MYRF_HUMAN
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 03-AUG-2022, entry version 144.
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; 22.
DR DIP; DIP-60483N; -.
DR IntAct; Q9Y2G1; 6.
DR STRING; 9606.ENSP00000278836; -.
DR MEROPS; S74.003; -.
DR GlyGen; Q9Y2G1; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2G1; -.
DR PhosphoSitePlus; Q9Y2G1; -.
DR BioMuta; MYRF; -.
DR DMDM; 182637560; -.
DR jPOST; Q9Y2G1; -.
DR MassIVE; Q9Y2G1; -.
DR MaxQB; Q9Y2G1; -.
DR PaxDb; Q9Y2G1; -.
DR PeptideAtlas; Q9Y2G1; -.
DR PRIDE; Q9Y2G1; -.
DR ProteomicsDB; 85759; -. [Q9Y2G1-1]
DR ProteomicsDB; 85760; -. [Q9Y2G1-2]
DR Antibodypedia; 14689; 87 antibodies from 15 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 CTD; 745; -.
DR DisGeNET; 745; -.
DR GeneCards; MYRF; -.
DR HGNC; HGNC:1181; MYRF.
DR HPA; ENSG00000124920; Tissue enhanced (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 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; KEQPCEE; -.
DR OrthoDB; 311898at2759; -.
DR PhylomeDB; Q9Y2G1; -.
DR TreeFam; TF312888; -.
DR PathwayCommons; Q9Y2G1; -.
DR SignaLink; Q9Y2G1; -.
DR BioGRID-ORCS; 745; 44 hits in 1094 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 145 other tissues.
DR ExpressionAtlas; Q9Y2G1; baseline and differential.
DR Genevisible; Q9Y2G1; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
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 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; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30532227"
FT /id="VAR_081886"
FT VARIANT 695
FT /note="R -> H (in CUGS; unknown pathological 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
