ID   MYRF_HUMAN              Reviewed;        1151 AA.
AC   Q9Y2G1; O43582; Q9P1Q6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Myelin regulatory factor;
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q3UR85};
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=C11orf9, KIAA0954, MRF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   PubMed=10828591; DOI=10.1159/000015552;
RA   Stoehr H., Marquardt A., White K., Weber B.H.F.;
RT   "cDNA cloning and genomic structure of a novel gene (C11orf9) localized to
RT   chromosome 11q12-->q13.1 which encodes a highly conserved, potential
RT   membrane-associated protein.";
RL   Cytogenet. Cell Genet. 88:211-216(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 476-660.
RX   PubMed=9615227; DOI=10.1006/geno.1998.5291;
RA   Cooper P.R., Nowak N.J., Higgins M.J., Church D.M., Shows T.B.;
RT   "Transcript mapping of the human chromosome 11q12-q13.1 gene-rich region
RT   identifies several newly described conserved genes.";
RL   Genomics 49:419-429(1998).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
RP   SUBCELLULAR LOCATION, SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION,
RP   AUTOCATALYTIC CLEAVAGE, TOPOLOGY, MUTAGENESIS OF SER-587; ASP-588; LYS-592;
RP   SER-608; GLY-635; LEU-688 AND LEU-699, FUNCTION, AND DOMAIN.
RX   PubMed=23966832; DOI=10.1371/journal.pbio.1001624;
RA   Li Z., Park Y., Marcotte E.M.;
RT   "A bacteriophage tailspike domain promotes self-cleavage of a human
RT   membrane-bound transcription factor, the myelin regulatory factor MYRF.";
RL   PLoS Biol. 11:E1001624-E1001624(2013).
RN   [8]
RP   INVOLVEMENT IN MMERV, AND VARIANT MMERV ARG-403.
RX   PubMed=29265453; DOI=10.1002/ana.25125;
RA   Kurahashi H., Azuma Y., Masuda A., Okuno T., Nakahara E., Imamura T.,
RA   Saitoh M., Mizuguchi M., Shimizu T., Ohno K., Okumura A.;
RT   "MYRF is associated with encephalopathy with reversible myelin
RT   vacuolization.";
RL   Ann. Neurol. 83:98-106(2018).
RN   [9]
RP   INVOLVEMENT IN CUGS, AND VARIANT CUGS 840-ARG--ASP-1151 DEL.
RX   PubMed=29446546; DOI=10.1002/ajmg.a.38620;
RA   Pinz H., Pyle L.C., Li D., Izumi K., Skraban C., Tarpinian J.,
RA   Braddock S.R., Telegrafi A., Monaghan K.G., Zackai E., Bhoj E.J.;
RT   "De novo variants in Myelin regulatory factor (MYRF) as candidates of a new
RT   syndrome of cardiac and urogenital anomalies.";
RL   Am. J. Med. Genet. A 176:969-972(2018).
RN   [10]
RP   INVOLVEMENT IN CUGS.
RX   PubMed=30070761; DOI=10.1002/ajmg.a.40360;
RA   Chitayat D., Shannon P., Uster T., Nezarati M.M., Schnur R.E., Bhoj E.J.;
RT   "An additional individual with a de novo variant in myelin regulatory
RT   factor (MYRF) with cardiac and urogenital anomalies: Further proof of
RT   causality: Comments on the article by Pinz et al.";
RL   Am. J. Med. Genet. A 176:2041-2043(2018).
RN   [11]
RP   INVOLVEMENT IN CUGS, AND VARIANTS CUGS ARG-435; 596-GLN--ASP-1151 DEL;
RP   ALA-679 AND HIS-695.
RX   PubMed=30532227; DOI=10.1371/journal.pgen.1007822;
RA   Qi H., Yu L., Zhou X., Wynn J., Zhao H., Guo Y., Zhu N., Kitaygorodsky A.,
RA   Hernan R., Aspelund G., Lim F.Y., Crombleholme T., Cusick R., Azarow K.,
RA   Danko M.E., Chung D., Warner B.W., Mychaliska G.B., Potoka D., Wagner A.J.,
RA   ElFiky M., Wilson J.M., Nickerson D., Bamshad M., High F.A., Longoni M.,
RA   Donahoe P.K., Chung W.K., Shen Y.;
RT   "De novo variants in congenital diaphragmatic hernia identify MYRF as a new
RT   syndrome and reveal genetic overlaps with other developmental disorders.";
RL   PLoS Genet. 14:E1007822-E1007822(2018).
RN   [12] {ECO:0007744|PDB:5YHU, ECO:0007744|PDB:5ZHU}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 332-578, MUTAGENESIS OF ARG-454;
RP   ARG-478 AND ARG-530, AND DNA-BINDING.
RX   PubMed=29729323; DOI=10.1016/j.jsb.2018.04.007;
RA   Chen B., Zhu Y., Ye S., Zhang R.;
RT   "Structure of the DNA-binding domain of human myelin-gene regulatory factor
RT   reveals its potential protein-DNA recognition mode.";
RL   J. Struct. Biol. 203:170-178(2018).
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       (PubMed:23966832). {ECO:0000269|PubMed:23966832}.
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:23966832}.
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. Specifically recognizes and binds DNA sequence 5'-CTGGYAC-
CC       3' in the regulatory regions of myelin-specific genes and directly
CC       activates their expression. Not only required during oligodendrocyte
CC       differentiation but is also required on an ongoing basis for the
CC       maintenance of expression of myelin genes and for the maintenance of a
CC       mature, viable oligodendrocyte phenotype (PubMed:23966832).
CC       {ECO:0000269|PubMed:23966832}.
CC   -!- SUBUNIT: Homotrimer (PubMed:23966832). Interacts (via C-terminal
CC       region) with TMEM98; the interaction inhibits MYRF self-cleavage (By
CC       similarity). {ECO:0000250|UniProtKB:Q3UR85,
CC       ECO:0000269|PubMed:23966832}.
CC   -!- INTERACTION:
CC       Q9Y2G1-2; Q9Y2G1-2: MYRF; NbExp=3; IntAct=EBI-16070782, EBI-16070782;
CC   -!- SUBCELLULAR LOCATION: [Myelin regulatory factor]: Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:23966832}; Single-pass membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, N-terminal]: Nucleus
CC       {ECO:0000269|PubMed:23966832}. Cytoplasm {ECO:0000269|PubMed:23966832}.
CC       Note=Translocates from the cytoplasm to the nucleus upon autocatalytic
CC       cleavage. {ECO:0000269|PubMed:23966832}.
CC   -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, C-terminal]:
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966832}; Single-
CC       pass membrane protein {ECO:0000269|PubMed:23966832}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y2G1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2G1-2; Sequence=VSP_031300, VSP_031301, VSP_031302;
CC   -!- TISSUE SPECIFICITY: Expressed in lung, ARPE-19 cell line, brainstem,
CC       uterus and, to a lesser extent, in basal ganglion and liver. Weakly
CC       expressed in cerebellum and retina. {ECO:0000269|PubMed:10828591}.
CC   -!- DOMAIN: [Myelin regulatory factor, N-terminal]: The nuclear
CC       localization signals mediate translocation to the nucleus.
CC       {ECO:0000269|PubMed:23966832}.
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:23966832}.
CC   -!- PTM: [Myelin regulatory factor, C-terminal]: Glycosylated.
CC       {ECO:0000269|PubMed:23966832}.
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:23966832). Autocatalytic
CC       cleavage is inhibited by interaction with TMEM98 (By similarity).
CC       {ECO:0000250|UniProtKB:Q3UR85, ECO:0000269|PubMed:23966832}.
CC   -!- DISEASE: Encephalitis/encephalopathy, mild, with reversible myelin
CC       vacuolization (MMERV) [MIM:618113]: An autosomal dominant disease
CC       characterized by episodes of acute encephalitis associated with
CC       impaired consciousness, delirious behavior, seizures, and reversible
CC       splenial lesions observed on diffusion magnetic resonance imaging. Most
CC       patients completely recover and there are no neurologic sequelae. MMERV
CC       occurs in children and is frequently associated with a trigger, such as
CC       a febrile illness. {ECO:0000269|PubMed:29265453}. Note=The disease may
CC       be caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Cardiac-urogenital syndrome (CUGS) [MIM:618280]: An autosomal
CC       dominant syndrome characterized by partial anomalous pulmonary venous
CC       return, tracheal anomalies, pulmonary hypoplasia, congenital
CC       diaphragmatic hernia, thyroid fibrosis, thymic involution, cleft
CC       spleen, penoscrotal hypospadias, and cryptorchidism.
