ID M3XJC3_LATCH Unreviewed; 652 AA.
AC M3XJC3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=FMR1 autosomal homolog 1 {ECO:0000313|Ensembl:ENSLACP00000022829.1};
GN Name=FXR1 {ECO:0000313|Ensembl:ENSLACP00000022829.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022829.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022829.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000256|ARBA:ARBA00004331}.
CC -!- SIMILARITY: Belongs to the FMR1 family.
CC {ECO:0000256|ARBA:ARBA00006633}.
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DR EMBL; AFYH01036942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01036943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01036944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005991965.1; XM_005991903.2.
DR AlphaFoldDB; M3XJC3; -.
DR Ensembl; ENSLACT00000025815.1; ENSLACP00000022829.1; ENSLACG00000011290.2.
DR GeneID; 102366404; -.
DR CTD; 8087; -.
DR GeneTree; ENSGT00950000183189; -.
DR HOGENOM; CLU_020699_3_0_1; -.
DR OrthoDB; 2995592at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000011290; Expressed in post-anal tail muscle and 6 other cell types or tissues.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:InterPro.
DR CDD; cd22504; KH_I_FXR1_rpt1; 1.
DR CDD; cd22507; KH_I_FXR1_rpt2; 1.
DR CDD; cd22510; KH_I_FXR1_rpt3; 1.
DR CDD; cd20472; Tudor_Agenet_FXR1_rpt1; 1.
DR CDD; cd20475; Tudor_Agenet_FXR1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR022034; FMR1-like_C_core.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR032172; FXR1_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; IPR047494; KH_I_FXR1_rpt1.
DR InterPro; IPR047495; KH_I_FXR1_rpt2.
DR InterPro; IPR047496; KH_I_FXR1_rpt3.
DR InterPro; IPR047425; Tudor_Agenet_FXR1_rpt1.
DR InterPro; IPR047427; Tudor_Agenet_FXR1_rpt2.
DR InterPro; IPR041560; Tudor_FRM1.
DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR PANTHER; PTHR10603:SF6; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN 1; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}.
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 382..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 72454 MW; 92212606DDC978CB CRC64;
MEELTVEVRG SNGAFYKGFV KDVHDDSLTI VFENNWQPER QVPFSDVRLP PPSDVKKEIS
EGDEVEVFSR ANDQEPCGWW LAKVRMMKGD FYVIEYAACD ATYNEIVTYE RLRPVNQNSS
VTKSTFFKCT VAVPEDIKDV CANENAHKDF KKAIGACRIF YCAEENQLVI LSTNEATVKR
VSMLSDMHLR SIRTKIMLMS RNEEATKHLE STKQLAAAFH EEFTVREDLM GLAIGTHGSN
IQQARKVSGV TAIELDEDSG TFRIYGESAE AVSKARSYLE FVEDAVQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNDSKFPREE GMVPFIFVGT KECIGNVQVL LEYHIAYLKE
VEQLRMQRLQ IDEQLRQIGM GFRPSSSRVA EKDRGYTTDD STASSAHGTR SYSGRGRGRR
GPNYTSGYGT NSELSNASET DSERKDELSD WSLAGEDEKE TRQQRDSRRR PGGGRGRGGP
GSRGRGGSRG GGSSISSVLK DPDSNPYSLL DNTETDQTAD TDASDSHHNT NRRRRSRRRR
TDEDATLMDG MTESDNASVS ENGIVTVADY ISRAESQSRQ RNAPRENLAK NKKGMAQDVI
EEHSTSGNAL NGPCNASGDE SSKPLRTSKE RTQKGSYQGD GNQQQTMLNG VS
//
