Detail Information for IndEnz0002015527
IED ID IndEnz0002015527
Enzyme Type ID protease015527
Protein Name Myelin regulatory factor
EC 3.4.-.-
Myelin gene regulatory factor

Cleaved into: Myelin regulatory factor, N-terminal; Myelin regulatory factor, C-terminal
Gene Name Myrf Gm1804 Gm98 Mrf
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MEVVDETEALQRFFEGHDISGALEPSNIDTSILEEYIGKEDASDLCFPEISAPASTASFPHGPPAIPGSSGLHHLSPPGSGPSPGRHGPLPPPTYGTPLNCNNNNGMGTAPKPFLGGSGPPIKAEPKAPYAPGTLPDSPPDSGSEAYSPQQVNDPHLLRTITPETLCHVGVSSRLEHPPPPPAHLPGPPPPPPPPPHYPVLQRDLYMKAEPPVPPYAAMGPGLVPPELHHTQQTQVLHQLLQQHGAELPPHPSKKRKHSESPPNTLNAQMLNGMIKQEPGTVTALPPHPARAPSPPWPPQGPLSPGTGSLPLSIARAQTPPWHPPGAPSPGLLQDSDSLSGSYLDPNYQSIKWQPHQQNKWATLYDANYKELPMLTYRVDADKGFNFSVGDDAFVCQKKNHFQVTVYIGMLGEPKYVKTPEGLKPLDCFYLKLHGVKLEALNQSINIEQSQSDRSKRPFNPVTVNLPPEQVTKVTVGRLHFSETTANNMRKKGKPNPDQRYFMLVVALQAHAQNQNYTLAAQISERIIVRASNPGQFESDSDVLWQRAQLPDTVFHHGRVGINTDRPDEALVVHGNVKVMGSLMHPSDLRAKEHVQEVDTTEQLKRISRMRLVHYRYKPEFAASAGIEATAPETGVIAQEVKEILPEAVKDTGDVVFANGKTIENFLVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHKLAKLRRLDSLKSTGSSGAFSHAGSQFSRAGSVPHKKRPPKLANKSSPAVPDQACISQRFLQGTIIALVVVMAFSVVSMSTLYVLSLRSEEDLVDADGSLAVSTSCLLALLRPQDPGGSEAMCPWSSQSFGTTQLRQSSMTTGLPGTQPSLLLVTKSASGPALRALDLCSSQPCPIVCCSPPVSSPATDPALGPTLTPTPSPSSNPKHSGPGQMAPLPVTNIRAKSWGISANGISYSKHSKSLEPLASPVVPFPGGQSKTKNSPSFNLQSRARRGAPQPSPSPAQFTQTQGQLDPAPSLTSIQLLENSMPITSQYCVPEGACRLGNFTYHIPVSSSTPLHLSLTLQMNSSTPVSVVLCSLTSEEEPCEEGGFLQRFHPHQDTQGTSHQWPVTILSFREFTYHFRVTLLGQANCSSEAIVQPATDYYFHFYRLCD
Enzyme Length 1138
Uniprot Accession Number Q3UR85
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 250..541; /note=NDT80; /evidence=ECO:0000255|PROSITE-ProRule:PRU00850
EC Number 3.4.-.-
Enzyme Function FUNCTION: [Myelin regulatory factor]: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291}.; FUNCTION: [Myelin regulatory factor, C-terminal]: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. {ECO:0000269|PubMed:23966833}.; FUNCTION: [Myelin regulatory factor, N-terminal]: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG, DUSP15 and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination (PubMed:19596243, PubMed:22956843, PubMed:23966833, PubMed:24204311, PubMed:27532821). Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:19596243, PubMed:22956843, PubMed:23966833). {ECO:0000269|PubMed:19596243, ECO:0000269|PubMed:22956843, ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:24204311, ECO:0000269|PubMed:27532821}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (5); Beta strand (17); Chain (3); Coiled coil (1); Compositional bias (4); DNA binding (1); Domain (1); Glycosylation (3); Helix (1); Modified residue (1); Motif (2); Mutagenesis (10); Region (8); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1)
Keywords 3D-structure;Acetylation;Activator;Alternative splicing;Autocatalytic cleavage;Coiled coil;Cytoplasm;DNA-binding;Differentiation;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Nucleus;Protease;Reference proteome;Transcription;Transcription regulation;Transmembrane;Transmembrane helix
Interact With
Induction INDUCTION: Expression is directly regulated by SOX10. {ECO:0000269|PubMed:24204311}.
Subcellular Location SUBCELLULAR LOCATION: [Myelin regulatory factor]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Myelin regulatory factor, N-terminal]: Nucleus {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28441531, ECO:0000269|PubMed:30249802}. Cytoplasm {ECO:0000269|PubMed:23966833}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}.; SUBCELLULAR LOCATION: [Myelin regulatory factor, C-terminal]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}; Single-pass membrane protein {ECO:0000269|PubMed:23966833}.
Modified Residue MOD_RES 123; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9Y2G1
Post Translational Modification PTM: [Myelin regulatory factor, C-terminal]: Glycosylated. {ECO:0000250|UniProtKB:Q9Y2G1}.; PTM: [Myelin regulatory factor]: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity (PubMed:23966833, PubMed:28623291, PubMed:30249802). Autocatalytic cleavage is inhibited by interaction with TMEM98 (PubMed:30249802). {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291, ECO:0000269|PubMed:30249802}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 5H5P; 7DC3;
Mapped Pubmed ID 14610273; 17967808; 18799693; 21267068; 21938520; 22365546; 23332759; 23575864; 24257626; 25324381; 25568100; 25680202; 25789755; 26395480; 26525805; 26928066; 27149841; 27455109; 28160598; 28336932; 28695847; 29361054; 29472293; 29500351; 29556912; 30076300; 30166609; 30996143; 31048900; 31081019; 31753579; 31828317; 32042175; 32075970; 32236127; 32266943; 32270922; 32290105; 33472075; 33646289; 34345217; 34615523;
Motif MOTIF 254..257; /note=Nuclear localization signal; /evidence=ECO:0000269|PubMed:23966833; MOTIF 491..494; /note=Nuclear localization signal; /evidence=ECO:0000269|PubMed:23966833
Gene Encoded By
Mass 123,288
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda