MYRF_MOUSE
ID MYRF_MOUSE Reviewed; 1138 AA.
AC Q3UR85; B2RXQ7; F8WJJ9; Q3V3K4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Myelin regulatory factor;
DE EC=3.4.-.- {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291};
DE AltName: Full=Myelin gene regulatory factor;
DE Contains:
DE RecName: Full=Myelin regulatory factor, N-terminal;
DE Contains:
DE RecName: Full=Myelin regulatory factor, C-terminal;
GN Name=Myrf; Synonyms=Gm1804, Gm98, Mrf;
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 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 525-1138 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19596243; DOI=10.1016/j.cell.2009.04.031;
RA Emery B., Agalliu D., Cahoy J.D., Watkins T.A., Dugas J.C., Mulinyawe S.B.,
RA Ibrahim A., Ligon K.L., Rowitch D.H., Barres B.A.;
RT "Myelin gene regulatory factor is a critical transcriptional regulator
RT required for CNS myelination.";
RL Cell 138:172-185(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22956843; DOI=10.1523/jneurosci.1069-12.2012;
RA Koenning M., Jackson S., Hay C.M., Faux C., Kilpatrick T.J., Willingham M.,
RA Emery B.;
RT "Myelin gene regulatory factor is required for maintenance of myelin and
RT mature oligodendrocyte identity in the adult CNS.";
RL J. Neurosci. 32:12528-12542(2012).
RN [6]
RP SUBCELLULAR LOCATION, SUBUNIT, PROTEOLYTIC PROCESSING, CATALYTIC ACTIVITY,
RP DNA-BINDING, AND MUTAGENESIS OF 254-LYS--ARG-257; LYS-399; ARG-454;
RP ARG-478; SER-587 AND LYS-592.
RX PubMed=23966833; DOI=10.1371/journal.pbio.1001625;
RA Bujalka H., Koenning M., Jackson S., Perreau V.M., Pope B., Hay C.M.,
RA Mitew S., Hill A.F., Lu Q.R., Wegner M., Srinivasan R., Svaren J.,
RA Willingham M., Barres B.A., Emery B.;
RT "MYRF is a membrane-associated transcription factor that
RT autoproteolytically cleaves to directly activate myelin genes.";
RL PLoS Biol. 11:E1001625-E1001625(2013).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=24204311; DOI=10.1371/journal.pgen.1003907;
RA Hornig J., Froeb F., Vogl M.R., Hermans-Borgmeyer I., Tamm E.R., Wegner M.;
RT "The transcription factors Sox10 and Myrf define an essential regulatory
RT network module in differentiating oligodendrocytes.";
RL PLoS Genet. 9:E1003907-E1003907(2013).
RN [8]
RP FUNCTION.
RX PubMed=27532821; DOI=10.1002/glia.23044;
RA Muth K.N., Piefke S., Weider M., Sock E., Hermans-Borgmeyer I., Wegner M.,
RA Kuespert M.;
RT "The dual-specificity phosphatase Dusp15 is regulated by Sox10 and Myrf in
RT myelinating oligodendrocytes.";
RL Glia 64:2120-2132(2016).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-384.
RX PubMed=28441531; DOI=10.1016/j.devcel.2017.03.022;
RA Meng J., Ma X., Tao H., Jin X., Witvliet D., Mitchell J., Zhu M.,
RA Dong M.Q., Zhen M., Jin Y., Qi Y.B.;
RT "Myrf ER-bound transcription factors drive C. elegans synaptic plasticity
RT via cleavage-dependent nuclear translocation.";
RL Dev. Cell 41:180-194(2017).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP TMEM98, AND PROTEOLYTIC PROCESSING.
RX PubMed=30249802; DOI=10.1523/jneurosci.0154-18.2018;
RA Huang H., Teng P., Du J., Meng J., Hu X., Tang T., Zhang Z., Qi Y.B.,
RA Qiu M.;
RT "Interactive Repression of MYRF Self-Cleavage and Activity in
RT Oligodendrocyte Differentiation by TMEM98 Protein.";
RL J. Neurosci. 38:9829-9839(2018).
