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Myocyte-specific enhancer factor 2A (Serum response factor-like protein 1)

 MEF2A_HUMAN             Reviewed;         507 AA.
Q02078; B4DFQ7; F6XG23; O43814; Q14223; Q14224; Q59GX4; Q7Z6C9;
Q96D14;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
30-AUG-2017, entry version 179.
RecName: Full=Myocyte-specific enhancer factor 2A;
AltName: Full=Serum response factor-like protein 1;
Name=MEF2A; Synonyms=MEF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2; RSRFC4 AND RSRFC9),
DNA-BINDING, TISSUE SPECIFICITY, AND DIMERIZATION.
TISSUE=Placenta;
PubMed=1748287; DOI=10.1101/gad.5.12a.2327;
Pollock R., Treisman R.;
"Human SRF-related proteins: DNA-binding properties and potential
regulatory targets.";
Genes Dev. 5:2327-2341(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RSRFC9), AND SEQUENCE REVISION.
Treisman R.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2 AND RSRFC9), AND TISSUE
SPECIFICITY.
TISSUE=Heart, and Skeletal muscle;
PubMed=1516833; DOI=10.1101/gad.6.9.1783;
Yu Y.-T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V.,
Nadal-Ginard B.;
"Human myocyte-specific enhancer factor 2 comprises a group of tissue-
restricted MADS box transcription factors.";
Genes Dev. 6:1783-1798(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RSRFC4 AND RSRFC9).
Suzuki E., Lowry J., Sonoda G., Testa J.R., Walsh K.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
TISSUE=Pancreas, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH MAPK7, AND PHOSPHORYLATION.
PubMed=9753748; DOI=10.1093/nar/26.20.4771;
Yang C.-C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A.;
"Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-
activated protein kinase, ERK5/BMK1.";
Nucleic Acids Res. 26:4771-4777(1998).
[10]
INTERACTION WITH HDAC4 AND HDAC9.
PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J.,
Kouzarides T.;
"HDAC4 deacetylase associates with and represses the MEF2
transcription factor.";
EMBO J. 18:5099-5107(1999).
[11]
PHOSPHORYLATION AT THR-312; THR-319 AND SER-453, FUNCTION,
HETERODIMERIZATION, AND MUTAGENESIS OF THR-312; THR-319; SER-355;
SER-453 AND SER-479.
PubMed=9858528; DOI=10.1128/MCB.19.1.21;
Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F.,
Olson E.N., Ulevitch R.J., Han J.-D.;
"Regulation of the MEF2 family of transcription factors by p38.";
Mol. Cell. Biol. 19:21-30(1999).
[12]
INTERACTION WITH MAPK14, PHOSPHORYLATION AT THR-312 AND THR-319, AND
MUTAGENESIS OF ARG-269; LYS-270; LEU-273; VAL-275; ILE-277 AND
PRO-278.
PubMed=10330143; DOI=10.1128/MCB.19.6.4028;
Yang S.-H., Galanis A., Sharrocks A.D.;
"Targeting of p38 mitogen-activated protein kinases to MEF2
transcription factors.";
Mol. Cell. Biol. 19:4028-4038(1999).
[13]
PHOSPHORYLATION AT THR-312; THR-319 AND SER-355, AND MUTAGENESIS OF
THR-312; THR-319 AND SER-355.
PubMed=10849446; DOI=10.1074/jbc.M001573200;
Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N.,
Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.;
"Big mitogen-activated kinase regulates multiple members of the MEF2
protein family.";
J. Biol. Chem. 275:18534-18540(2000).
[14]
PROTEOLYTIC PROCESSING AT ASP-176; ASP-213 AND ASP-466, FUNCTION, AND
MUTAGENESIS OF ASP-176 AND ASP-213.
PubMed=11904443; DOI=10.1073/pnas.022036399;
Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J.,
Salvesen G.S., Bossy-Wetzel E., Lipton S.A.;
"Dominant-interfering forms of MEF2 generated by caspase cleavage
contribute to NMDA-induced neuronal apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002).
[15]
PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-255.
PubMed=12586839; DOI=10.1074/jbc.M211312200;
Cox D.M., Du M., Marback M., Yang E.C.C., Chan J., Siu K.W.M.,
McDermott J.C.;
"Phosphorylation motifs regulating the stability and function of
myocyte enhancer factor 2A.";
J. Biol. Chem. 278:15297-15303(2003).
[16]
PHOSPHORYLATION AT SER-408, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-408.