CC       {ECO:0000269|PubMed:29446546, ECO:0000269|PubMed:30070761,
CC       ECO:0000269|PubMed:30532227}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76798.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF086762; AAF28400.1; -; mRNA.
DR   EMBL; AB023171; BAA76798.2; ALT_INIT; mRNA.
DR   EMBL; CH471076; EAW73968.1; -; Genomic_DNA.
DR   EMBL; AF038536; AAB92668.1; -; mRNA.
DR   CCDS; CCDS31579.1; -. [Q9Y2G1-2]
DR   CCDS; CCDS44622.1; -. [Q9Y2G1-1]
DR   RefSeq; NP_001120864.1; NM_001127392.2. [Q9Y2G1-1]
DR   RefSeq; NP_037411.1; NM_013279.3. [Q9Y2G1-2]
DR   PDB; 5YHU; X-ray; 1.85 A; A/B=332-578.
DR   PDB; 5ZHU; X-ray; 2.20 A; A/B/C=349-531.
DR   PDBsum; 5YHU; -.
DR   PDBsum; 5ZHU; -.
DR   AlphaFoldDB; Q9Y2G1; -.
DR   SMR; Q9Y2G1; -.
DR   BioGRID; 107203; 24.
DR   DIP; DIP-60483N; -.
DR   IntAct; Q9Y2G1; 6.
DR   STRING; 9606.ENSP00000278836; -.
DR   MEROPS; S74.003; -.
DR   GlyCosmos; Q9Y2G1; 5 sites, 1 glycan.
DR   GlyGen; Q9Y2G1; 16 sites, 2 O-linked glycans (12 sites).
DR   iPTMnet; Q9Y2G1; -.
DR   PhosphoSitePlus; Q9Y2G1; -.
DR   SwissPalm; Q9Y2G1; -.
DR   BioMuta; MYRF; -.
DR   DMDM; 182637560; -.
DR   jPOST; Q9Y2G1; -.
DR   MassIVE; Q9Y2G1; -.
DR   MaxQB; Q9Y2G1; -.
DR   PaxDb; 9606-ENSP00000278836; -.
DR   PeptideAtlas; Q9Y2G1; -.
DR   ProteomicsDB; 85759; -. [Q9Y2G1-1]
DR   ProteomicsDB; 85760; -. [Q9Y2G1-2]
DR   Antibodypedia; 14689; 103 antibodies from 16 providers.
DR   DNASU; 745; -.
DR   Ensembl; ENST00000265460.9; ENSP00000265460.5; ENSG00000124920.14. [Q9Y2G1-2]
DR   Ensembl; ENST00000278836.10; ENSP00000278836.4; ENSG00000124920.14. [Q9Y2G1-1]
DR   GeneID; 745; -.
DR   KEGG; hsa:745; -.
DR   MANE-Select; ENST00000278836.10; ENSP00000278836.4; NM_001127392.3; NP_001120864.1.
DR   UCSC; uc001nsc.2; human. [Q9Y2G1-1]
DR   AGR; HGNC:1181; -.
DR   CTD; 745; -.
DR   DisGeNET; 745; -.
DR   GeneCards; MYRF; -.
DR   GeneReviews; MYRF; -.
DR   HGNC; HGNC:1181; MYRF.
DR   HPA; ENSG00000124920; Group enriched (brain, stomach).
DR   MalaCards; MYRF; -.
DR   MIM; 608329; gene.
DR   MIM; 618113; phenotype.
DR   MIM; 618280; phenotype.
DR   neXtProt; NX_Q9Y2G1; -.
DR   OpenTargets; ENSG00000124920; -.
DR   Orphanet; 647811; Cardiac-urogenital syndrome.
DR   PharmGKB; PA25500; -.
DR   VEuPathDB; HostDB:ENSG00000124920; -.
DR   eggNOG; KOG3661; Eukaryota.
DR   GeneTree; ENSGT00530000063626; -.
DR   HOGENOM; CLU_004919_0_0_1; -.
DR   InParanoid; Q9Y2G1; -.
DR   OMA; LCSSYPC; -.
DR   OrthoDB; 2880761at2759; -.
DR   PhylomeDB; Q9Y2G1; -.
DR   TreeFam; TF312888; -.
DR   PathwayCommons; Q9Y2G1; -.
DR   SignaLink; Q9Y2G1; -.
DR   BioGRID-ORCS; 745; 51 hits in 1181 CRISPR screens.
DR   ChiTaRS; MYRF; human.
DR   GeneWiki; Myelin_gene_Regulatory_Factor; -.
