MBNL1_MOUSE
ID MBNL1_MOUSE Reviewed; 341 AA.
AC Q9JKP5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Muscleblind-like protein 1;
DE AltName: Full=Triplet-expansion RNA-binding protein;
GN Name=Mbnl1; Synonyms=Exp, Mbnl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Castagnola P., Monticone M., Borsani G., Bassi M.T., Tonachini L.;
RT "cDNA cloning of mouse muscleblind.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-9, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10970838; DOI=10.1093/emboj/19.17.4439;
RA Miller J.W., Urbinati C.R., Teng-Umnuay P., Stenberg M.G., Byrne B.J.,
RA Thornton C.A., Swanson M.S.;
RT "Recruitment of human muscleblind proteins to (CUG)(n) expansions
RT associated with myotonic dystrophy.";
RL EMBO J. 19:4439-4448(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts
CC either as activator or repressor of splicing on specific pre-mRNA
CC targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion
CC but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle.
CC Antagonizes the alternative splicing activity pattern of CELF proteins.
CC Regulates the TNNT2 exon 5 skipping through competition with U2AF2.
CC Inhibits the formation of the spliceosome A complex on intron 4 of
CC TNNT2 pre-mRNA. Binds to the stem-loop structure within the
CC polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly.
CC Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA.
CC Binds to CUG triplet repeat expansion in myotonic dystrophy muscle
CC cells by sequestering the target RNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the
CC interaction in RNA-independent (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q9NR56}. Note=Localized with DDX1, TIAL1 and
CC YBX1 in stress granules upon stress. Localized in the cytoplasm of
CC multinucleated myotubes. {ECO:0000250|UniProtKB:Q9NR56}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cardiac and skeletal muscle.
CC Weakly expressed in heart and eye (at protein level).
CC {ECO:0000269|PubMed:10970838}.
CC -!- SIMILARITY: Belongs to the muscleblind family. {ECO:0000305}.
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DR EMBL; AF231110; AAF72159.1; -; mRNA.
DR CCDS; CCDS79917.1; -.
DR RefSeq; NP_001240637.1; NM_001253708.2.
DR AlphaFoldDB; Q9JKP5; -.
DR SMR; Q9JKP5; -.
DR BioGRID; 208165; 4.
DR STRING; 10090.ENSMUSP00000096686; -.
DR iPTMnet; Q9JKP5; -.
DR PhosphoSitePlus; Q9JKP5; -.
DR EPD; Q9JKP5; -.
DR jPOST; Q9JKP5; -.
DR MaxQB; Q9JKP5; -.
DR PaxDb; Q9JKP5; -.
DR PRIDE; Q9JKP5; -.
DR ProteomicsDB; 295805; -.
DR Antibodypedia; 4292; 355 antibodies from 34 providers.
DR DNASU; 56758; -.
DR Ensembl; ENSMUST00000192607; ENSMUSP00000142095; ENSMUSG00000027763.
DR GeneID; 56758; -.
DR KEGG; mmu:56758; -.
DR UCSC; uc008pjf.1; mouse.
DR CTD; 4154; -.
DR MGI; MGI:1928482; Mbnl1.
DR VEuPathDB; HostDB:ENSMUSG00000027763; -.
DR eggNOG; KOG2494; Eukaryota.
DR GeneTree; ENSGT00950000182897; -.
DR InParanoid; Q9JKP5; -.
DR OrthoDB; 1543798at2759; -.
DR PhylomeDB; Q9JKP5; -.
DR BioGRID-ORCS; 56758; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Mbnl1; mouse.
DR PRO; PR:Q9JKP5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JKP5; protein.
DR Bgee; ENSMUSG00000027763; Expressed in aorta tunica media and 261 other tissues.
DR ExpressionAtlas; Q9JKP5; baseline and differential.
DR Genevisible; Q9JKP5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001069; F:regulatory region RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEP:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IMP:MGI.
DR GO; GO:0045445; P:myoblast differentiation; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..341
FT /note="Muscleblind-like protein 1"
FT /id="PRO_0000089179"
FT ZN_FING 13..41
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 47..73
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 178..206
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 214..240
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR56"
SQ SEQUENCE 341 AA; 36976 MW; 8E008DB5C7EF8AB9 CRC64;
MAVSVTPIRD TKWLTLEVCR EFQRGTCSRP DTECKFAHPS KSCQVENGRV IACFDSLKGR
CSRENCKYLH PPPHLKTQLE INGRNNLIQQ KNMAMLAQQM QLANAMMPGA PLQPVPMFSV
APSLATSASA AFNPYLGPVS PSLVPAEILP TAPMLVTGNP GVPVPAAAAA AAQKLMRTDR
LEVCREYQRG NCNRGENDCR FAHPADSTMI DTNDNTVTVC MDYIKGRCSR EKCKYFHPPA
HLQAKIKAAQ YQVNQAAAAQ AAATAAAMGI PQAVLPPLPK RPALEKTNGA TAVFNTGIFQ
YQQALANMQL QQHTAFLPPG SILCMTPATS VDTHNICRTS D
