FXR1_BOVIN
ID FXR1_BOVIN Reviewed; 621 AA.
AC Q2TBT7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=RNA-binding protein FXR1 {ECO:0000305};
GN Name=FXR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein required for embryonic and postnatal
CC development of muscle tissue. May regulate intracellular transport and
CC local translation of certain mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FMR1. Interacts with FRX2. Interacts with
CC TDRD3. Interacts with HABP4. Interacts with CYFIP2 but not with CYFIP1.
CC {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR EMBL; BC109677; AAI09678.1; -; mRNA.
DR RefSeq; NP_001033651.1; NM_001038562.2.
DR AlphaFoldDB; Q2TBT7; -.
DR SMR; Q2TBT7; -.
DR STRING; 9913.ENSBTAP00000021880; -.
DR PaxDb; Q2TBT7; -.
DR PRIDE; Q2TBT7; -.
DR GeneID; 536793; -.
DR KEGG; bta:536793; -.
DR CTD; 8087; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR InParanoid; Q2TBT7; -.
DR OrthoDB; 374073at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:1902737; C:dendritic filopodium; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0044326; C:dendritic spine neck; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR022034; FXMRP1_C_core.
DR InterPro; IPR032172; FXR_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; IPR041560; Tudor_FRX1.
DR PANTHER; PTHR10603; PTHR10603; 2.
DR Pfam; PF05641; Agenet; 1.
DR Pfam; PF12235; FXMRP1_C_core; 2.
DR Pfam; PF16096; FXR_C1; 1.
DR Pfam; PF16097; FXR_C3; 1.
DR Pfam; PF00013; KH_1; 1.
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 Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW Isopeptide bond; Methylation; Myogenesis; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT CHAIN 2..621
FT /note="RNA-binding protein FXR1"
FT /id="PRO_0000254031"
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 381..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..457
FT /note="RNA-binding RGG-box"
FT REGION 545..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 68
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61584"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI81"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 447
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 447
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 453
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 453
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 455
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 455
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61584"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51116"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51114"
SQ SEQUENCE 621 AA; 69751 MW; D20B7FEDF7E5DE4A CRC64;
MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
VKKNTFFKCT VDVPEDLREA CANENAHKDY KKAVGACRIF YHPETTQLMI LSASEATVKR
VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS
DWSLAGEDDR ESRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL
DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY
ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDE ISKLQRTPGE
EKINTLKEEN TQDAAVLNGV S
