GenomeNet

Database: UniProt
Entry: A0A3Q7U6M5_VULVU
LinkDB: A0A3Q7U6M5_VULVU
Original site: A0A3Q7U6M5_VULVU 
ID   A0A3Q7U6M5_VULVU        Unreviewed;       568 AA.
AC   A0A3Q7U6M5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=RNA-binding protein FXR1 {ECO:0000256|ARBA:ARBA00034847};
GN   Name=FXR1 {ECO:0000313|RefSeq:XP_025863005.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025863005.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025863005.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025863005.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025863005.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm, Cytoplasmic
CC       ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Postsynapse
CC       {ECO:0000256|ARBA:ARBA00034110}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the FMR1 family.
CC       {ECO:0000256|ARBA:ARBA00006633}.
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DR   RefSeq; XP_025863005.1; XM_026007220.1.
DR   AlphaFoldDB; A0A3Q7U6M5; -.
DR   SMR; A0A3Q7U6M5; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; 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; 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; 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:UP000286640};
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          380..568
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        496..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  63877 MW;  417233ECD6CBFB07 CRC64;
     MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
     EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
     VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
     VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
     IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
     GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
     VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EKEKGYATDE STVSSVQGSR SYSGRGRGRR
     GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE SRHQRDSRRR PGGRGRSVSG
     GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT
     DEDAVLMDGM TESDTASVNE NGLGKRCD
//
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