MEF2C_MOUSE
ID MEF2C_MOUSE Reviewed; 474 AA.
AC Q8CFN5; Q8R0H1; Q9D7L0; Q9QW20;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Myocyte-specific enhancer factor 2C {ECO:0000305};
DE AltName: Full=Myocyte enhancer factor 2C {ECO:0000312|MGI:MGI:99458};
GN Name=Mef2c {ECO:0000312|MGI:MGI:99458};
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 2), AND TISSUE SPECIFICITY.
RX PubMed=8506376; DOI=10.1073/pnas.90.11.5282;
RA Martin J.F., Schwarz J.J., Olson E.N.;
RT "Myocyte enhancer factor (MEF) 2C: a tissue-restricted member of the MEF-2
RT family of transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5282-5286(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Eye;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=9013788; DOI=10.1016/s0169-328x(96)00135-0;
RA Lin X., Shah S., Bulleit R.F.;
RT "The expression of MEF2 genes is implicated in CNS neuronal
RT differentiation.";
RL Brain Res. Mol. Brain Res. 42:307-316(1996).
RN [5]
RP PHOSPHORYLATION AT SER-59, AND MUTAGENESIS OF SER-59.
RX PubMed=8663403; DOI=10.1074/jbc.271.29.17199;
RA Molkentin J.D., Li L., Olson E.N.;
RT "Phosphorylation of the MADS-Box transcription factor MEF2C enhances its
RT DNA binding activity.";
RL J. Biol. Chem. 271:17199-17204(1996).
RN [6]
RP FUNCTION.
RX PubMed=9162005; DOI=10.1126/science.276.5317.1404;
RA Lin Q., Schwarz J., Bucana C., Olson E.N.;
RT "Control of mouse cardiac morphogenesis and myogenesis by transcription
RT factor MEF2C.";
RL Science 276:1404-1407(1997).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9778514; DOI=10.1242/dev.125.22.4565;
RA Lin Q., Lu J., Yanagisawa H., Webb R., Lyons G.E., Richardson J.A.,
RA Olson E.N.;
RT "Requirement of the MADS-box transcription factor MEF2C for vascular
RT development.";
RL Development 125:4565-4574(1998).
RN [8]
RP FUNCTION, INTERACTION WITH SOX18, AND SUBCELLULAR LOCATION.
RX PubMed=11554755; DOI=10.1006/bbrc.2001.5589;
RA Hosking B.M., Wang S.C., Chen S.L., Penning S., Koopman P., Muscat G.E.;
RT "SOX18 directly interacts with MEF2C in endothelial cells.";
RL Biochem. Biophys. Res. Commun. 287:493-500(2001).
RN [9]
RP INTERACTION WITH HDAC7.
RX PubMed=11279209; DOI=10.1074/jbc.m101508200;
RA Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
RA Muscat G.E.O.;
RT "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
RL J. Biol. Chem. 276:17007-17013(2001).
RN [10]
RP INTERACTION WITH CARM1.
RX PubMed=11713257; DOI=10.1074/jbc.m109835200;
RA Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E.;
RT "The coactivator-associated arginine methyltransferase is necessary for
RT muscle differentiation: CARM1 coactivates myocyte enhancer factor-2.";
RL J. Biol. Chem. 277:4324-4333(2002).
RN [11]
RP TISSUE SPECIFICITY OF ISOFORMS.
RX PubMed=15340086; DOI=10.1128/mcb.24.18.8264-8275.2004;
RA Zhu B., Gulick T.;
RT "Phosphorylation and alternative pre-mRNA splicing converge to regulate
RT myocyte enhancer factor 2C activity.";
RL Mol. Cell. Biol. 24:8264-8275(2004).
RN [12]
RP TISSUE SPECIFICITY OF ISOFORMS.
RX PubMed=15834131; DOI=10.1074/jbc.m502491200;
RA Zhu B., Ramachandran B., Gulick T.;
RT "Alternative pre-mRNA splicing governs expression of a conserved acidic
RT transactivation domain in myocyte enhancer factor 2 factors of striated
RT muscle and brain.";
RL J. Biol. Chem. 280:28749-28760(2005).
RN [13]
RP INTERACTION WITH MYOCD.
