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Database: UniProt
Entry: A0A2K6KGK0_RHIBE
LinkDB: A0A2K6KGK0_RHIBE
Original site: A0A2K6KGK0_RHIBE 
ID   A0A2K6KGK0_RHIBE        Unreviewed;       595 AA.
AC   A0A2K6KGK0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Fragile X messenger ribonucleoprotein 1 {ECO:0000313|Ensembl:ENSRBIP00000010402.1};
GN   Name=FMR1 {ECO:0000313|Ensembl:ENSRBIP00000010402.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000010402.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000010402.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000010402.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection,
CC       dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic
CC       spine {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium tip
CC       {ECO:0000256|ARBA:ARBA00004495}. Cell projection, growth cone
CC       {ECO:0000256|ARBA:ARBA00004624}. Cell projection, neuron projection
CC       {ECO:0000256|ARBA:ARBA00004487}. Chromosome, centromere
CC       {ECO:0000256|ARBA:ARBA00004584}. Cytoplasm, Cytoplasmic
CC       ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Cytoplasm,
CC       perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome
CC       {ECO:0000256|ARBA:ARBA00034102}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034109}.
CC   -!- SIMILARITY: Belongs to the FMR1 family.
CC       {ECO:0000256|ARBA:ARBA00006633}.
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DR   AlphaFoldDB; A0A2K6KGK0; -.
DR   SMR; A0A2K6KGK0; -.
DR   STRING; 61621.ENSRBIP00000010402; -.
DR   Ensembl; ENSRBIT00000034029.1; ENSRBIP00000010402.1; ENSRBIG00000028998.1.
DR   GeneTree; ENSGT00950000183189; -.
DR   OMA; ASKQLEX; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0071598; C:neuronal ribonucleoprotein granule; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032797; C:SMN complex; IEA:Ensembl.
DR   GO; GO:0002151; F:G-quadruplex RNA binding; IEA:Ensembl.
DR   GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR   GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR   GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; IEA:Ensembl.
DR   GO; GO:0008143; F:poly(A) binding; IEA:Ensembl.
DR   GO; GO:0034046; F:poly(G) binding; IEA:Ensembl.
DR   GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR   GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR   GO; GO:0033592; F:RNA strand annealing activity; IEA:Ensembl.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; IEA:Ensembl.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR   GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
DR   GO; GO:0030371; F:translation repressor activity; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR   GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR   GO; GO:0044830; P:modulation by host of viral RNA genome replication; IEA:Ensembl.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR   GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IEA:Ensembl.
DR   GO; GO:1902373; P:negative regulation of mRNA catabolic process; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:1901254; P:positive regulation of intracellular transport of viral material; IEA:Ensembl.
DR   GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IEA:Ensembl.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:0060998; P:regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0098908; P:regulation of neuronal action potential; IEA:Ensembl.
DR   GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
DR   CDD; cd22509; KH_I_FMR1_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR   InterPro; IPR040148; FMR1.
DR   InterPro; IPR022034; FMR1-like_C_core.
DR   InterPro; IPR032196; FMR1_C2.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR047440; KH_I_FMR1_rpt2.
DR   PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR   PANTHER; PTHR10603:SF4; SYNAPTIC FUNCTIONAL REGULATOR FMR1; 1.
DR   Pfam; PF16098; FXMR_C2; 1.
DR   Pfam; PF12235; FXMRP1_C_core; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   SMART; SM00322; KH; 2.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT   DOMAIN          173..239
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          240..339
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          78..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..96
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  66914 MW;  ED302206B9A4E19D CRC64;
     MEELVVEVRG SNGAFYKVLD SRPERQIPFH DVRFPPPVGY NKDINESDEV EVSFPCHKPC
     CWWLAKVRMI KGEKCPQIER QKKKKKKTKK KLRSVNPNKP ATKDTFHIRI QTGTLKRQFG
     AFSVTYDPEN FTCHFGDEVT SSRAHMLIEC TFGLIKCIYQ TCISLQSSRQ LASRFHEQFI
     VREDLMGLAI GTHGANIQQA RKVPGVTAID LDEDTCTFHI YGEDQDAVKK ARSFLEFAED
     VIQVPRNLVG KVIGKNGKLI QEIVDKSGVV RVRIEAENEK NVPQEEEIIP PNSLPSNNSR
     VGPNAPEEKK HLDIKENSTH FSQPNSTKVQ RVLVASSVVA GESQKPELKA WQVGEHSLRR
     YGTICFVGTK DSIANATVLL DYHLNYLKEV DQLRLERLQI DEQLRQIGAS SRPPPNRTDK
     EKSYVTDDGQ GMGRGSRPYR NRGHGRRGPG YTSGTNSEAS NASETESDHR DELSDWSLAP
     TEEERENFLR RGDGRRRGGG GRGQGGRGRG GGFKGNDDHS RTDNRPRNPR EAKGRTTDGS
     LQIRVDCNNE RSVHTKTLQN TSSEGNRLRT GKDRNQKKEK PDTVDGQQPL VNGVP
//
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