1 homolog B {ECO:0000250|UniProtKB:Q06787};
DE AltName: Full=xFMR1-B {ECO:0000305};
GN Name=fmr1-b {ECO:0000250|UniProtKB:Q06787};
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:AAI12953.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye {ECO:0000312|EMBL:AAI12953.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}. Cytoplasm,
CC Stress 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}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
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DR EMBL; BC112952; AAI12953.1; -; mRNA.
DR RefSeq; NP_001089964.1; NM_001096495.1.
DR AlphaFoldDB; Q2KHP9; -.
DR SMR; Q2KHP9; -.
DR DNASU; 735034; -.
DR GeneID; 735034; -.
DR KEGG; xla:735034; -.
DR CTD; 735034; -.
DR Xenbase; XB-GENE-977118; fmr1.S.
DR OMA; WKAIIKM; -.
DR OrthoDB; 374073at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 735034; Expressed in testis and 19 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; ISS: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: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:0043005; C:neuron projection; ISS:UniProtKB.
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; ISS: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:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
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: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; 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 Cell membrane; Cell projection; Centromere; Chromosome; Cytoplasm;
KW Membrane; mRNA processing; mRNA splicing; mRNA transport; Neurogenesis;
KW Nucleus; Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
KW Ribonucleoprotein; RNA-binding; Synapse; Synaptosome;
KW Translation regulation; Transport.
FT CHAIN 1..564
FT /note="Fragile X messenger ribonucleoprotein 1 homolog B"
FT /id="PRO_0000245322"
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 377..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..481
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000255"
FT REGION 529..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63858 MW; 5ABAD5631F437DCC CRC64;
MEELAVEVRG SNGAFYKAFV KDVHEDSITV TFENNWQQEK QIPFHDVRFP PPSGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTID RLRSVNPNKS
ATKNSFHKVK LDVPEDLRQM CAKDSAHKDF KKAVGAFSVS YDSENYQLVI LSVNEVTIKR
ANMLCDMHFR SLRTKLSLML RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQE AVKKARTYLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENDKNISQEE GNVPFVFVGT KDSITNATVL LDYHLNYLKE
VDQLRLERLQ IDEQLRQIGA SSRPPSNRPD KEKGYLSEDC SGTVRGSRPY NNRGRSRRGT
GYASGTNSEA SNASETESDH RDELSDWSLA PAEDDRDNYH RRGDGRRRGG MRGQGMRGRG
GFKGNDDQPR PDNRQRNSRE TKARTSDGSL QIRIDCNNER SVHTKTLQNA SVEGSRLRTG
KDRIQKKEKT DGVDGPQVVV NGVP