DR   GenomeRNAi; 745; -.
DR   Pharos; Q9Y2G1; Tbio.
DR   PRO; PR:Q9Y2G1; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9Y2G1; Protein.
DR   Bgee; ENSG00000124920; Expressed in middle frontal gyrus and 147 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2G1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; ISS:UniProtKB.
DR   GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   CDD; cd10144; Peptidase_S74_CIMCD; 1.
DR   Gene3D; 2.60.40.1390; NDT80 DNA-binding domain; 1.
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_sf.
DR   InterPro; IPR030392; S74_ICA.
DR   PANTHER; PTHR13029:SF16; MYELIN REGULATORY FACTOR; 1.
DR   PANTHER; PTHR13029; UNCHARACTERIZED; 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; p53-like transcription factors; 1.
DR   PROSITE; PS51688; ICA; 1.
DR   PROSITE; PS51517; NDT80; 1.
DR   Genevisible; Q9Y2G1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Autocatalytic cleavage; Coiled coil; Cytoplasm; Differentiation;
KW   Disease variant; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW   Hydrolase; Membrane; Nucleus; Protease; Reference proteome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1151
FT                   /note="Myelin regulatory factor"
FT                   /id="PRO_0000318919"
FT   CHAIN           1..586
FT                   /note="Myelin regulatory factor, N-terminal"
FT                   /evidence="ECO:0000305|PubMed:23966832"
FT                   /id="PRO_0000424310"
FT   CHAIN           587..1151
FT                   /note="Myelin regulatory factor, C-terminal"
FT                   /evidence="ECO:0000305|PubMed:23966832"
FT                   /id="PRO_0000424311"
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..1151
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          55..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..925
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:23966832"
FT   MOTIF           491..494
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   COMPBIAS        82..96
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..136
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..200
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Pro 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:23966832"
FT   MOD_RES         123
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CARBOHYD        919
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1043
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1065
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..15
FT                   /note="MEVVDETEALQRFFE -> MHWLPA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10828591"
FT                   /id="VSP_031300"
FT   VAR_SEQ         803..829
FT                   /note="SFAVSTSCLLALLRPQPPGGSEALCPW -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10828591"
FT                   /id="VSP_031301"
FT   VAR_SEQ         1006..1010
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10828591"
FT                   /id="VSP_031302"
FT   VARIANT         403
FT                   /note="Q -> R (in MMERV; dbSNP:rs1565295286)"
FT                   /evidence="ECO:0000269|PubMed:29265453"
FT                   /id="VAR_081183"
FT   VARIANT         435
FT                   /note="G -> R (in CUGS; dbSNP:rs1565295550)"
FT                   /evidence="ECO:0000269|PubMed:30532227"
FT                   /id="VAR_081884"
FT   VARIANT         596..1151
FT                   /note="Missing (in CUGS)"
FT                   /evidence="ECO:0000269|PubMed:30532227"
FT                   /id="VAR_081885"
FT   VARIANT         679
FT                   /note="V -> A (in CUGS; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:30532227"
FT                   /id="VAR_081886"
FT   VARIANT         695
FT                   /note="R -> H (in CUGS; uncertain significance;
FT                   dbSNP:rs1382225004)"
FT                   /evidence="ECO:0000269|PubMed:30532227"
FT                   /id="VAR_081887"
FT   VARIANT         723
FT                   /note="A -> T (in dbSNP:rs34038946)"
FT                   /id="VAR_038907"
FT   VARIANT         840..1151
FT                   /note="Missing (in CUGS)"
FT                   /evidence="ECO:0000269|PubMed:29446546"
FT                   /id="VAR_081888"
FT   MUTAGEN         454
FT                   /note="R->A: Decreased affinity for DNA."
FT                   /evidence="ECO:0000269|PubMed:29729323"
FT   MUTAGEN         478
FT                   /note="R->A: Decreased affinity for DNA."
FT                   /evidence="ECO:0000269|PubMed:29729323"
FT   MUTAGEN         530
FT                   /note="R->A: Decreased affinity for DNA."