RX PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
RA Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
RT "Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR.";
RL Mol. Cell 23:83-96(2006).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18438409; DOI=10.1038/ni.1609;
RA Wilker P.R., Kohyama M., Sandau M.M., Albring J.C., Nakagawa O.,
RA Schwarz J.J., Murphy K.M.;
RT "Transcription factor Mef2c is required for B cell proliferation and
RT survival after antigen receptor stimulation.";
RL Nat. Immunol. 9:603-612(2008).
RN [15]
RP ACETYLATION AT LYS-4, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, AND MUTAGENESIS OF ARG-3 AND LYS-4.
RX PubMed=18086704; DOI=10.1093/nar/gkm1114;
RA Angelelli C., Magli A., Ferrari D., Ganassi M., Matafora V., Parise F.,
RA Razzini G., Bachi A., Ferrari S., Molinari S.;
RT "Differentiation-dependent lysine 4 acetylation enhances MEF2C binding to
RT DNA in skeletal muscle cells.";
RL Nucleic Acids Res. 36:915-928(2008).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18599438; DOI=10.1073/pnas.0802679105;
RA Barbosa A.C., Kim M.S., Ertunc M., Adachi M., Nelson E.D., McAnally J.,
RA Richardson J.A., Kavalali E.T., Monteggia L.M., Bassel-Duby R., Olson E.N.;
RT "MEF2C, a transcription factor that facilitates learning and memory by
RT negative regulation of synapse numbers and function.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9391-9396(2008).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18599437; DOI=10.1073/pnas.0802876105;
RA Li H., Radford J.C., Ragusa M.J., Shea K.L., McKercher S.R., Zaremba J.D.,
RA Soussou W., Nie Z., Kang Y.J., Nakanishi N., Okamoto S., Roberts A.J.,
RA Schwarz J.J., Lipton S.A.;
RT "Transcription factor MEF2C influences neural stem/progenitor cell
RT differentiation and maturation in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9397-9402(2008).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19211936; DOI=10.1182/blood-2008-07-167577;
RA Gekas C., Rhodes K.E., Gereige L.M., Helgadottir H., Ferrari R.,
RA Kurdistani S.K., Montecino-Rodriguez E., Bassel-Duby R., Olson E.,
RA Krivtsov A.V., Armstrong S., Orkin S.H., Pellegrini M., Mikkola H.K.;
RT "Mef2C is a lineage-restricted target of Scl/Tal1 and regulates
RT megakaryopoiesis and B-cell homeostasis.";
RL Blood 113:3461-3471(2009).
RN [19]
RP INTERACTION WITH LIPN1.
RX PubMed=19753306; DOI=10.1371/journal.pone.0007031;
RA Liu G.H., Gerace L.;
RT "Sumoylation regulates nuclear localization of lipin-1alpha in neuronal
RT cells.";
RL PLoS ONE 4:E7031-E7031(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-110; SER-222
RP AND SER-240, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108 (ISOFORMS 4
RP AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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).
RN [21]
RP INTERACTION WITH AKAP13.
RX PubMed=20139090; DOI=10.1074/jbc.m110.106856;
RA Mayers C.M., Wadell J., McLean K., Venere M., Malik M., Shibata T.,
RA Driggers P.H., Kino T., Guo X.C., Koide H., Gorivodsky M., Grinberg A.,
RA Mukhopadhyay M., Abu-Asab M., Westphal H., Segars J.H.;
RT "The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential for
RT cardiac development in mice.";
RL J. Biol. Chem. 285:12344-12354(2010).
RN [22]
RP INTERACTION WITH FOXK1.
RX PubMed=22956541; DOI=10.1242/jcs.105239;
RA Shi X., Wallis A.M., Gerard R.D., Voelker K.A., Grange R.W., DePinho R.A.,
RA Garry M.G., Garry D.J.;
RT "Foxk1 promotes cell proliferation and represses myogenic differentiation
RT by regulating Foxo4 and Mef2.";
RL J. Cell Sci. 125:5329-5337(2012).
RN [23]
RP INTERACTION WITH JPH2.
