FRG1_XENLA
ID FRG1_XENLA Reviewed; 210 AA.
AC Q6GLS8;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein FRG1 {ECO:0000250|UniProtKB:Q14331};
GN Name=frg1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH74376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH74376.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RC TISSUE=Oocyte {ECO:0000269|PubMed:21699900};
RX PubMed=21699900; DOI=10.1016/j.jmb.2011.06.014;
RA Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K., Klooster R.,
RA Jones T.I., Bellini M., Levesque L., Brieher W.M., van der Maarel S.M.,
RA Jones P.L.;
RT "Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-
RT associated and actin-bundling protein.";
RL J. Mol. Biol. 411:397-416(2011).
CC -!- FUNCTION: Binds to mRNA in a sequence-independent manner. May play a
CC role in regulation of pre-mRNA splicing or in the assembly of rRNA into
CC ribosomal subunits. May be involved in mRNA transport. May be involved
CC in epigenetic regulation of muscle differentiation through regulation
CC of activity of the histone-lysine N-methyltransferase KMT5B (By
CC similarity). {ECO:0000250|UniProtKB:Q14331}.
CC -!- SUBUNIT: Homodimer and homotetramer in solution.
CC {ECO:0000250|UniProtKB:Q14331}.
CC -!- SUBCELLULAR LOCATION: Nucleus, Cajal body
CC {ECO:0000269|PubMed:21699900}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:21699900}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14331}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q14331}.
CC -!- SIMILARITY: Belongs to the FRG1 family. {ECO:0000250|UniProtKB:Q14331}.
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DR EMBL; BC074376; AAH74376.1; -; mRNA.
DR RefSeq; NP_001086250.1; NM_001092781.1.
DR AlphaFoldDB; Q6GLS8; -.
DR SMR; Q6GLS8; -.
DR DNASU; 444679; -.
DR GeneID; 444679; -.
DR CTD; 444679; -.
DR Xenbase; XB-GENE-1008656; frg1.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 444679; Expressed in egg cell and 19 other tissues.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR008999; Actin-crosslinking.
DR InterPro; IPR010414; FRG1.
DR PANTHER; PTHR12928; PTHR12928; 1.
DR Pfam; PF06229; FRG1; 1.
DR SUPFAM; SSF50405; SSF50405; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; mRNA processing; mRNA splicing; Myogenesis;
KW Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..210
FT /note="Protein FRG1"
FT /id="PRO_0000430489"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..30
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q14331, ECO:0000255"
FT COMPBIAS 13..27
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23131 MW; 87C61A06139B4D1C CRC64;
MAEYSKVKST KLMLKGIKNK SKKNKDKKRK REESDEDKLD IAGNWWSVKN FGEISGTVAI
EMDKGAYIHA LDNGLFTIGA PHKDDDDGPS PPEQFTAIKL SDSRVALKSG YGKYLGINSD
GLVIGRSDAI GAREQWEPVF DTGKMALLAS NSCFVGCNEE GDLVAQSKTA GEGEMIKIRS
CAEREAKRDD DIPNEDKGNV KQCEINYVYV