PubMed=12691662; DOI=10.1016/S0896-6273(03)00191-0;
Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D.,
Blair L.A.C., Marshall J., Mao Z.;
"Cdk5-mediated inhibition of the protective effects of transcription
factor MEF2 in neurotoxicity-induced apoptosis.";
Neuron 38:33-46(2003).
[17]
INTERACTION WITH SLC2A4RG.
PubMed=14630949; DOI=10.1073/pnas.2432756100;
Knight J.B., Eyster C.A., Griesel B.A., Olson A.L.;
"Regulation of the human GLUT4 gene promoter: interaction between a
transcriptional activator and myocyte enhancer factor 2A.";
Proc. Natl. Acad. Sci. U.S.A. 100:14725-14730(2003).
[18]
FUNCTION OF BETA DOMAIN.
PubMed=15834131; DOI=10.1074/jbc.M502491200;
Zhu B., Ramachandran B., Gulick T.;
"Alternative pre-mRNA splicing governs expression of a conserved
acidic transactivation domain in myocyte enhancer factor 2 factors of
striated muscle and brain.";
J. Biol. Chem. 280:28749-28760(2005).
[19]
PROTEOLYTIC PROCESSING, AND PHOSPHORYLATION.
PubMed=15888658; DOI=10.1523/JNEUROSCI.1331-05.2005;
Tang X., Wang X., Gong X., Tong M., Park D., Xia Z., Mao Z.;
"Cyclin-dependent kinase 5 mediates neurotoxin-induced degradation of
the transcription factor myocyte enhancer factor 2.";
J. Neurosci. 25:4823-4834(2005).
[20]
SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-403.
PubMed=16563226; DOI=10.1111/j.1582-4934.2006.tb00295.x;
Riquelme C., Barthel K.K., Liu X.;
"SUMO-1 modification of MEF2A regulates its transcriptional
activity.";
J. Cell. Mol. Med. 10:132-144(2006).
[21]
SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, AND
MUTAGENESIS OF LYS-403 AND SER-408.
PubMed=16371476; DOI=10.1073/pnas.0503698102;
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,
Nakai A., Sistonen L.;
"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
[22]
PHOSPHORYLATION AT SER-408, AND FUNCTION.
PubMed=16484498; DOI=10.1126/science.1122513;
Shalizi A., Gaudilliere B., Yuan Z., Stegmueller J., Shirogane T.,
Ge Q., Tan Y., Schulman B., Harper J.W., Bonni A.;
"A calcium-regulated MEF2 sumoylation switch controls postsynaptic
differentiation.";
Science 311:1012-1017(2006).
[23]
PHOSPHORYLATION AT THR-312 BY NLK.
PubMed=17785444; DOI=10.1128/MCB.01481-07;
Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,
Shibuya H.;
"Nemo-like kinase-myocyte enhancer factor 2A signaling regulates
anterior formation in Xenopus development.";
Mol. Cell. Biol. 27:7623-7630(2007).
[24]
ACETYLATION, AND INVOLVEMENT IN CARDIAC HYPERTROPHY.
PubMed=18697823; DOI=10.1161/CIRCULATIONAHA.107.760488;
Wei J.Q., Shehadeh L.A., Mitrani J.M., Pessanha M., Slepak T.I.,
Webster K.A., Bishopric N.H.;
"Quantitative control of adaptive cardiac hypertrophy by
acetyltransferase p300.";
Circulation 118:934-946(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-235 AND SER-255,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 (ISOFORMS 6; MEFA AND
RSRFC9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORMS 7
AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
FUNCTION, AND CHROMATIN BINDING.
PubMed=21468593; DOI=10.3892/mmr.2011.465;
Liu X., Jin E.Z., Zhi J.X., Li X.Q.;
"Identification of HZF1 as a novel target gene of the MEF2
transcription factor.";
Mol. Med. Report. 4:465-469(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-255, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
VARIANTS SER-263; LEU-279 AND ASP-283, AND CHARACTERIZATION OF
VARIANTS SER-263; LEU-279 AND ASP-283.
