MRTFA_MOUSE
ID MRTFA_MOUSE Reviewed; 964 AA.
AC Q8K4J6; Q642U1;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Myocardin-related transcription factor A {ECO:0000305};
DE Short=MRTF-A {ECO:0000303|PubMed:27304076};
DE AltName: Full=Basic SAP coiled-coil transcription activator {ECO:0000303|PubMed:12019265};
DE AltName: Full=MKL/myocardin-like protein 1;
DE AltName: Full=Megakaryoblastic leukemia 1 protein homolog;
DE AltName: Full=Megakaryocytic acute leukemia protein homolog {ECO:0000303|PubMed:12732141, ECO:0000303|PubMed:19008859};
GN Name=Mrtfa;
GN Synonyms=Bsac {ECO:0000303|PubMed:12019265},
GN Mal {ECO:0000303|PubMed:12732141, ECO:0000303|PubMed:19008859},
GN Mkl1 {ECO:0000312|MGI:MGI:2384495};
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=12019265; DOI=10.1074/jbc.m203190200;
RA Sasazuki T., Sawada Y., Sakon S., Kitamura T., Kishi T., Okazaki T.,
RA Katano M., Tanaka M., Watanabe M., Yagita H., Okumura K., Nakano H.;
RT "Identification of a novel transcriptional activator, BSAC, by a functional
RT cloning to inhibit tumor necrosis factor-induced cell death.";
RL J. Biol. Chem. 277:28853-28860(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRF AND ACTIN.
RX PubMed=12732141; DOI=10.1016/s0092-8674(03)00278-2;
RA Miralles F., Posern G., Zaromytidou A.I., Treisman R.;
RT "Actin dynamics control SRF activity by regulation of its coactivator
RT MAL.";
RL Cell 113:329-342(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN, AND MUTAGENESIS OF
RP ARG-24; ARG-68 AND ARG-112.
RX PubMed=17588931; DOI=10.1126/science.1141084;
RA Vartiainen M.K., Guettler S., Larijani B., Treisman R.;
RT "Nuclear actin regulates dynamic subcellular localization and activity of
RT the SRF cofactor MAL.";
RL Science 316:1749-1752(2007).
RN [7]
RP FUNCTION, INTERACTION WITH ACTB; SCAI AND SRF, AND SUBCELLULAR LOCATION.
RX PubMed=19350017; DOI=10.1038/ncb1862;
RA Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA Grosse R.;
RT "SCAI acts as a suppressor of cancer cell invasion through the
RT transcriptional control of beta1-integrin.";
RL Nat. Cell Biol. 11:557-568(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [9]
RP FUNCTION.
RX PubMed=23558171; DOI=10.1126/science.1235038;
RA Baarlink C., Wang H., Grosse R.;
RT "Nuclear actin network assembly by formins regulates the SRF coactivator
RT MAL.";
RL Science 340:864-867(2013).
RN [10]
RP FUNCTION.
RX PubMed=24732378; DOI=10.1101/gad.239327.114;
RA Esnault C., Stewart A., Gualdrini F., East P., Horswell S., Matthews N.,
RA Treisman R.;
RT "Rho-actin signaling to the MRTF coactivators dominates the immediate
RT transcriptional response to serum in fibroblasts.";
RL Genes Dev. 28:943-958(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25759381; DOI=10.1074/jbc.m114.627166;
RA Plessner M., Melak M., Chinchilla P., Baarlink C., Grosse R.;
RT "Nuclear F-actin formation and reorganization upon cell spreading.";
RL J. Biol. Chem. 290:11209-11216(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-85 IN COMPLEX WITH G-ACTIN,
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 16-41 IN COMPLEX WITH G-ACTIN,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19008859; DOI=10.1038/emboj.2008.235;
RA Mouilleron S., Guettler S., Langer C.A., Treisman R., McDonald N.Q.;
RT "Molecular basis for G-actin binding to RPEL motifs from the serum response
RT factor coactivator MAL.";
RL EMBO J. 27:3198-3208(2008).
