FXR1_RAT
ID FXR1_RAT Reviewed; 568 AA.
AC Q5XI81;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=RNA-binding protein FXR1 {ECO:0000305};
DE AltName: Full=FMR1 autosomal homolog 1 {ECO:0000312|RGD:1311733};
GN Name=Fxr1 {ECO:0000312|RGD:1311733};
GN Synonyms=Fxr1h {ECO:0000312|EMBL:AAH83807.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-398; SER-432; SER-435;
RP SER-438; SER-449; SER-452; THR-512 AND SER-514, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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).
CC {ECO:0000250|UniProtKB:Q61584}.
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|UniProtKB:P51114}.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein corresponds to isoform B in mouse and
CC isoform 2 in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
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DR EMBL; BC083807; AAH83807.1; -; mRNA.
DR RefSeq; NP_001012179.1; NM_001012179.2.
DR AlphaFoldDB; Q5XI81; -.
DR SMR; Q5XI81; -.
DR BioGRID; 263063; 2.
DR IntAct; Q5XI81; 4.
DR MINT; Q5XI81; -.
DR STRING; 10116.ENSRNOP00000065667; -.
DR BindingDB; Q5XI81; -.
DR iPTMnet; Q5XI81; -.
DR PhosphoSitePlus; Q5XI81; -.
DR jPOST; Q5XI81; -.
DR PRIDE; Q5XI81; -.
DR GeneID; 361927; -.
DR KEGG; rno:361927; -.
DR UCSC; RGD:1311733; rat.
DR CTD; 8087; -.
DR RGD; 1311733; Fxr1.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR InParanoid; Q5XI81; -.
DR OrthoDB; 374073at2759; -.
DR PhylomeDB; Q5XI81; -.
DR PRO; PR:Q5XI81; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:1902737; C:dendritic filopodium; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0044326; C:dendritic spine neck; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:RGD.
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; ISS:UniProtKB.
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 GO; GO:0060538; P:skeletal muscle organ development; ISO:RGD.
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; 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; 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; SSF54791; 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein 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..568
FT /note="RNA-binding protein FXR1"
FT /id="PRO_0000248488"
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 218..279
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 281..351
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 380..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..486
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000255"
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"
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 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 476
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 476
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 482
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 482
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 484
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 484
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51116"
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 568 AA; 63947 MW; C6FBCD4F23B248AF CRC64;
MAELTVEVRG SNGAFYKVFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
IQQARKVPGV TAIELDEDTG TFRIYGESAE AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EKEKGYATDE STVSSVQGSR SYSGRGRGRR
GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE TRHQRDSRRR PGGRGRSVSG
GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT
DEDAVLMDGM TESDTASVNE NGLGKRCD