PubMed=15496429; DOI=10.1093/hmg/ddh329;
Bhagavatula M.R.K., Fan C., Shen G.-Q., Cassano J., Plow E.F.,
Topol E.J., Wang Q.;
"Transcription factor MEF2A mutations in patients with coronary artery
disease.";
Hum. Mol. Genet. 13:3181-3188(2004).
[31]
VARIANT LEU-279, AND ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL
INFARCTION.
PubMed=15958500; DOI=10.1136/jmg.2005.035071;
Gonzalez P., Garcia-Castro M., Reguero J.R., Batalla A., Ordonez A.G.,
Palop R.L., Lozano I., Montes M., Alvarez V., Coto E.;
"The Pro279Leu variant in the transcription factor MEF2A is associated
with myocardial infarction.";
J. Med. Genet. 43:167-169(2006).
[32]
VARIANT LEU-279, AND LACK OF ASSOCIATION WITH MYOCARDIAL INFARCTION.
PubMed=18086930; DOI=10.1161/CIRCULATIONAHA.107.728485;
Lieb W., Mayer B., Koenig I.R., Borwitzky I., Goetz A., Kain S.,
Hengstenberg C., Linsel-Nitschke P., Fischer M., Doering A.,
Wichmann H.E., Meitinger T., Kreutz R., Ziegler A., Schunkert H.,
Erdmann J.;
"Lack of association between the MEF2A gene and myocardial
infarction.";
Circulation 117:185-191(2008).
[33]
STRUCTURE BY NMR OF 2-86 IN COMPLEX WITH DNA.
PubMed=10835359; DOI=10.1093/emboj/19.11.2615;
Huang K., Louis J.M., Donaldson L., Lim F.L., Sharrocks A.D.,
Clore G.M.;
"Solution structure of the MEF2A-DNA complex: structural basis for the
modulation of DNA bending and specificity by MADS-box transcription
factors.";
EMBO J. 19:2615-2628(2000).
[34]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-78 IN COMPLEX WITH DNA, AND
DIMERIZATION.
PubMed=10715212; DOI=10.1006/jmbi.2000.3568;
Santelli E., Richmond T.J.;
"Crystal structure of MEF2A core bound to DNA at 1.5 A resolution.";
J. Mol. Biol. 297:437-449(2000).
-!- FUNCTION: Transcriptional activator which binds specifically to
the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-
specific genes. Also involved in the activation of numerous growth
factor- and stress-induced genes. Mediates cellular functions not
only in skeletal and cardiac muscle development, but also in
neuronal differentiation and survival. Plays diverse roles in the
control of cell growth, survival and apoptosis via p38 MAPK
signaling in muscle-specific and/or growth factor-related
transcription. In cerebellar granule neurons, phosphorylated and
sumoylated MEF2A represses transcription of NUR77 promoting
synaptic differentiation. Associates with chromatin to the ZNF16
promoter. {ECO:0000269|PubMed:11904443,
ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15834131,
ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16484498,
ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:21468593,
ECO:0000269|PubMed:9858528}.
-!- SUBUNIT: Binds DNA as a homo- or heterodimer. Dimerizes with
MEF2D. Interacts with HDAC7 (By similarity). Interacts with PIAS1;
the interaction enhances sumoylation. Interacts with HDAC4, HDAC9
and SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the
interaction results in the phosphorylation and transcriptional
activity of MEF2A. {ECO:0000250, ECO:0000269|PubMed:10330143,
ECO:0000269|PubMed:10487761, ECO:0000269|PubMed:10715212,
ECO:0000269|PubMed:10835359, ECO:0000269|PubMed:14630949,
ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:9753748}.
-!- INTERACTION:
Q99697-3:PITX2; NbExp=2; IntAct=EBI-2656305, EBI-1175243;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00251, ECO:0000269|PubMed:12691662,
ECO:0000269|PubMed:16563226}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=MEF2;
IsoId=Q02078-1; Sequence=Displayed;
Name=MEFA;
IsoId=Q02078-2; Sequence=VSP_006240;
Note=Contains a phosphoserine at position 98.
{ECO:0000244|PubMed:18669648};
Name=RSRFC4;
IsoId=Q02078-3; Sequence=VSP_006241, VSP_006242;
Name=RSRFC9;
IsoId=Q02078-4; Sequence=VSP_006240, VSP_006241, VSP_006242;
Note=Contains a phosphoserine at position 98.