RX PubMed=30409805; DOI=10.1126/science.aan3303;
RA Guo A., Wang Y., Chen B., Wang Y., Yuan J., Zhang L., Hall D., Wu J.,
RA Shi Y., Zhu Q., Chen C., Thiel W.H., Zhan X., Weiss R.M., Zhan F.,
RA Musselman C.A., Pufall M., Zhu W., Au K.F., Hong J., Anderson M.E.,
RA Grueter C.E., Song L.S.;
RT "E-C coupling structural protein junctophilin-2 encodes a stress-adaptive
RT transcription regulator.";
RL Science 0:0-0(2018).
CC -!- FUNCTION: Transcription activator which binds specifically to the MEF2
CC element present in the regulatory regions of many muscle-specific
CC genes. Controls cardiac morphogenesis and myogenesis, and is also
CC involved in vascular development. Enhances transcriptional activation
CC mediated by SOX18 (PubMed:11554755). May also be involved in
CC neurogenesis and in the development of cortical architecture. Isoforms
CC that lack the repressor domain are more active than isoform 1 (By
CC similarity). Plays an essential role in hippocampal-dependent learning
CC and memory by suppressing the number of excitatory synapses and thus
CC regulating basal and evoked synaptic transmission. Crucial for normal
CC neuronal development, distribution, and electrical activity in the
CC neocortex. Necessary for proper development of megakaryocytes and
CC platelets and for bone marrow B-lymphopoiesis. Required for B-cell
CC survival and proliferation in response to BCR stimulation, efficient
CC IgG1 antibody responses to T-cell-dependent antigens and for normal
CC induction of germinal center B-cells. {ECO:0000250|UniProtKB:Q06413,
CC ECO:0000269|PubMed:11554755, ECO:0000269|PubMed:18086704,
CC ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599437,
CC ECO:0000269|PubMed:18599438, ECO:0000269|PubMed:19211936,
CC ECO:0000269|PubMed:9162005, ECO:0000269|PubMed:9778514}.
CC -!- SUBUNIT: Forms a complex with class II HDACs in undifferentiating
CC cells. On myogenic differentiation, HDACs are released into the
CC cytoplasm allowing MEF2s to interact with other proteins for
CC activation. Interacts with EP300 in differentiating cells; the
CC interaction acetylates MEF2C leading to increased DNA binding and
CC activation (By similarity). Interacts with HDAC7 and CARM1
CC (PubMed:11279209, PubMed:11713257). Interacts with HDAC4, HDAC7 AND
CC HDAC9; the interaction with HDACs represses transcriptional activity
CC (By similarity). Interacts with LPIN1 (PubMed:19753306). Interacts with
CC MYOCD (PubMed:16818234). Interacts with AKAP13 (PubMed:20139090).
CC Interacts with FOXK1; the interaction inhibits MEF2C transactivation
CC activity (PubMed:22956541). Interacts (via N-terminus) with HABP4; this
CC interaction decreases DNA-binding activity of MEF2C in myocardial cells
CC in response to mechanical stress (By similarity). Interacts with JPH2;
CC interaction specifically takes place with the Junctophilin-2 N-terminal
CC fragment cleavage product of JPH2 (PubMed:30409805). Interacts (via
CC MADS box) with SOX18 (PubMed:11554755).
CC {ECO:0000250|UniProtKB:A0A096MJY4, ECO:0000250|UniProtKB:Q06413,
CC ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11554755,
CC ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:16818234,
CC ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:20139090,
CC ECO:0000269|PubMed:22956541, ECO:0000269|PubMed:30409805}.
