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 27-MAR-2024, entry version 177. 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}, Mal GN {ECO:0000303|PubMed:12732141, ECO:0000303|PubMed:19008859}, Mkl1 GN {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; 3. DR DIP; DIP-60884N; -. DR ELM; Q8K4J6; -. DR IntAct; Q8K4J6; 7. DR MINT; Q8K4J6; -. DR STRING; 10090.ENSMUSP00000105207; -. DR GlyGen; Q8K4J6; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q8K4J6; -. DR PhosphoSitePlus; Q8K4J6; -. DR EPD; Q8K4J6; -. DR MaxQB; Q8K4J6; -. DR PaxDb; 10090-ENSMUSP00000105207; -. DR ProteomicsDB; 295952; -. [Q8K4J6-1] DR ProteomicsDB; 295953; -. [Q8K4J6-2] DR Pumba; Q8K4J6; -. DR Antibodypedia; 26780; 426 antibodies from 33 providers. DR DNASU; 223701; -. DR Ensembl; ENSMUST00000109579.9; ENSMUSP00000105207.3; ENSMUSG00000042292.19. [Q8K4J6-1] DR Ensembl; ENSMUST00000149582.8; ENSMUSP00000117745.2; ENSMUSG00000042292.19. [Q8K4J6-2] DR GeneID; 223701; -. DR KEGG; mmu:223701; -. DR UCSC; uc007wwc.2; mouse. [Q8K4J6-1] DR AGR; MGI:2384495; -. DR CTD; 57591; -. DR MGI; MGI:2384495; Mrtfa. DR VEuPathDB; HostDB:ENSMUSG00000042292; -. DR eggNOG; ENOG502R5FB; Eukaryota. DR GeneTree; ENSGT00950000182979; -. DR InParanoid; Q8K4J6; -. DR OrthoDB; 2997330at2759; -. 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 79 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 251 other cell types or tissues. DR ExpressionAtlas; Q8K4J6; baseline and differential. 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:0060090; F:molecular adaptor activity; EXP:DisProt. 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:0001764; P:neuron migration; IGI:MGI. DR GO; GO:0031175; P:neuron projection development; IGI:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA: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: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; 6.10.140.2040; -; 1. DR Gene3D; 6.10.150.10; -; 1. DR Gene3D; 1.10.720.30; SAP domain; 1. DR IDEAL; IID50055; -. DR InterPro; IPR043451; Myocardin-like. DR InterPro; IPR004018; RPEL_repeat. DR InterPro; IPR003034; SAP_dom. DR InterPro; IPR036361; SAP_dom_sf. DR PANTHER; PTHR22793:SF6; MYOCARDIN-RELATED TRANSCRIPTION FACTOR A; 1. DR PANTHER; PTHR22793; MYOCARDIN-RELATED TRANSCRIPTION FACTOR-RELATED; 1. DR Pfam; PF02755; RPEL; 3. DR Pfam; PF02037; SAP; 1. DR SMART; SM00707; RPEL; 3. DR SMART; SM00513; SAP; 1. DR SUPFAM; SSF68906; SAP domain; 1. DR PROSITE; PS51073; RPEL; 3. DR PROSITE; PS50800; SAP; 1. DR Genevisible; Q8K4J6; MM. 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 //