{ECO:0000244|PubMed:18669648};
Name=5;
IsoId=Q02078-5; Sequence=VSP_006241;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q02078-6; Sequence=VSP_006240, VSP_006241;
Note=No experimental confirmation available. Contains a
phosphoserine at position 98. {ECO:0000244|PubMed:18669648};
Name=7;
IsoId=Q02078-7; Sequence=VSP_043338, VSP_006240;
Note=No experimental confirmation available. Contains a
phosphoserine at position 30. {ECO:0000244|PubMed:18669648};
Name=8;
IsoId=Q02078-8; Sequence=VSP_046018, VSP_046019, VSP_006241;
Note=No experimental confirmation available. Contains a
phosphoserine at position 30. {ECO:0000244|PubMed:18669648};
-!- TISSUE SPECIFICITY: Isoform MEF2 and isoform MEFA are expressed
only in skeletal and cardiac muscle and in the brain. Isoform
RSRFC4 and isoform RSRFC9 are expressed in all tissues examined.
{ECO:0000269|PubMed:1516833, ECO:0000269|PubMed:1748287}.
-!- PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403
sumoylation thus preventing acetylation at this site.
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization
promotes a switch from sumoylation to acetylation on residue Lys-
403 leading to inhibition of dendrite claw differentiation.
Phosphorylation on Thr-312 and Thr-319 are the main sites involved
in p38 MAPK signaling and activate transcription. Phosphorylated
on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by
MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408
by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional
activation leading to apoptosis of cortical neurons.
Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by
EGF. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:12586839, ECO:0000269|PubMed:12691662,
ECO:0000269|PubMed:15888658, ECO:0000269|PubMed:16371476,
ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:16563226,
ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:9753748,
ECO:0000269|PubMed:9858528}.
-!- PTM: Sumoylation on Lys-403 is enhanced by PIAS1 and represses
transcriptional activity. Phosphorylation on Ser-408 is required
for sumoylation. Has no effect on nuclear location nor on DNA
binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2
and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites
in the cerebellar cortex and promotes their morphogenesis (By
similarity). {ECO:0000250}.
-!- PTM: Acetylation on Lys-403 activates transcriptional activity.
Acetylated by p300 on several sites in diffentiating myocytes.
Acetylation on Lys-4 increases DNA binding and transactivation (By
similarity). Hyperacetylation by p300 leads to enhanced cardiac
myocyte growth and heart failure. {ECO:0000250}.
-!- PTM: Proteolytically cleaved in cerebellar granule neurons on
several sites by caspase 3 and caspase 7 following neurotoxicity.
Preferentially cleaves the CDK5-mediated hyperphosphorylated form
which leads to neuron apoptosis and transcriptional inactivation.
{ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:15888658}.
-!- DISEASE: Coronary artery disease, autosomal dominant, 1 (ADCAD1)
[MIM:608320]: A common heart disease characterized by reduced or
absent blood flow in one or more of the arteries that encircle and
supply the heart. Its most important complication is acute
myocardial infarction. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH53871.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD92222.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y16312; CAA76175.1; -; mRNA.
EMBL; X63381; CAA44979.1; -; mRNA.
EMBL; X68503; CAA48516.1; -; mRNA.
EMBL; X68505; CAA48517.1; -; mRNA.
EMBL; U49020; AAB17195.1; -; Genomic_DNA.
EMBL; U44889; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49012; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49013; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49015; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49016; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49017; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49018; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49019; AAB17195.1; JOINED; Genomic_DNA.
EMBL; U49020; AAB17196.1; -; Genomic_DNA.
EMBL; U44889; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49012; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49013; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49015; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49016; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49017; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49018; AAB17196.1; JOINED; Genomic_DNA.
EMBL; U49019; AAB17196.1; JOINED; Genomic_DNA.
EMBL; AK294207; BAG57518.1; -; mRNA.
EMBL; AB208985; BAD92222.1; ALT_INIT; mRNA.
EMBL; AC015660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013437; AAH13437.1; -; mRNA.
EMBL; BC053871; AAH53871.1; ALT_INIT; mRNA.
CCDS; CCDS45362.1; -. [Q02078-5]
CCDS; CCDS45363.1; -. [Q02078-7]
CCDS; CCDS53978.1; -. [Q02078-6]
CCDS; CCDS58401.1; -. [Q02078-8]
CCDS; CCDS81920.1; -. [Q02078-2]
PIR; C39481; C39481.