RN [11] {ECO:0007744|PDB:5H5P}
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 351-532, CATALYTIC ACTIVITY,
RP FUNCTION, PROTEOLYTIC PROCESSING, SUBUNIT, AND MUTAGENESIS OF
RP 439-GLU--LEU-441; GLU-469 AND SER-587.
RX PubMed=28623291; DOI=10.1038/s41598-017-03768-9;
RA Zhen X., Li B., Hu F., Yan S., Meloni G., Li H., Shi N.;
RT "Crystal structure of the DNA-binding domain of Myelin-gene Regulatory
RT Factor.";
RL Sci. Rep. 7:3696-3696(2017).
CC -!- FUNCTION: [Myelin regulatory factor]: Constitutes a precursor of the
CC transcription factor. Mediates the autocatalytic cleavage that releases
CC the Myelin regulatory factor, N-terminal component that specifically
CC activates transcription of central nervous system (CNS) myelin genes.
CC {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291}.
CC -!- FUNCTION: [Myelin regulatory factor, C-terminal]: Membrane-bound part
CC that has no transcription factor activity and remains attached to the
CC endoplasmic reticulum membrane following cleavage.
CC {ECO:0000269|PubMed:23966833}.
CC -!- FUNCTION: [Myelin regulatory factor, N-terminal]: Transcription factor
CC that specifically activates expression of myelin genes such as MBP,
CC MOG, MAG, DUSP15 and PLP1 during oligodendrocyte (OL) maturation,
CC thereby playing a central role in oligodendrocyte maturation and CNS
CC myelination (PubMed:19596243, PubMed:22956843, PubMed:23966833,
CC PubMed:24204311, PubMed:27532821). Specifically recognizes and binds
CC DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific
CC genes and directly activates their expression. Not only required during
CC oligodendrocyte differentiation but is also required on an ongoing
CC basis for the maintenance of expression of myelin genes and for the
CC maintenance of a mature, viable oligodendrocyte phenotype
CC (PubMed:19596243, PubMed:22956843, PubMed:23966833).
CC {ECO:0000269|PubMed:19596243, ECO:0000269|PubMed:22956843,
CC ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:24204311,
CC ECO:0000269|PubMed:27532821}.
CC -!- SUBUNIT: Homotrimer (PubMed:23966833, PubMed:28623291). Interacts (via
CC C-terminal region) with TMEM98; the interaction inhibits MYRF self-
CC cleavage (PubMed:30249802). {ECO:0000269|PubMed:23966833,
CC ECO:0000269|PubMed:28623291, ECO:0000269|PubMed:30249802}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor]: Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802};
CC Single-pass membrane protein.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, N-terminal]: Nucleus
CC {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28441531,
CC ECO:0000269|PubMed:30249802}. Cytoplasm {ECO:0000269|PubMed:23966833}.
CC Note=Translocates from the cytoplasm to the nucleus upon autocatalytic
CC cleavage. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, C-terminal]:
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833,
CC ECO:0000269|PubMed:30249802}; Single-pass membrane protein
CC {ECO:0000269|PubMed:23966833}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UR85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UR85-2; Sequence=VSP_031303, VSP_031304;
CC Name=3;
CC IsoId=Q3UR85-3; Sequence=VSP_053374;
CC Name=4;
CC IsoId=Q3UR85-5; Sequence=VSP_053992, VSP_053993;
CC -!- TISSUE SPECIFICITY: Specifically expressed by postmitotic
CC oligodendrocytes in the CNS. Not detected in the peripheral nervous
CC system (PNS). {ECO:0000269|PubMed:19596243,
CC ECO:0000269|PubMed:30249802}.
CC -!- DEVELOPMENTAL STAGE: At postnatal day 3 (P3), the expression is
CC restricted to cells in the hindbrain and cerebellum, subsequently
CC spreading rostrally throughout the white matter tracks over the first 2
CC weeks postnatal, mirroring the expression of Plp1.
CC {ECO:0000269|PubMed:19596243}.
CC -!- INDUCTION: Expression is directly regulated by SOX10.
CC {ECO:0000269|PubMed:24204311}.
