MRTFB_MOUSE
ID MRTFB_MOUSE Reviewed; 1080 AA.
AC P59759;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Myocardin-related transcription factor B {ECO:0000305};
DE Short=MRTF-B {ECO:0000305};
DE AltName: Full=MKL/myocardin-like protein 2;
GN Name=Mrtfb; Synonyms=Mkl2 {ECO:0000312|MGI:MGI:3050795};
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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH SRF.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12397177; DOI=10.1073/pnas.222561499;
RA Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
RA Richardson J.A., Nordheim A., Olson E.N.;
RT "Potentiation of serum response factor activity by a family of myocardin-
RT related transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
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: Acts as a transcriptional coactivator of serum response
CC factor (SRF). Required for skeletal myogenic differentiation.
CC {ECO:0000269|PubMed:12397177}.
CC -!- SUBUNIT: Interacts with MRTFA and SRF. {ECO:0000269|PubMed:12397177}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in heart, brain
CC and testis. Lower expression in lung, liver and kidney.
CC {ECO:0000269|PubMed:12397177}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the embryo at 10.5 dpc. High
CC expression in epithelial cells of the lung, kidney, bladder, colon,
CC testis, in the smooth muscle of the colon and small intestines, and in
CC the mesenchymal cells adjacent to the olfactory epithelium at 15.5 dpc.
CC {ECO:0000269|PubMed:12397177}.
CC -!- DOMAIN: The N-terminal region is required for nuclear localization and
CC the C-terminal region mediates transcriptional activity. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
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DR EMBL; AF532598; AAN33042.1; -; mRNA.
DR CCDS; CCDS37258.1; -.
DR RefSeq; NP_705816.2; NM_153588.3.
DR AlphaFoldDB; P59759; -.
DR SMR; P59759; -.
DR BioGRID; 232120; 4.
DR DIP; DIP-60885N; -.
DR IntAct; P59759; 2.
DR STRING; 10090.ENSMUSP00000009713; -.
DR iPTMnet; P59759; -.
DR PhosphoSitePlus; P59759; -.
DR EPD; P59759; -.
DR jPOST; P59759; -.
DR MaxQB; P59759; -.
DR PaxDb; P59759; -.
DR PRIDE; P59759; -.
DR ProteomicsDB; 295635; -.
DR DNASU; 239719; -.
DR GeneID; 239719; -.
DR KEGG; mmu:239719; -.
DR CTD; 57496; -.
DR MGI; MGI:3050795; Mrtfb.
DR eggNOG; ENOG502QU1Z; Eukaryota.
DR InParanoid; P59759; -.
DR OrthoDB; 190145at2759; -.
DR PhylomeDB; P59759; -.
DR BioGRID-ORCS; 239719; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Mrtfb; mouse.
DR PRO; PR:P59759; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P59759; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045844; P:positive regulation of striated muscle tissue development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IMP:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR043451; Myocardin-like.
DR InterPro; IPR004018; RPEL_repeat.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR22793; PTHR22793; 1.
DR Pfam; PF02755; RPEL; 2.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00707; RPEL; 3.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51073; RPEL; 3.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Developmental protein; Differentiation;
KW Glycoprotein; Isopeptide bond; Myogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1080
FT /note="Myocardin-related transcription factor B"
FT /id="PRO_0000126629"
FT REPEAT 40..65
FT /note="RPEL 1"
FT REPEAT 84..109
FT /note="RPEL 2"
FT REPEAT 128..153
FT /note="RPEL 3"
FT DOMAIN 383..417
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 170..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..585
FT /note="Required for interaction with itself and with MRTFA"
FT /evidence="ECO:0000250"
FT REGION 588..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..594
FT /evidence="ECO:0000255"
FT COMPBIAS 181..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH7"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH7"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH7"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH7"
SQ SEQUENCE 1080 AA; 117547 MW; 1781D8EF34517DAC CRC64;
MIDSSKKQPQ GFPEILTAED FEPFKEKECL EGSNQKSLKE VLQLRLQQRR TREQLVDQGI
MPPLKSPAAF HEQIKSLERA RTENFLKHKI RSRPDRSELV RMHILEETFA EPSLQATQMK
LKRARLADDL NEKIAQRPGP MELVEKNILP VDSSVKEAII GVVKEDYPHT HGEFSFDEDS
SDALSPDQPA SQESQGSAAS PSEPKVSASP PPVTASTPAQ FTSVSPAVPE FLKTPLTADQ
PPTRSTAPVL PTNTVSSAKS GPMLVKQSHP KNPNDKHRSK KCKDPKPRVK KLKYHQYIPP
NQKGEKSEPQ MDSNYARLLQ QQQLFLQLQI LSQQQQQQQQ QHYNYQTILP APIKTDKNSS
SGSNSGSSSS MPARRPGPLP SSLDDLKVSE LKTELKLRGL PVSGTKPDLI ERLKPYQEVT
SSNLATGSIV AVSSATIVTS NPEVTVALPV TTLHNAVTSS VSTFKADLAL PATSSVPHVE
NAHSPLPISP SPSEQSSLST DDTNMTDTFT EIMTMMSPSQ LLCSSPLRVV SHDDSLSPSS
STLSTLELDA AEKDRKLQEK EKQIEELKRK LEQEQKLVEV LKMQLEVEKR GQQRPPDPQP
SDPPHPFNTS DPKHGSVGSS IKDEASLPDC SSPQQPITVP GHSVGQPIST GSQTLVAKKT
VVVKQEVPMA QAEQQNVVSQ FYLSSQGQPP ALVAQPQALL TTQTTQLLLP VSIQGSNVTS
VQLPVGSLQL QTPAQGRVQA QPHVAAATQV PAAALPSALT SALPQKQEAF PQHVLGQPQP
VRKVFTNSAP NTVLQYQRQP GPTNQQPFVS KTSNPALQSR TAPLAPLQNG PSLASKPSSP
PPPQQFVVQH SLFATPITKT KDPPRYEEAI KQTRSTQPAL PEVSSVHSQQ MDDLFDILIK
SGEISFPIKE EPSPISKMKP VTASITTMPV NTVVSRPPPQ VQIAPPVSLE PVNSLSASLE
NQLEAFLDGT LPSATDTGPL QNSSEDRESF SLIEDLQNDL LSHSSMLYQS HSPMETSEAQ
LVSGTPCLSL DLSDSNLDNM EWLDITMPTT SSGLTPLSTT APSMFSADFL DPQDLPLPWD