CC -!- INTERACTION:
CC Q8CFN5; Q9QZR5: Hipk2; NbExp=5; IntAct=EBI-643797, EBI-366905;
CC Q8CFN5; Q8WUI4: HDAC7; Xeno; NbExp=2; IntAct=EBI-643797, EBI-1048378;
CC Q8CFN5-4; Q91V92: Acly; NbExp=3; IntAct=EBI-643822, EBI-644049;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11554755}. Cytoplasm,
CC sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q8CFN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CFN5-2; Sequence=VSP_012504;
CC Name=3;
CC IsoId=Q8CFN5-3; Sequence=VSP_012505;
CC Name=4;
CC IsoId=Q8CFN5-4; Sequence=VSP_012501, VSP_012502, VSP_012503,
CC VSP_012504, VSP_012505;
CC Name=5;
CC IsoId=Q8CFN5-5; Sequence=VSP_012501, VSP_012502, VSP_012503;
CC -!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to
CC skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta
CC domain-lacking isoforms are the most predominantly expressed in all
CC tissues including skeletal and cardiac muscle and brain. Only brain
CC expresses all isoforms. Expression occurs primarily in the internal
CC granule cell layer of the olfactory bulb, cortex, thalamus, hippocampus
CC and cerebellum. Low levels in the cerebellum and hindbrain. Expressed
CC throughout the cortex, including the frontal and entorhinal cortex,
CC dentate gyrus, and basolateral amygdala. Selectively expressed in B-
CC cells but not in T-cells, and its expression increases as B-cells
CC mature. {ECO:0000269|PubMed:15340086, ECO:0000269|PubMed:15834131,
CC ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599438,
CC ECO:0000269|PubMed:8506376, ECO:0000269|PubMed:9013788}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing endothelial cells and
CC smooth muscle cells, as well as in surrounding mesenchyme, during
CC embryogenesis. Up-regulated during myogenesis.
CC {ECO:0000269|PubMed:9778514}.
CC -!- DOMAIN: The beta domain, missing in a number of isoforms, is required
CC for enhancement of transcriptional activity. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By
CC similarity). Phosphorylation on Ser-396 is required for Lys-391
CC sumoylation and inhibits transcriptional activity. {ECO:0000250,
CC ECO:0000269|PubMed:8663403}.
CC -!- PTM: Acetylated by p300 on several sites in diffentiating myocytes (By
CC similarity). Acetylation on Lys-4 increases DNA binding and
CC transactivation. {ECO:0000250, ECO:0000269|PubMed:18086704}.
CC -!- PTM: Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses
CC transcriptional activity. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved in cerebellar granule neurons, probably by
CC caspase 7, following neurotoxicity. Preferentially cleaves the CDK5-
CC mediated hyperphosphorylated form which leads to neuron apoptosis and
CC transcriptional inactivation (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show impairment in hippocampal-dependent
CC learning and also increase in the number of excitatory synapses and
CC potentiation of basal and evoked synaptic transmission. Mice surviving
CC to adulthood manifest smaller, apparently less mature neurons and
CC smaller whole brain size, with resultant aberrant electrophysiology and
CC behavior. Mice exhibit thrombocytopenia and a defect in B-
CC lymphopoiesis. {ECO:0000269|PubMed:18599437,
CC ECO:0000269|PubMed:18599438, ECO:0000269|PubMed:19211936}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR EMBL; AK009139; BAB26099.1; -; mRNA.
DR EMBL; BC026841; AAH26841.1; -; mRNA.
DR EMBL; BC037731; AAH37731.1; -; mRNA.
DR EMBL; BC057650; AAH57650.1; -; mRNA.
DR CCDS; CCDS26664.1; -. [Q8CFN5-4]
DR CCDS; CCDS49320.1; -. [Q8CFN5-2]
DR CCDS; CCDS84042.1; -. [Q8CFN5-1]
DR CCDS; CCDS84043.1; -. [Q8CFN5-3]
DR CCDS; CCDS84045.1; -. [Q8CFN5-5]
DR RefSeq; NP_001334493.1; NM_001347564.1. [Q8CFN5-1]
DR RefSeq; NP_001334495.1; NM_001347566.1. [Q8CFN5-1]
DR RefSeq; NP_001334496.1; NM_001347567.1. [Q8CFN5-1]
DR RefSeq; NP_001334497.1; NM_001347568.1. [Q8CFN5-5]
DR RefSeq; NP_001334498.1; NM_001347569.1. [Q8CFN5-5]
DR RefSeq; NP_001334500.1; NM_001347571.1. [Q8CFN5-3]
DR RefSeq; NP_001334501.1; NM_001347572.1. [Q8CFN5-3]
DR RefSeq; NP_001334502.1; NM_001347573.1. [Q8CFN5-3]
DR RefSeq; NP_001334503.1; NM_001347574.1. [Q8CFN5-3]
DR RefSeq; NP_001334504.1; NM_001347575.1. [Q8CFN5-3]
DR RefSeq; NP_001334505.1; NM_001347576.1. [Q8CFN5-3]
DR RefSeq; NP_001334506.1; NM_001347577.1. [Q8CFN5-3]
DR RefSeq; NP_079558.1; NM_025282.3. [Q8CFN5-4]
DR RefSeq; XP_006517186.1; XM_006517123.2. [Q8CFN5-1]
DR RefSeq; XP_006517187.1; XM_006517124.3. [Q8CFN5-1]
DR RefSeq; XP_006517189.1; XM_006517126.2. [Q8CFN5-5]
DR RefSeq; XP_006517195.1; XM_006517132.3. [Q8CFN5-4]
DR RefSeq; XP_011242794.1; XM_011244492.2. [Q8CFN5-1]
DR RefSeq; XP_017170894.1; XM_017315405.1. [Q8CFN5-1]
DR PDB; 5F28; X-ray; 2.90 A; A/B/C/D=1-95.