RN [13]
RP PHOSPHORYLATION AT SER-41; SER-159; SER-174; SER-191; SER-349; SER-351;
RP THR-352; SER-355; SER-358; THR-360; SER-423; SER-484; THR-485; SER-487;
RP THR-488; SER-492; THR-494; SER-496; SER-520; SER-530; SER-544; SER-548;
RP SER-605; SER-606; SER-651; SER-687; SER-718; SER-724; SER-728; SER-810;
RP THR-822; SER-826; SER-840; THR-842 AND SER-892, INTERACTION WITH ACTIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27304076; DOI=10.7554/elife.15460;
RA Panayiotou R., Miralles F., Pawlowski R., Diring J., Flynn H.R., Skehel M.,
RA Treisman R.;
RT "Phosphorylation acts positively and negatively to regulate MRTF-A
RT subcellular localisation and activity.";
RL Elife 5:0-0(2016).
RN [14] {ECO:0007744|PDB:2YJE, ECO:0007744|PDB:2YJF}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 16-142 IN COMPLEX WITH G-ACTIN,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-45; GLN-48; LEU-52;
RP ARG-54; ARG-56; LEU-89; LYS-92; LEU-96; ARG-98 AND ARG-100.
RX PubMed=21673315; DOI=10.1126/scisignal.2001750;
RA Mouilleron S., Langer C.A., Guettler S., McDonald N.Q., Treisman R.;
RT "Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin
RT controls nucleocytoplasmic shuttling of a transcriptional coactivator.";
RL Sci. Signal. 4:ra40-ra40(2011).
CC -!- FUNCTION: Transcription coactivator that associates with the serum
CC response factor (SRF) transcription factor to control expression of
CC genes regulating the cytoskeleton during development, morphogenesis and
CC cell migration (PubMed:12019265, PubMed:12732141, PubMed:17588931,
CC PubMed:19350017, PubMed:24732378). The SRF-MRTFA complex activity
CC responds to Rho GTPase-induced changes in cellular globular actin (G-
CC actin) concentration, thereby coupling cytoskeletal gene expression to
CC cytoskeletal dynamics (PubMed:24732378). MRTFA binds G-actin via its
CC RPEL repeats, regulating activity of the MRTFA-SRF complex
CC (PubMed:12732141, PubMed:17588931). Activity is also regulated by
CC filamentous actin (F-actin) in the nucleus (PubMed:23558171,
CC PubMed:25759381). {ECO:0000269|PubMed:12019265,
CC ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931,
CC ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:23558171,
CC ECO:0000269|PubMed:24732378, ECO:0000269|PubMed:25759381}.
CC -!- SUBUNIT: Interacts with SRF, forming the SRF-MRTFA nuclear complex
CC which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF
CC (PubMed:12732141, PubMed:19350017). Interacts (via RPEL repeats) with
CC globular actin (G-actin), thereby regulating its subcellular location
CC and activity of the complex formed with SRF (PubMed:12732141,
CC PubMed:17588931, PubMed:19350017, PubMed:19008859, PubMed:27304076,
CC PubMed:21673315). Either forms a trivalent (by binding three G-actin
CC monomers) or pentavalent (by binding five G-actin monomers) complex
CC with G-actin (PubMed:21673315). Forms a nuclear ternary complex with
CC SCAI and SRF, leading to suppress MRTFA-induced SRF transcriptional
CC activity (PubMed:19350017). Interacts with beta-actin (ACTB);
CC interaction with ACTB prevents interaction with SCAI (PubMed:19350017).
CC Interacts with MRTFB (By similarity). {ECO:0000250|UniProtKB:Q969V6,
CC ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931,
CC ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:19350017,
CC ECO:0000269|PubMed:21673315, ECO:0000269|PubMed:27304076}.