PIR; S25831; S25831.
RefSeq; NP_001124399.1; NM_001130927.2. [Q02078-7]
RefSeq; NP_001124400.1; NM_001130928.2. [Q02078-8]
RefSeq; NP_001165365.1; NM_001171894.2. [Q02078-6]
RefSeq; NP_001306135.1; NM_001319206.1. [Q02078-2]
RefSeq; NP_005578.2; NM_005587.3. [Q02078-5]
RefSeq; XP_011519883.1; XM_011521581.2. [Q02078-1]
RefSeq; XP_011519884.1; XM_011521582.2. [Q02078-1]
RefSeq; XP_011519888.1; XM_011521586.2. [Q02078-7]
RefSeq; XP_016877679.1; XM_017022190.1. [Q02078-1]
RefSeq; XP_016877680.1; XM_017022191.1. [Q02078-1]
RefSeq; XP_016877682.1; XM_017022193.1. [Q02078-5]
RefSeq; XP_016877683.1; XM_017022194.1. [Q02078-5]
UniGene; Hs.268675; -.
PDB; 1C7U; NMR; -; A/B=2-86.
PDB; 1EGW; X-ray; 1.50 A; A/B/C/D=2-78.
PDB; 1LEW; X-ray; 2.30 A; B=269-280.
PDB; 3KOV; X-ray; 2.90 A; A/B/I/J=2-91.
PDB; 3MU6; X-ray; 2.43 A; A/B/C/D=2-70.
PDB; 3P57; X-ray; 2.19 A; A/B/C/D/I/J=2-91.
PDBsum; 1C7U; -.
PDBsum; 1EGW; -.
PDBsum; 1LEW; -.
PDBsum; 3KOV; -.
PDBsum; 3MU6; -.
PDBsum; 3P57; -.
ProteinModelPortal; Q02078; -.
SMR; Q02078; -.
BioGrid; 110369; 53.
DIP; DIP-40711N; -.
ELM; Q02078; -.
IntAct; Q02078; 36.
MINT; MINT-104848; -.
STRING; 9606.ENSP00000346389; -.
iPTMnet; Q02078; -.
PhosphoSitePlus; Q02078; -.
BioMuta; MEF2A; -.
EPD; Q02078; -.
MaxQB; Q02078; -.
PaxDb; Q02078; -.
PeptideAtlas; Q02078; -.
PRIDE; Q02078; -.
DNASU; 4205; -.
Ensembl; ENST00000338042; ENSP00000337202; ENSG00000068305. [Q02078-6]
Ensembl; ENST00000354410; ENSP00000346389; ENSG00000068305. [Q02078-5]
Ensembl; ENST00000449277; ENSP00000399460; ENSG00000068305. [Q02078-8]
Ensembl; ENST00000557785; ENSP00000453441; ENSG00000068305. [Q02078-6]
Ensembl; ENST00000557942; ENSP00000453095; ENSG00000068305. [Q02078-2]
Ensembl; ENST00000558812; ENSP00000454120; ENSG00000068305. [Q02078-7]
GeneID; 4205; -.
KEGG; hsa:4205; -.
UCSC; uc002bve.4; human. [Q02078-1]
CTD; 4205; -.
DisGeNET; 4205; -.
GeneCards; MEF2A; -.
H-InvDB; HIX0012611; -.
HGNC; HGNC:6993; MEF2A.
HPA; CAB004499; -.
HPA; HPA046597; -.
MalaCards; MEF2A; -.
MIM; 600660; gene.
MIM; 608320; phenotype.
neXtProt; NX_Q02078; -.
OpenTargets; ENSG00000068305; -.
PharmGKB; PA30731; -.
eggNOG; KOG0014; Eukaryota.
eggNOG; COG5068; LUCA.
GeneTree; ENSGT00390000011828; -.
HOGENOM; HOG000230620; -.
HOVERGEN; HBG053944; -.
InParanoid; Q02078; -.
KO; K09260; -.
OMA; DPRSDFH; -.
OrthoDB; EOG091G05BY; -.
PhylomeDB; Q02078; -.
TreeFam; TF314067; -.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-375170; CDO in myogenesis.
SignaLink; Q02078; -.
SIGNOR; Q02078; -.
ChiTaRS; MEF2A; human.
EvolutionaryTrace; Q02078; -.