CC -!- DOMAIN: [Myelin regulatory factor, N-terminal]: The nuclear
CC localization signals mediate translocation to the nucleus.
CC {ECO:0000269|PubMed:23966833}.
CC -!- DOMAIN: [Myelin regulatory factor]: The peptidase S74 domain, also
CC named Intramolecular Chaperone Auto-processed (ICA) domain or
CC Intramolecular Chaperone Domain (ICD), has protease activity and
CC mediates autocatalytic processing of the protein to generate the Myelin
CC regulatory factor, N-terminal active transcription factor and the
CC Myelin regulatory factor, C-terminal components.
CC {ECO:0000269|PubMed:23966833}.
CC -!- PTM: [Myelin regulatory factor, C-terminal]: Glycosylated.
CC {ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- PTM: [Myelin regulatory factor]: Follows autocatalytic cleavage via the
CC peptidase S74 domain. Autoprocessing is apparently constitutive and is
CC essential for transcriptional activity (PubMed:23966833,
CC PubMed:28623291, PubMed:30249802). Autocatalytic cleavage is inhibited
CC by interaction with TMEM98 (PubMed:30249802).
CC {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291,
CC ECO:0000269|PubMed:30249802}.
CC -!- DISRUPTION PHENOTYPE: Embryos die around 12.5 dpc. Conditional knockout
CC mice in which Mrf is lacking within the oligodendrocyte lineage display
CC severe deficits in myelin gene expression and premyelinating
CC oligodendrocytes fail to myelinate. These mice display severe
CC neurological abnormalities and die because of seizures during the third
CC postnatal week. {ECO:0000269|PubMed:19596243,
CC ECO:0000269|PubMed:22956843}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. Dubious isoform due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
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DR EMBL; AK039649; BAE20548.1; -; mRNA.
DR EMBL; AK141695; BAE24803.1; -; mRNA.
DR EMBL; AC132148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC157942; AAI57943.1; -; mRNA.
DR CCDS; CCDS50387.1; -. [Q3UR85-3]
DR RefSeq; NP_001028653.1; NM_001033481.1. [Q3UR85-3]
DR RefSeq; XP_006526992.1; XM_006526929.3. [Q3UR85-1]
DR PDB; 5H5P; X-ray; 2.46 A; A=351-532.
DR PDB; 7DC3; X-ray; 2.40 A; A/B/C=539-717.
DR PDBsum; 5H5P; -.
DR PDBsum; 7DC3; -.
DR AlphaFoldDB; Q3UR85; -.
DR SMR; Q3UR85; -.
DR BioGRID; 230445; 1.
DR STRING; 10090.ENSMUSP00000139601; -.
DR GlyGen; Q3UR85; 3 sites.
DR iPTMnet; Q3UR85; -.
DR PhosphoSitePlus; Q3UR85; -.
DR SwissPalm; Q3UR85; -.
DR CPTAC; non-CPTAC-3480; -.
DR MaxQB; Q3UR85; -.
DR PaxDb; Q3UR85; -.
DR PeptideAtlas; Q3UR85; -.
DR PRIDE; Q3UR85; -.
DR ProteomicsDB; 287540; -. [Q3UR85-1]
DR ProteomicsDB; 287541; -. [Q3UR85-2]
DR ProteomicsDB; 287542; -. [Q3UR85-3]
DR ProteomicsDB; 287543; -. [Q3UR85-5]
DR Antibodypedia; 14689; 87 antibodies from 15 providers.
DR Ensembl; ENSMUST00000088013; ENSMUSP00000085329; ENSMUSG00000036098. [Q3UR85-1]
DR Ensembl; ENSMUST00000186056; ENSMUSP00000140871; ENSMUSG00000036098. [Q3UR85-5]
DR Ensembl; ENSMUST00000189897; ENSMUSP00000139601; ENSMUSG00000036098. [Q3UR85-3]
DR GeneID; 225908; -.
DR KEGG; mmu:225908; -.
DR UCSC; uc008gpk.2; mouse. [Q3UR85-1]
DR UCSC; uc012bil.1; mouse. [Q3UR85-3]
DR UCSC; uc012bim.1; mouse. [Q3UR85-5]
DR CTD; 745; -.