CC -!- INTERACTION:
CC Q8K4J6; P68135: ACTA1; Xeno; NbExp=15; IntAct=EBI-8291665, EBI-367540;
CC Q8K4J6; P60709: ACTB; Xeno; NbExp=3; IntAct=EBI-8291665, EBI-353944;
CC Q8K4J6; O00629: KPNA4; Xeno; NbExp=4; IntAct=EBI-8291665, EBI-396343;
CC Q8K4J6; Q14974: KPNB1; Xeno; NbExp=2; IntAct=EBI-8291665, EBI-286758;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12732141,
CC ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:19008859,
CC ECO:0000269|PubMed:21673315, ECO:0000269|PubMed:25759381,
CC ECO:0000269|PubMed:27304076}. Nucleus {ECO:0000269|PubMed:12019265,
CC ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931,
CC ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:21673315,
CC ECO:0000269|PubMed:25759381, ECO:0000269|PubMed:27304076}.
CC Note=Subcellular location is tightly regulated by actin both in
CC cytoplasm and nucleus: high levels of G-actin in the nucleus observed
CC during serum deprivation lead to low levels of nuclear MRTFA, while
CC reduced levels of nuclear G-actin result in accumulation of MRTFA in
CC the nucleus (PubMed:17588931, PubMed:21673315). G-actin-binding in the
CC cytoplasm inhibits nuclear import by masking the nuclear localization
CC signal (NLS) (PubMed:17588931, PubMed:21673315). In contrast, binding
CC to nuclear globular actin (G-actin) promotes nuclear export to the
CC cytoplasm (PubMed:17588931). Nuclear localization is regulated by
CC MICAL2, which mediates depolymerization of nuclear actin, which
CC decreases nuclear G-actin pool, thereby promoting retention of MRTFA in
CC the nucleus and subsequent formation of an active complex with SRF (By
CC similarity). {ECO:0000250|UniProtKB:Q969V6,
CC ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:21673315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K4J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4J6-2; Sequence=VSP_007652;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC muscle, kidney and testis. {ECO:0000269|PubMed:12019265}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the embryo at 10.5 dpc; higher
CC expression is found at 13.5 dpc in neural mesenchymal cells, skeletal
CC muscle of the tongue, and epithelial cells of the colon and small
CC intestine; at 15.5 dpc, expression in epithelial cells of lung, kidney,
CC bladder, and colon is also detected. {ECO:0000269|PubMed:12397177}.
CC -!- DOMAIN: The N-terminal region is required for nuclear localization and
CC the C-terminal region mediates transcriptional activity.
CC {ECO:0000269|PubMed:19008859}.
CC -!- DOMAIN: The RPEL repeats mediate binding to globular actin (G-actin);
CC each RPEL repeat-binding to one G-actin monomer (PubMed:19008859,
CC PubMed:21673315). In addition, each intervening spacer sequence region
CC can bind one G-actin monomer, to reach a pentavalent complex
CC (PubMed:21673315). {ECO:0000269|PubMed:19008859,
CC ECO:0000269|PubMed:21673315}.
CC -!- PTM: Phosphorylation at Ser-41 by Erk inhibits binding of globular
CC actin (G-actin), unmasking the nuclear localization signal (NLS) and
CC promoting nuclear import. {ECO:0000269|PubMed:27304076}.
CC -!- CAUTION: Some publications use a protein sequence that is longer at the
CC N-terminus and is based on an artificial construct (PubMed:12732141,
CC PubMed:27304076). The sequence used in these publications modifies a
CC non-canonical CTG leucine codon upstream of the initiator codon into
CC ATG, generating a protein of 1021 residues (PubMed:12732141,
CC PubMed:27304076). The existence of this form has not been confirmed in
CC vivo and is therefore unsure (PubMed:12732141, PubMed:27304076).
CC Similarly, the existence of the S33 ('Ser-33') phosphorylation site
CC described in Panayiotou et al. is unsure (PubMed:27304076).
CC {ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:27304076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF385582; AAM94258.1; -; mRNA.