DR PDBsum; 5F28; -.
DR AlphaFoldDB; Q8CFN5; -.
DR SMR; Q8CFN5; -.
DR BioGRID; 201383; 13.
DR DIP; DIP-49524N; -.
DR ELM; Q8CFN5; -.
DR IntAct; Q8CFN5; 10.
DR MINT; Q8CFN5; -.
DR STRING; 10090.ENSMUSP00000132547; -.
DR iPTMnet; Q8CFN5; -.
DR PhosphoSitePlus; Q8CFN5; -.
DR MaxQB; Q8CFN5; -.
DR PaxDb; Q8CFN5; -.
DR PeptideAtlas; Q8CFN5; -.
DR PRIDE; Q8CFN5; -.
DR ProteomicsDB; 292210; -. [Q8CFN5-1]
DR ProteomicsDB; 292211; -. [Q8CFN5-2]
DR ProteomicsDB; 292212; -. [Q8CFN5-3]
DR ProteomicsDB; 292213; -. [Q8CFN5-4]
DR ProteomicsDB; 292214; -. [Q8CFN5-5]
DR Antibodypedia; 755; 1349 antibodies from 36 providers.
DR DNASU; 17260; -.
DR Ensembl; ENSMUST00000185052; ENSMUSP00000138826; ENSMUSG00000005583. [Q8CFN5-5]
DR Ensembl; ENSMUST00000197146; ENSMUSP00000143227; ENSMUSG00000005583. [Q8CFN5-3]
DR Ensembl; ENSMUST00000197681; ENSMUSP00000143420; ENSMUSG00000005583. [Q8CFN5-3]
DR Ensembl; ENSMUST00000198199; ENSMUSP00000143742; ENSMUSG00000005583. [Q8CFN5-4]
DR Ensembl; ENSMUST00000199019; ENSMUSP00000143401; ENSMUSG00000005583. [Q8CFN5-1]
DR Ensembl; ENSMUST00000199105; ENSMUSP00000143212; ENSMUSG00000005583. [Q8CFN5-1]
DR Ensembl; ENSMUST00000199450; ENSMUSP00000143315; ENSMUSG00000005583. [Q8CFN5-2]
DR GeneID; 17260; -.
DR KEGG; mmu:17260; -.
DR UCSC; uc007rie.2; mouse. [Q8CFN5-4]
DR UCSC; uc007rih.2; mouse. [Q8CFN5-5]
DR UCSC; uc007rii.3; mouse. [Q8CFN5-3]
DR CTD; 4208; -.
DR MGI; MGI:99458; Mef2c.
DR VEuPathDB; HostDB:ENSMUSG00000005583; -.
DR eggNOG; KOG0014; Eukaryota.
DR GeneTree; ENSGT00940000157492; -.
DR InParanoid; Q8CFN5; -.
DR PhylomeDB; Q8CFN5; -.
DR TreeFam; TF314067; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17260; 2 hits in 28 CRISPR screens.
DR ChiTaRS; Mef2c; mouse.
DR PRO; PR:Q8CFN5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CFN5; protein.
DR Bgee; ENSMUSG00000005583; Expressed in barrel cortex and 321 other tissues.
DR ExpressionAtlas; Q8CFN5; baseline and differential.
DR Genevisible; Q8CFN5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001782; P:B cell homeostasis; IMP:UniProtKB.