DR MGI; MGI:2684944; Myrf.
DR VEuPathDB; HostDB:ENSMUSG00000036098; -.
DR eggNOG; KOG3661; Eukaryota.
DR GeneTree; ENSGT00530000063626; -.
DR HOGENOM; CLU_004919_0_0_1; -.
DR InParanoid; Q3UR85; -.
DR OMA; KEQPCEE; -.
DR OrthoDB; 311898at2759; -.
DR PhylomeDB; Q3UR85; -.
DR TreeFam; TF312888; -.
DR BioGRID-ORCS; 225908; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Myrf; mouse.
DR PRO; PR:Q3UR85; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UR85; protein.
DR Bgee; ENSMUSG00000036098; Expressed in pyloric antrum and 124 other tissues.
DR ExpressionAtlas; Q3UR85; baseline and differential.
DR Genevisible; Q3UR85; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0032286; P:central nervous system myelin maintenance; IMP:UniProtKB.
DR GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IDA:GO_Central.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR Gene3D; 2.60.40.1390; -; 1.
DR InterPro; IPR026933; MRF.
DR InterPro; IPR025719; MYRF_C2.
DR InterPro; IPR026932; MYRF_ICA.
DR InterPro; IPR024061; NDT80_DNA-bd_dom.
DR InterPro; IPR037141; NDT80_DNA-bd_dom_sf.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030392; S74_ICA.
DR PANTHER; PTHR13029:SF16; PTHR13029:SF16; 1.
DR Pfam; PF13888; MRF_C2; 1.
DR Pfam; PF13887; MYRF_ICA; 1.
DR Pfam; PF05224; NDT80_PhoG; 1.
DR Pfam; PF13884; Peptidase_S74; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS51688; ICA; 1.
DR PROSITE; PS51517; NDT80; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Autocatalytic cleavage; Coiled coil; Cytoplasm; Differentiation;
KW DNA-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Nucleus; Protease; Reference proteome; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..1138
FT /note="Myelin regulatory factor"
FT /id="PRO_0000318920"
FT CHAIN 1..586
FT /note="Myelin regulatory factor, N-terminal"
FT /evidence="ECO:0000305|PubMed:23966833"
FT /id="PRO_0000424312"
FT CHAIN 587..1138
FT /note="Myelin regulatory factor, C-terminal"
FT /evidence="ECO:0000305|PubMed:23966833"
FT /id="PRO_0000424313"
FT TOPO_DOM 1..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..1138
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 587..696
FT /note="Peptidase S74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT DNA_BIND 250..541
FT /note="NDT80"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00850"
FT REGION 56..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..1003
FT /note="Required for interaction with TMEM98"
FT /evidence="ECO:0000269|PubMed:30249802"
FT REGION 891..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 680..711
FT /evidence="ECO:0000255"
FT MOTIF 254..257
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23966833"
FT MOTIF 491..494
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23966833"
FT COMPBIAS 82..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 586..587
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025,
FT ECO:0000269|PubMed:23966833"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G1"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 46..247
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053992"
FT VAR_SEQ 779
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031303"
FT VAR_SEQ 780..1138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031304"
FT VAR_SEQ 803..829
FT /note="SLAVSTSCLLALLRPQDPGGSEAMCPW -> R (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053374"
FT VAR_SEQ 829
FT /note="W -> CR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053993"
FT MUTAGEN 254..256
FT /note="KKR->AAA: Abolishes nuclear localization."
FT MUTAGEN 384
FT /note="G->R: Does not affect subcellular location. Impaired
FT DNA-binding."
FT /evidence="ECO:0000269|PubMed:28441531"
FT MUTAGEN 399
FT /note="K->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:23966833"
FT MUTAGEN 439..441
FT /note="Missing: Loss of trimerization; when associated with
FT R-469."
FT /evidence="ECO:0000269|PubMed:28623291"
FT MUTAGEN 454
FT /note="R->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:23966833"
FT MUTAGEN 469
FT /note="E->R: Loss of trimerization; when associated with
FT 439-E--L-441 DEL."