FT                   /evidence="ECO:0000269|PubMed:29729323"
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:23966832"
FT   MUTAGEN         588
FT                   /note="D->A: Reduces autocatalytic cleavage and generation
FT                   of Myelin regulatory factor, N-terminal part."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   MUTAGEN         592
FT                   /note="K->A: Prevents autocatalytic cleavage and generation
FT                   of Myelin regulatory factor, N-terminal part."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   MUTAGEN         608
FT                   /note="S->A: Does not affect autocatalytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   MUTAGEN         635
FT                   /note="G->A: Reduces autocatalytic cleavage and generation
FT                   of Myelin regulatory factor, N-terminal part."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   MUTAGEN         688
FT                   /note="L->A: Does not affect autocatalytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   MUTAGEN         699
FT                   /note="L->A: Prevents autocatalytic cleavage and generation
FT                   of Myelin regulatory factor, N-terminal part."
FT                   /evidence="ECO:0000269|PubMed:23966832"
FT   CONFLICT        478..484
FT                   /note="RLHFSET -> GGCIQRD (in Ref. 5; AAB92668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="R -> K (in Ref. 5; AAB92668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657..658
FT                   /note="FA -> LP (in Ref. 5; AAB92668)"
FT                   /evidence="ECO:0000305"
FT   TURN            346..348
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          376..384
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          386..388
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   TURN            389..392
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          393..397
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          402..410
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          416..419
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          422..425
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          428..437
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          440..445
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          447..450
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          462..464
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          470..483
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          491..494
FT                   /evidence="ECO:0007829|PDB:5ZHU"
FT   STRAND          502..512
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          515..524
FT                   /evidence="ECO:0007829|PDB:5YHU"
FT   STRAND          527..530
FT                   /evidence="ECO:0007829|PDB:5YHU"
SQ   SEQUENCE   1151 AA;  124397 MW;  9875DE9D72B6C50C CRC64;
     MEVVDETEAL QRFFEGHDIN GALEPSNIDT SILEEYISKE DASDLCFPDI SAPASSASYS
     HGQPAMPGSS GVHHLSPPGG GPSPGRHGPL PPPGYGTPLN CNNNNGMGAA PKPFPGGTGP
     PIKAEPKAPY APGTLPDSPP DSGSEAYSPQ QVNEPHLLRT ITPETLCHVG VPSRLEHPPP
     PPAHLPGPPP PPPPPPHYPV LQRDLYMKAE PPIPHYAAMG QGLVPTDLHH TQQSQMLHQL
     LQQHGAELPT HPSKKRKHSE SPPSTLNAQM LNGMIKQEPG TVTALPLHPT RAPSPPWPPQ
     GPLSPGPGSL PLSIARVQTP PWHPPGAPSP GLLQDSDSLS GSYLDPNYQS IKWQPHQQNK
     WATLYDANYK ELPMLTYRVD ADKGFNFSVG DDAFVCQKKN HFQVTVYIGM LGEPKYVKTP
     EGLKPLDCFY LKLHGVKLEA LNQSINIEQS QSDRSKRPFN PVTVNLPPEQ VTKVTVGRLH
     FSETTANNMR KKGKPNPDQR YFMLVVALQA HAQNQNYTLA AQISERIIVR ASNPGQFESD
     SDVLWQRAQV PDTVFHHGRV GINTDRPDEA LVVHGNVKVM GSLMHPSDLR AKEHVQEVDT
     TEQLKRISRM RLVHYRYKPE FAASAGIEAT APETGVIAQE VKEILPEAVK DTGDMVFANG
     KTIENFLVVN KERIFMENVG AVKELCKLTD NLETRIDELE RWSHKLAKLR RLDSLKSTGS
     SGAFSHAGSQ FSRAGSVPHK KRPPKVASKS SSVVPDQACI SQRFLQGTII ALVVVMAFSV
     VSMSTLYVLS LRTEEDLVDT DGSFAVSTSC LLALLRPQPP GGSEALCPWS SQSFGTTQLR
     QSPLTTGLPG IQPSLLLVTT SLTSSAPGSA VRTLDMCSSH PCPVICCSSP TTNPTTGPSL
     GPSFNPGHVL SPSPSPSTNR SGPSQMALLP VTNIRAKSWG LSVNGIGHSK HHKSLEPLAS
     PAVPFPGGQG KAKNSPSLGF HGRARRGALQ SSVGPAEPTW AQGQSASLLA EPVPSLTSIQ
     VLENSMSITS QYCAPGDACR PGNFTYHIPV SSGTPLHLSL TLQMNSSSPV SVVLCSLRSK
     EEPCEEGSLP QSLHTHQDTQ GTSHRWPITI LSFREFTYHF RVALLGQANC SSEALAQPAT
     DYHFHFYRLC D
//