GeneWiki; Myocyte-specific_enhancer_factor_2A; -.
GenomeRNAi; 4205; -.
PMAP-CutDB; Q02078; -.
PRO; PR:Q02078; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000068305; -.
CleanEx; HS_MEF2A; -.
ExpressionAtlas; Q02078; baseline and differential.
Genevisible; Q02078; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0070375; P:ERK5 cascade; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IEP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:BHF-UCL.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0055005; P:ventricular cardiac myofibril assembly; ISS:UniProtKB.
CDD; cd00265; MADS_MEF2_like; 1.
Gene3D; 3.40.1810.10; -; 1.
InterPro; IPR022102; HJURP_C.
InterPro; IPR033896; MADS_MEF2-like.
InterPro; IPR002100; TF_MADSbox.
Pfam; PF12347; HJURP_C; 1.
Pfam; PF00319; SRF-TF; 1.
PRINTS; PR00404; MADSDOMAIN.
SMART; SM00432; MADS; 1.
SUPFAM; SSF55455; SSF55455; 1.
PROSITE; PS00350; MADS_BOX_1; 1.
PROSITE; PS50066; MADS_BOX_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
Complete proteome; Developmental protein; Differentiation;
Disease mutation; DNA-binding; Isopeptide bond; Neurogenesis; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 507 Myocyte-specific enhancer factor 2A.
/FTId=PRO_0000199428.
DOMAIN 3 57 MADS-box. {ECO:0000255|PROSITE-
ProRule:PRU00251}.
DNA_BIND 58 86 Mef2-type. {ECO:0000255}.
REGION 266 283 Required for interaction with MAPKs.
REGION 289 296 Beta domain.
COMPBIAS 4 31 Lys-rich (basic).
COMPBIAS 141 186 Ser/Thr-rich.
COMPBIAS 420 446 Gln/Pro-rich.
SITE 176 177 Cleavage. {ECO:0000305}.
SITE 213 214 Cleavage. {ECO:0000305}.
SITE 466 467 Cleavage. {ECO:0000305}.
MOD_RES 59 59 Phosphoserine; by CK2. {ECO:0000250}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 249 249 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 255 255 Phosphoserine; by MAPK14.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12586839}.
MOD_RES 312 312 Phosphothreonine; by MAPK7 and MAPK14.
{ECO:0000269|PubMed:10330143,
ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:12586839,
ECO:0000269|PubMed:17785444,
ECO:0000269|PubMed:9858528}.
MOD_RES 312 312 Phosphothreonine; by NLK.
{ECO:0000269|PubMed:10330143,
ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:12586839,
ECO:0000269|PubMed:17785444,
ECO:0000269|PubMed:9858528}.
MOD_RES 319 319 Phosphothreonine; by MAPK7 and MAPK14.
{ECO:0000269|PubMed:10330143,
ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:12586839,
ECO:0000269|PubMed:9858528}.
MOD_RES 355 355 Phosphoserine; by MAPK7.
{ECO:0000269|PubMed:10849446}.
MOD_RES 403 403 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q2MJT0}.
MOD_RES 408 408 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:12586839,
ECO:0000269|PubMed:12691662,
ECO:0000269|PubMed:16371476,
ECO:0000269|PubMed:16484498}.
MOD_RES 415 415 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60929}.
MOD_RES 453 453 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:9858528}.
CROSSLNK 403 403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
VAR_SEQ 19 86 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043338.
VAR_SEQ 19 62 VTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYAS
TDM -> TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNE
DSDFIFKRGP (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046018.
VAR_SEQ 63 132 Missing (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046019.
VAR_SEQ 87 132 ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMR
NHKIA -> TLRKKGLNGCESPDADDYFEHSPLSEDRFSKL
NEDSDFIFKRGP (in isoform MEFA, isoform
RSRFC9, isoform 6 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:1516833,
ECO:0000303|PubMed:1748287,
ECO:0000303|Ref.2, ECO:0000303|Ref.6}.
/FTId=VSP_006240.
VAR_SEQ 289 296 Missing (in isoform RSRFC4, isoform
RSRFC9, isoform 5, isoform 6 and isoform
8). {ECO:0000303|PubMed:1516833,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1748287,
ECO:0000303|Ref.2, ECO:0000303|Ref.6}.
/FTId=VSP_006241.