FT /evidence="ECO:0000269|PubMed:28623291"
FT MUTAGEN 478
FT /note="R->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:23966833"
FT MUTAGEN 587
FT /note="S->A: Prevents autocatalytic cleavage and generation
FT of Myelin regulatory factor, N-terminal part."
FT /evidence="ECO:0000269|PubMed:23966833,
FT ECO:0000269|PubMed:28623291"
FT MUTAGEN 587
FT /note="S->C: Does not affect autocatalytic cleavage and
FT generation of Myelin regulatory factor, N-terminal part."
FT /evidence="ECO:0000269|PubMed:23966833"
FT MUTAGEN 592
FT /note="K->H,R,M: Prevents autocatalytic cleavage and
FT generation of Myelin regulatory factor, N-terminal part."
FT /evidence="ECO:0000269|PubMed:23966833"
FT CONFLICT 860
FT /note="K -> N (in Ref. 3; AAI57943)"
FT /evidence="ECO:0000305"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5H5P"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5H5P"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 470..483
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 502..512
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 515..524
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:5H5P"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 600..609
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 619..624
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 638..644
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:7DC3"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:7DC3"
FT HELIX 671..704
FT /evidence="ECO:0007829|PDB:7DC3"
SQ SEQUENCE 1138 AA; 123288 MW; A59CDDA18CDE7054 CRC64;
MEVVDETEAL QRFFEGHDIS GALEPSNIDT SILEEYIGKE DASDLCFPEI SAPASTASFP
HGPPAIPGSS GLHHLSPPGS GPSPGRHGPL PPPTYGTPLN CNNNNGMGTA PKPFLGGSGP
PIKAEPKAPY APGTLPDSPP DSGSEAYSPQ QVNDPHLLRT ITPETLCHVG VSSRLEHPPP
PPAHLPGPPP PPPPPPHYPV LQRDLYMKAE PPVPPYAAMG PGLVPPELHH TQQTQVLHQL
LQQHGAELPP HPSKKRKHSE SPPNTLNAQM LNGMIKQEPG TVTALPPHPA RAPSPPWPPQ
GPLSPGTGSL PLSIARAQTP PWHPPGAPSP GLLQDSDSLS GSYLDPNYQS IKWQPHQQNK
WATLYDANYK ELPMLTYRVD ADKGFNFSVG DDAFVCQKKN HFQVTVYIGM LGEPKYVKTP
EGLKPLDCFY LKLHGVKLEA LNQSINIEQS QSDRSKRPFN PVTVNLPPEQ VTKVTVGRLH
FSETTANNMR KKGKPNPDQR YFMLVVALQA HAQNQNYTLA AQISERIIVR ASNPGQFESD
SDVLWQRAQL PDTVFHHGRV GINTDRPDEA LVVHGNVKVM GSLMHPSDLR AKEHVQEVDT
TEQLKRISRM RLVHYRYKPE FAASAGIEAT APETGVIAQE VKEILPEAVK DTGDVVFANG
KTIENFLVVN KERIFMENVG AVKELCKLTD NLETRIDELE RWSHKLAKLR RLDSLKSTGS
SGAFSHAGSQ FSRAGSVPHK KRPPKLANKS SPAVPDQACI SQRFLQGTII ALVVVMAFSV
VSMSTLYVLS LRSEEDLVDA DGSLAVSTSC LLALLRPQDP GGSEAMCPWS SQSFGTTQLR
QSSMTTGLPG TQPSLLLVTK SASGPALRAL DLCSSQPCPI VCCSPPVSSP ATDPALGPTL
TPTPSPSSNP KHSGPGQMAP LPVTNIRAKS WGISANGISY SKHSKSLEPL ASPVVPFPGG
QSKTKNSPSF NLQSRARRGA PQPSPSPAQF TQTQGQLDPA PSLTSIQLLE NSMPITSQYC
VPEGACRLGN FTYHIPVSSS TPLHLSLTLQ MNSSTPVSVV LCSLTSEEEP CEEGGFLQRF
HPHQDTQGTS HQWPVTILSF REFTYHFRVT LLGQANCSSE AIVQPATDYY FHFYRLCD
