ID A0A7J8EJ01_ROUAE Unreviewed; 611 AA.
AC A0A7J8EJ01;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=Fragile X messenger ribonucleoprotein 1 {ECO:0000256|ARBA:ARBA00067715};
DE AltName: Full=Fragile X messenger ribonucleoprotein {ECO:0000256|ARBA:ARBA00081016};
GN ORFNames=HJG63_005215 {ECO:0000313|EMBL:KAF6435410.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6435410.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6435410.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6435410.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6435410.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium tip
CC {ECO:0000256|ARBA:ARBA00004495}. Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Cytoplasm, Stress granule
CC {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. 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}.
CC -!- SIMILARITY: Belongs to the FMR1 family.
CC {ECO:0000256|ARBA:ARBA00006633}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6435410.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JACASE010000009; KAF6435410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8EJ01; -.
DR CTD; 2332; -.
DR OrthoDB; 424249at2759; -.
DR Proteomes; UP000593571; Unassembled WGS sequence.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
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:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:TreeGrafter.
DR GO; GO:0045182; F:translation regulator activity; IEA:TreeGrafter.
DR GO; GO:0048513; P:animal organ development; IEA:TreeGrafter.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:TreeGrafter.
DR GO; GO:0045727; P:positive regulation of translation; IEA:TreeGrafter.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:TreeGrafter.
DR GO; GO:0099577; P:regulation of translation at presynapse, modulating synaptic transmission; IEA:TreeGrafter.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd22506; KH_I_FMR1_rpt1; 1.
DR CDD; cd22509; KH_I_FMR1_rpt2; 1.
DR CDD; cd22512; KH_I_FMR1_rpt3; 1.
DR CDD; cd20471; Tudor_Agenet_FMR1_rpt1; 1.
DR CDD; cd20474; Tudor_Agenet_FMR1_rpt2; 1.
DR FunFam; 2.30.30.140:FF:000001; Fragile X mental retardation 1, isoform CRA_e; 1.
DR FunFam; 2.30.30.140:FF:000002; Fragile X mental retardation 1, isoform CRA_e; 1.
DR FunFam; 3.30.1370.10:FF:000004; Fragile X mental retardation 1, isoform CRA_e; 1.
DR FunFam; 3.30.1370.10:FF:000032; synaptic functional regulator FMR1 isoform X2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR022034; FMR1-like_C_core.
DR InterPro; IPR032196; FMR1_C2.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR047438; KH_I_FMR1_rpt1.
DR InterPro; IPR047440; KH_I_FMR1_rpt2.
DR InterPro; IPR047431; Tudor_Agenet_FMR1_rpt1.
DR InterPro; IPR047436; Tudor_Agenet_FMR1_rpt2.
DR InterPro; IPR041560; Tudor_FRM1.
DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR PANTHER; PTHR10603:SF4; FRAGILE X MESSENGER RIBONUCLEOPROTEIN 1; 1.
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; Eukaryotic type KH-domain (KH-domain type I); 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000593571};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 4..50
FT /note="Agenet-like"
FT /evidence="ECO:0000259|PROSITE:PS51641"
FT DOMAIN 63..115
FT /note="Agenet-like"
FT /evidence="ECO:0000259|PROSITE:PS51641"
FT REGION 325..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..463
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..480
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68911 MW; 016049E319E799BF CRC64;
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP PPVGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKDTFHKIK LDVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
AHMLIDMHFR SLRTKLSLIL RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPP SNSRIGPTPS EDKKHIDIKE
NSAHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL
RQIGASSRPP PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE
TESDHRDELS DWSLAPTEEE RENFLRRGEG RRRGGGGRGQ GGRGRGGGFK GNDDHSRTDN
RPRNPREAKG RTADGSLQIR VDCNNERSVH TKTLQNTSSE GNRLRTGKDR NQKKEKPDSV
DGPQPLVNGV P
//