DR GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IGI:MGI.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR GO; GO:0003211; P:cardiac ventricle formation; IMP:UniProtKB.
DR GO; GO:0060536; P:cartilage morphogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0071838; P:cell proliferation in bone marrow; IGI:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
DR GO; GO:0035984; P:cellular response to trichostatin A; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; IMP:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0002467; P:germinal center formation; IMP:UniProtKB.
DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0007521; P:muscle cell fate determination; IMP:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0030279; P:negative regulation of ossification; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0072160; P:nephron tubule epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0014033; P:neural crest cell differentiation; IMP:UniProtKB.
DR GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
DR GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000111; P:positive regulation of macrophage apoptotic process; IMP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; ISO:MGI.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0003138; P:primary heart field specification; IMP:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0002634; P:regulation of germinal center formation; IMP:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0060297; P:regulation of sarcomere organization; IMP:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0060025; P:regulation of synaptic activity; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0061333; P:renal tubule morphogenesis; IMP:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0060021; P:roof of mouth development; IGI:MGI.
DR GO; GO:0003139; P:secondary heart field specification; IMP:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:MGI.
DR GO; GO:0003185; P:sinoatrial valve morphogenesis; IMP:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0097492; P:sympathetic neuron axon guidance; IMP:MGI.
DR GO; GO:0060290; P:transdifferentiation; ISO:MGI.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:UniProtKB.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR022102; HJURP_C.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF12347; HJURP_C; 1.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
KW Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..474
FT /note="Myocyte-specific enhancer factor 2C"
FT /id="PRO_0000199434"
FT DOMAIN 3..57
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 58..86
FT /note="Mef2-type"
FT /evidence="ECO:0000255"
FT REGION 91..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..278
FT /note="Beta domain"
FT /evidence="ECO:0000250"
FT REGION 368..399
FT /note="Transcription repressor"
FT /evidence="ECO:0000250"
FT REGION 375..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 433..434
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18086704"
FT MOD_RES 59
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:8663403"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 239
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 293
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 300
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 396
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 420
FT /note="Phosphoserine; by MAPK7"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 87..97
FT /note="TLRKKGLNGCD -> ALNKKENKGSE (in isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012501"
FT VAR_SEQ 103..118
FT /note="ADDSVGHSPESEDKYR -> SSYALTPRTEEKYK (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012502"
FT VAR_SEQ 123..134
FT /note="DIDLMISRQRLC -> EFDNMIKSHKIP (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012503"
FT VAR_SEQ 271..278
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8506376"
FT /id="VSP_012504"
FT VAR_SEQ 368..399
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012505"
FT MUTAGEN 3
FT /note="R->T: Increased mobility in differentiating cells.
FT Greatly reduced DNA binding."
FT /evidence="ECO:0000269|PubMed:18086704"
FT MUTAGEN 4
FT /note="K->Q: 7-fold increase in DNA binding."
FT /evidence="ECO:0000269|PubMed:18086704"
FT MUTAGEN 4
FT /note="K->R: Reduced acetylation by 30%. Some loss of DNA
FT binding and transactivation activity."
FT /evidence="ECO:0000269|PubMed:18086704"
FT MUTAGEN 59..60
FT /note="ST->CR: Reduced DNA binding activity."
FT MUTAGEN 59..60
FT /note="ST->DD: Enhanced DNA binding activity."
FT MUTAGEN 59
FT /note="S->A: Reduced DNA binding activity."
FT /evidence="ECO:0000269|PubMed:8663403"
FT MUTAGEN 59
FT /note="S->D: Enhanced DNA binding activity."
FT /evidence="ECO:0000269|PubMed:8663403"
FT CONFLICT 141
FT /note="F -> L (in Ref. 3; AAH37731)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="C -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 22..38
FT /evidence="ECO:0007829|PDB:5F28"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5F28"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5F28"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:5F28"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5F28"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5F28"
FT MOD_RES Q8CFN5-4:108
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CFN5-5:108
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 474 AA; 51278 MW; CEFC2DB21E89632A CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI
NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN
SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS
PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT
PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP
SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD RTTTPSRYPQ HTTRHEAGRS
PVDSLSSCSS SYDGSDREDH RNEFHSPIGL TRPSPDERES PSVKRMRLSE GWAT