VAR_SEQ 420 421 Missing (in isoform RSRFC4 and isoform
RSRFC9). {ECO:0000303|PubMed:1516833,
ECO:0000303|PubMed:1748287,
ECO:0000303|Ref.2}.
/FTId=VSP_006242.
VARIANT 263 263 N -> S (in dbSNP:rs121918530).
{ECO:0000269|PubMed:15496429}.
/FTId=VAR_038407.
VARIANT 279 279 P -> L (in dbSNP:rs121918529).
{ECO:0000269|PubMed:15496429,
ECO:0000269|PubMed:15958500,
ECO:0000269|PubMed:18086930}.
/FTId=VAR_038408.
VARIANT 283 283 G -> D. {ECO:0000269|PubMed:15496429}.
/FTId=VAR_038409.
VARIANT 440 446 Missing (loss of nuclear localization;
66% decrease in transcription activation;
loss of synergistic activation by MEF2A
and GATA1 through a dominant-negative
mechanism).
/FTId=VAR_017743.
MUTAGEN 176 176 D->A: Abolishes cleavage at sites 1 and 2
by caspase 3. Increased cleavage at site
3 by caspase 3.
{ECO:0000269|PubMed:11904443}.
MUTAGEN 213 213 D->A: Abolishes cleavage at sites 2 and 3
by caspase 7.
{ECO:0000269|PubMed:11904443}.
MUTAGEN 255 255 S->A: Slightly increased MEF2A protein
level. {ECO:0000269|PubMed:12586839}.
MUTAGEN 255 255 S->D: Decreased MEF2A protein level.
{ECO:0000269|PubMed:12586839}.
MUTAGEN 269 269 R->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-270.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 270 270 K->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-269.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 273 273 L->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-275.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 275 275 V->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-273.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 277 277 I->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-278.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 278 278 P->A: Reduced p38 alpha- and beta2-
mediated transcriptional activity; when
associated with A-277.
{ECO:0000269|PubMed:10330143}.
MUTAGEN 312 312 T->A: Greatly reduced p38-mediated
phosphorylation. Abolishes p38-mediated
transcriptional activation; when
associated with A-319.
{ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:9858528}.
MUTAGEN 319 319 T->A: Greatly reduced p38-mediated
phosphorylation. Abolishes P38-mediated
transcriptional activation; when
associated with A-312.
{ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:9858528}.
MUTAGEN 355 355 S->A: No effect on p38-mediated
transcriptional activity.
{ECO:0000269|PubMed:10849446,
ECO:0000269|PubMed:9858528}.
MUTAGEN 387 387 S->A: No effect on p38-mediated
phosphorylation.
MUTAGEN 403 403 K->R: Abolishes sumoylation. No change in
subcellular location nor in DNA binding.
Loss of transcriptional repression.
{ECO:0000269|PubMed:16371476,
ECO:0000269|PubMed:16563226}.
MUTAGEN 408 408 S->A: Loss of sumoylation.
{ECO:0000269|PubMed:12691662,
ECO:0000269|PubMed:16371476}.
MUTAGEN 408 408 S->D: Rescues sumoylation.
{ECO:0000269|PubMed:12691662,
ECO:0000269|PubMed:16371476}.
MUTAGEN 453 453 S->A: No effect on p38-mediated
phosphorylation.
{ECO:0000269|PubMed:9858528}.
MUTAGEN 479 479 S->A: No effect on p38-mediated
phosphorylation.
{ECO:0000269|PubMed:9858528}.
CONFLICT 430 430 Missing (in Ref. 4; AAB17195/AAB17196).
{ECO:0000305}.
HELIX 14 38 {ECO:0000244|PDB:1EGW}.
STRAND 42 48 {ECO:0000244|PDB:1EGW}.
TURN 50 52 {ECO:0000244|PDB:1C7U}.
STRAND 54 60 {ECO:0000244|PDB:1EGW}.
HELIX 62 71 {ECO:0000244|PDB:1EGW}.
STRAND 77 80 {ECO:0000244|PDB:3KOV}.
HELIX 81 90 {ECO:0000244|PDB:3P57}.
SEQUENCE 507 AA; 54811 MW; 362BA4FBCC792CE2 CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE
EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML
SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG
ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR
ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFNSPGMLS
LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI SIKSEPISPP RDRMTPSGFQ
QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP
IVLGRPPNTE DRESPSVKRM RMDAWVT


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