DR EMBL; AF532597; AAN33041.1; -; mRNA.
DR EMBL; AK044188; BAC31809.1; -; mRNA.
DR EMBL; AK089416; BAC40873.1; -; mRNA.
DR EMBL; BC050941; AAH50941.1; -; mRNA.
DR CCDS; CCDS37147.1; -. [Q8K4J6-1]
DR RefSeq; NP_001076005.1; NM_001082536.1.
DR RefSeq; NP_694629.2; NM_153049.3. [Q8K4J6-1]
DR PDB; 2V51; X-ray; 2.35 A; E/F=16-41.
DR PDB; 2V52; X-ray; 1.45 A; M=54-85.
DR PDB; 2YJE; X-ray; 3.10 A; M=16-142.
DR PDB; 2YJF; X-ray; 3.50 A; M=16-142.
DR PDBsum; 2V51; -.
DR PDBsum; 2V52; -.
DR PDBsum; 2YJE; -.
DR PDBsum; 2YJF; -.
DR AlphaFoldDB; Q8K4J6; -.
DR SMR; Q8K4J6; -.
DR BioGRID; 230180; 2.
DR DIP; DIP-60884N; -.
DR ELM; Q8K4J6; -.
DR IntAct; Q8K4J6; 7.
DR MINT; Q8K4J6; -.
DR STRING; 10090.ENSMUSP00000105207; -.
DR iPTMnet; Q8K4J6; -.
DR PhosphoSitePlus; Q8K4J6; -.
DR EPD; Q8K4J6; -.
DR MaxQB; Q8K4J6; -.
DR PaxDb; Q8K4J6; -.
DR PRIDE; Q8K4J6; -.
DR ProteomicsDB; 295952; -. [Q8K4J6-1]
DR ProteomicsDB; 295953; -. [Q8K4J6-2]
DR Antibodypedia; 26780; 362 antibodies from 33 providers.
DR DNASU; 223701; -.
DR Ensembl; ENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292. [Q8K4J6-1]
DR Ensembl; ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292. [Q8K4J6-2]
DR GeneID; 223701; -.
DR KEGG; mmu:223701; -.
DR UCSC; uc007wwc.2; mouse. [Q8K4J6-1]
DR CTD; 57591; -.
DR MGI; MGI:2384495; Mrtfa.
DR VEuPathDB; HostDB:ENSMUSG00000042292; -.
DR eggNOG; ENOG502R5FB; Eukaryota.
DR GeneTree; ENSGT00950000182979; -.
DR InParanoid; Q8K4J6; -.
DR OrthoDB; 190145at2759; -.
DR PhylomeDB; Q8K4J6; -.
DR TreeFam; TF326024; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR BioGRID-ORCS; 223701; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Smarca4; mouse.
DR EvolutionaryTrace; Q8K4J6; -.
DR PRO; PR:Q8K4J6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8K4J6; protein.
DR Bgee; ENSMUSG00000042292; Expressed in granulocyte and 248 other tissues.
DR ExpressionAtlas; Q8K4J6; baseline and differential.
DR Genevisible; Q8K4J6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IGI:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO:MGI.
DR DisProt; DP01999; -.
DR Gene3D; 1.10.720.30; -; 1.
DR IDEAL; IID50055; -.
DR InterPro; IPR029992; MRTF-A.
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 PANTHER; PTHR22793:SF6; PTHR22793:SF6; 1.
DR Pfam; PF02755; RPEL; 3.
