MYEF2_MOUSE
ID MYEF2_MOUSE Reviewed; 591 AA.
AC Q8C854; Q60690; Q6P930; Q6ZPT3; Q8QZZ1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Myelin expression factor 2;
DE Short=MEF-2;
DE Short=MyEF-2;
GN Name=Myef2; Synonyms=Kiaa1341, Mef2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-591 (ISOFORM 4).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 45-591 (ISOFORM 2).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-591 (ISOFORM 2), FUNCTION IN
RP TRANSCRIPTIONAL REPRESSION, AND DNA-BINDING.
RX PubMed=7534248; DOI=10.1016/0378-1119(94)00816-b;
RA Steplewski A., Haas S., Amini S., Khalili K.;
RT "Regulation of mouse myelin basic protein gene transcription by a sequence-
RT specific single-stranded DNA-binding protein in vitro.";
RL Gene 154:215-218(1995).
RN [6]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, DNA-BINDING, AND TISSUE
RP SPECIFICITY.
RX PubMed=7539003; DOI=10.1074/jbc.270.21.12503;
RA Haas S., Steplewski A., Siracusa L.D., Amini S., Khalili K.;
RT "Identification of a sequence-specific single-stranded DNA binding protein
RT that suppresses transcription of the mouse myelin basic protein gene.";
RL J. Biol. Chem. 270:12503-12510(1995).
RN [7]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND SUBUNIT.
RX PubMed=9282330;
RX DOI=10.1002/(sici)1097-4644(19970915)66:4<524::aid-jcb11>3.0.co;2-b;
RA Muralidharan V., Tretiakova A., Steplewski A., Haas S., Amini S.,
RA Johnson E., Khalili K.;
RT "Evidence for inhibition of MyEF-2 binding to MBP promoter by MEF-1/Pur
RT alpha.";
RL J. Cell. Biochem. 66:524-531(1997).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-397 AND ARG-417, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Transcriptional repressor of the myelin basic protein gene
CC (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP
CC promoter. Its binding to MB1 and function are inhibited by PURA.
CC {ECO:0000269|PubMed:7534248, ECO:0000269|PubMed:7539003,
CC ECO:0000269|PubMed:9282330}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9282330}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C854-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C854-3; Sequence=VSP_013455;
CC Name=3;
CC IsoId=Q8C854-1; Sequence=VSP_013457, VSP_013458, VSP_013459;
CC Name=4;
CC IsoId=Q8C854-2; Sequence=VSP_013456, VSP_013460, VSP_013461;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain.
CC {ECO:0000269|PubMed:7539003}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60946.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK048404; BAC33325.1; -; mRNA.
DR EMBL; AK129336; BAC98146.1; ALT_INIT; mRNA.
DR EMBL; BC060946; AAH60946.1; ALT_INIT; mRNA.
DR EMBL; AF483504; AAL90778.1; -; mRNA.
DR EMBL; AF483505; AAL90779.1; -; mRNA.
DR EMBL; U13262; AAA78270.1; -; mRNA.
DR CCDS; CCDS50690.1; -. [Q8C854-3]
DR CCDS; CCDS50691.1; -. [Q8C854-4]
DR PIR; A56704; A56704.
DR RefSeq; NP_001155889.1; NM_001162417.1. [Q8C854-4]
DR RefSeq; XP_006498947.1; XM_006498884.3. [Q8C854-3]
DR RefSeq; XP_017171620.1; XM_017316131.1. [Q8C854-4]
DR RefSeq; XP_017171621.1; XM_017316132.1. [Q8C854-4]
DR RefSeq; XP_017171623.1; XM_017316134.1. [Q8C854-4]
DR AlphaFoldDB; Q8C854; -.
DR SMR; Q8C854; -.
DR BioGRID; 201640; 18.
DR IntAct; Q8C854; 11.
DR MINT; Q8C854; -.
DR STRING; 10090.ENSMUSP00000123088; -.
DR iPTMnet; Q8C854; -.
DR PhosphoSitePlus; Q8C854; -.
DR SwissPalm; Q8C854; -.
DR EPD; Q8C854; -.
DR MaxQB; Q8C854; -.
DR PaxDb; Q8C854; -.
DR PeptideAtlas; Q8C854; -.
DR PRIDE; Q8C854; -.
DR ProteomicsDB; 286095; -. [Q8C854-4]
DR ProteomicsDB; 286096; -. [Q8C854-3]
DR ProteomicsDB; 286097; -. [Q8C854-1]
DR ProteomicsDB; 286098; -. [Q8C854-2]
DR DNASU; 17876; -.