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 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..964
FT /note="Myocardin-related transcription factor A"
FT /id="PRO_0000126626"
FT REPEAT 15..40
FT /note="RPEL 1"
FT REPEAT 59..84
FT /note="RPEL 2"
FT REPEAT 103..128
FT /note="RPEL 3"
FT DOMAIN 385..419
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..291
FT /note="Mediates interaction with SCAI and ACTB"
FT /evidence="ECO:0000269|PubMed:19350017"
FT REGION 41..58
FT /note="Intervening spacer sequence 1"
FT /evidence="ECO:0000269|PubMed:19008859"
FT REGION 85..102
FT /note="Intervening spacer sequence 2"
FT /evidence="ECO:0000269|PubMed:19008859"
FT REGION 145..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..600
FT /evidence="ECO:0000255"
FT COMPBIAS 145..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969V6"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 822
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 842
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27304076"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12397177,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_007652"
FT MUTAGEN 24
FT /note="R->A: In 123-1A: Reduced interaction with G-actin,
FT leading to a constitutively active SRF-MRTFA complex; when
FT associated with A-68 and A-112."
FT /evidence="ECO:0000269|PubMed:17588931"
FT MUTAGEN 45
FT /note="F->A,D: Induces a nuclear accumulation in
FT unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 48
FT /note="Q->A,D: Induces a nuclear accumulation in
FT unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 52
FT /note="L->A,D: Induces a nuclear accumulation in
FT unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 54
FT /note="R->A: Impaired interaction with G-actin, leading to
FT nuclear accumulation in unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 56
FT /note="R->A: Impaired interaction with G-actin, leading to
FT nuclear accumulation in unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 68
FT /note="R->A: In 123-1A: Reduced interaction with G-actin,
FT leading to a constitutively active SRF-MRTFA complex; when
FT associated with A-24 and A-112."
FT /evidence="ECO:0000269|PubMed:17588931"
FT MUTAGEN 89
FT /note="L->A,D: Does not induce a nuclear accumulation in
FT unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 92
FT /note="K->A,D: Does not induce a nuclear accumulation in
FT unstimulated cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 96
FT /note="L->A: Induces a nuclear accumulation in unstimulated
FT cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 96
FT /note="L->D: Induces a nuclear decrease in unstimulated
FT cells."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 98
FT /note="R->A: Impaired interaction with G-actin, leading to
FT cytoplasmic accumulation."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 100
FT /note="R->A: Impaired interaction with G-actin, leading to
FT cytoplasmic accumulation."
FT /evidence="ECO:0000269|PubMed:21673315"
FT MUTAGEN 112
FT /note="R->A: In 123-1A: Reduced interaction with G-actin,
FT leading to a constitutively active SRF-MRTFA complex; when
FT associated with A-24 and A-68."
FT /evidence="ECO:0000269|PubMed:17588931"
FT CONFLICT 53
FT /note="E -> Q (in Ref. 3; BAC31809)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="S -> D (in Ref. 3; BAC40873)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="S -> F (in Ref. 1; AAM94258)"
FT /evidence="ECO:0000305"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2V51"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:2V51"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2YJE"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2V52"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:2V52"
FT HELIX 87..110
FT /evidence="ECO:0007829|PDB:2YJF"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:2YJF"
SQ SEQUENCE 964 AA; 102546 MW; AFAEA328A1860CE5 CRC64;
MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR SLERARTEDY
LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR LADDLNEKIA QRPGPMELVE
KNILPVESSL KEAIIVGQVN YPKVADSSSF DEDSSDALSP EQPASHESQG SVPSPLESRV
SDPLPSATSI SPTQVLSQLP MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP
TLIKQSQPKS ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ
QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL STSSSPSSGT
PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR SLPVSGTKTE LIERLRAYQD
QVSPAPGAPK APATTSVLSK AGEVVVAFPA ALLSTGSALV TAGLAPAEMV VATVTSNGMV
KFGSTGSTPP VSPTPSERSL LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA
RAASCCLSPG ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ
PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE SPPVVVKQEA
GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL ILTVTNKSAD GPGLPAGSPQ
QPLSQPGSPA PGPPAQMDLE HPPQPPFATP TSLLKKEPPG YEETVTQQPK QQENGSSSQH
MDDLFDILIQ SGEISADFKE PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS
PTLPGRLEDF LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH
FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF LDGHDLQLHW
DSCL