DR Ensembl; ENSMUST00000061419; ENSMUSP00000058811; ENSMUSG00000049230. [Q8C854-2]
DR Ensembl; ENSMUST00000067780; ENSMUSP00000066312; ENSMUSG00000027201. [Q8C854-3]
DR Ensembl; ENSMUST00000110501; ENSMUSP00000106127; ENSMUSG00000027201. [Q8C854-3]
DR Ensembl; ENSMUST00000152367; ENSMUSP00000123088; ENSMUSG00000027201. [Q8C854-4]
DR GeneID; 17876; -.
DR KEGG; mmu:17876; -.
DR UCSC; uc008mbw.2; mouse. [Q8C854-4]
DR UCSC; uc008mby.2; mouse. [Q8C854-3]
DR UCSC; uc012cdb.1; mouse. [Q8C854-2]
DR CTD; 50804; -.
DR MGI; MGI:104592; Myef2.
DR VEuPathDB; HostDB:ENSMUSG00000027201; -.
DR VEuPathDB; HostDB:ENSMUSG00000049230; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000157397; -.
DR HOGENOM; CLU_019566_1_0_1; -.
DR InParanoid; Q8C854; -.
DR OMA; RDRVQQF; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; Q8C854; -.
DR TreeFam; TF313406; -.
DR BioGRID-ORCS; 17876; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Myef2; mouse.
DR PRO; PR:Q8C854; -.
DR Proteomes; UP000000589; Chromosome 2.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C854; protein.
DR Bgee; ENSMUSG00000027201; Expressed in ventricular zone and 240 other tissues.
DR ExpressionAtlas; Q8C854; baseline and differential.
DR Genevisible; Q8C854; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR CDD; cd12658; RRM1_MYEF2; 1.
DR CDD; cd12662; RRM3_MYEF2; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034632; MYEF2.
DR InterPro; IPR034630; MYEF2_RRM1.
DR InterPro; IPR034631; MYEF2_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23003:SF15; PTHR23003:SF15; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transcription; Ubl conjugation.
FT CHAIN 1..591
FT /note="Myelin expression factor 2"
FT /id="PRO_0000081656"
FT DOMAIN 91..169
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 224..301
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 514..590
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 397
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 417
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K5"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2K5"
FT VAR_SEQ 354..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:7534248"
FT /id="VSP_013455"
FT VAR_SEQ 394..451
FT /note="ELYRGAMTSSMERDFGRGDIGLSRGFGDSFGRLGSAMIGGFAGRIGASNMGP
FT VGTGIS -> G (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013456"
FT VAR_SEQ 427..451
FT /note="GSAMIGGFAGRIGASNMGPVGTGIS -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_013457"
FT VAR_SEQ 511..512
FT /note="SK -> RN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_013458"
FT VAR_SEQ 513..591
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_013459"
FT VAR_SEQ 539..555
FT /note="HVMFAEIKMENGKSKGC -> QINRDSKTHSNCGQHHS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013460"
FT VAR_SEQ 556..591
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013461"
FT CONFLICT 341
FT /note="L -> R (in Ref. 5; AAA78270)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="C -> L (in Ref. 5; AAA78270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 63295 MW; 7F30703C519DB9A6 CRC64;
MADADKSEAA AGDDGSQQQP AEPRRDTHPG EPEKPPRSSA NGVKMENDES VKEEKSDLKE
KSTGNKKANR FHPYSKDKNS GTGEKKGPNR NRVFISNIPY DMKWQAIKDL MREKVGEVTY
VELFKDAEGK SRGCGVVEFK DEEFVKKALE TMNKYDLSGR PLNIKEDPDG ENARRALQRT
GTSFQGSHAS DVGSGLVNLP PSILNNPNIP PEVISNLQAG RLGSTIFVAN LDFKVGWKKL
KEVFSIAGTV KRADIKEDKD GKSRGMGTVT FEQAIEAVQA ISMFNGQFLF DRPMHVKMDD
KSVPHEDYRS HDSKTSQLPR GLGGIGMGLG PGGQPISASQ LNITGVMGNL GPSGMGMDGP
GFGGVNRIGG GVGFGGLEAM NSMAGFGGVG RMGELYRGAM TSSMERDFGR GDIGLSRGFG
DSFGRLGSAM IGGFAGRIGA SNMGPVGTGI SGSMSGMSTV TGGMGMGLDR MSSSFDRMGP
GIGAILERSI DVDRGFLSGP MGSGMRDRLG SKGNQIFVRN LPFDLTWQKL KEKFSQCGHV
MFAEIKMENG KSKGCGTVRF ESAESAEKAC RIMNGIKISG REIDVRLDRN A
