MYRF_XENLA
ID MYRF_XENLA Reviewed; 1092 AA.
AC Q66IV1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myelin regulatory factor;
DE EC=3.4.-.-;
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=mrf;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q3UR85,
CC ECO:0000250|UniProtKB:Q9Y2G1}.
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:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- FUNCTION: [Myelin regulatory factor, N-terminal]: Transcription factor
CC that specifically activates expression of myelin genes during
CC oligodendrocyte (OL) maturation, thereby playing a central role in
CC oligodendrocyte maturation and CNS myelination.
CC {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q3UR85,
CC ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor]: Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q3UR85,
CC ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, N-terminal]: Nucleus
CC {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}.
CC Note=Translocates from the cytoplasm to the nucleus upon autocatalytic
CC cleavage. {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor, C-terminal]:
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3UR85,
CC ECO:0000250|UniProtKB:Q9Y2G1}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q3UR85, ECO:0000250|UniProtKB:Q9Y2G1}.
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:0000250|UniProtKB:Q3UR85, 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. {ECO:0000250|UniProtKB:Q3UR85,
CC ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
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DR EMBL; BC081179; AAH81179.1; -; mRNA.
DR RefSeq; NP_001087759.1; NM_001094290.1.
DR AlphaFoldDB; Q66IV1; -.
DR SMR; Q66IV1; -.
DR GeneID; 447583; -.
DR KEGG; xla:447583; -.
DR CTD; 447583; -.
DR OrthoDB; 311898at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 447583; Expressed in stomach and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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; 2.
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 2: Evidence at transcript level;
KW Activator; 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..1092
FT /note="Myelin regulatory factor"
FT /id="PRO_0000318921"
FT CHAIN 1..552
FT /note="Myelin regulatory factor, N-terminal"
FT /evidence="ECO:0000250|UniProtKB:Q3UR85,
FT ECO:0000250|UniProtKB:Q9Y2G1"
FT /id="PRO_0000424314"
FT CHAIN 553..1092
FT /note="Myelin regulatory factor, C-terminal"
FT /evidence="ECO:0000250|UniProtKB:Q3UR85,
FT ECO:0000250|UniProtKB:Q9Y2G1"
FT /id="PRO_0000424315"
FT TOPO_DOM 1..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..1092
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 553..662
FT /note="Peptidase S74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT DNA_BIND 246..507
FT /note="NDT80"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00850"
FT REGION 145..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..677
FT /evidence="ECO:0000255"
FT COMPBIAS 189..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 552..553
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1092 AA; 120780 MW; 47BD1F6F64AEA5C3 CRC64;
MDVEDENETL RRFFEGHDIN GALEPSNIDT SILEDYISKE DSSEICFPDI PSSVSYASPQ
PCGSSGVHLS SVLSNVGHTG SINSGGVHHL GQQMAVRPGP GPTCGGPPYP PHLNCNNNNA
MLNPKGYPMC MSNQGLPIKA EPKTSYAAGT LPDSPPDSGS EAYSPQQLSD PHLLRTMTPE
NICHITPPSR LEHPPPPHLQ GPLPPHSIHQ QHYPSMQREL YMKVESMMPQ YQNLGPAMPP
ADLHHAQQSQ MLHQLLQQQH GAELPVHPSK KRKHSDSPTN TLREQISNGG MVKSEPGLIQ
DNDSLNGSYL DPNYQSIKWQ PHLQNKWVSL YDASYKELPM LTYKVDADKG FNFSTGDDSF
VCQKKNHFQV TVYIGMIGEP KYVKTPEGIL PIECFFLKLN GVKLEAINQA ISIEQSQSDR
SKRPFHPVTL SLPPDQVTKV TVGRLHFSET TSNNMRKKGK PNPDQRYFLL VVALQVQAQN
QTYLVAAQAS ERIIVRASNP GQFESDSEVL WQRGQLPDTV FHHGRIGINT ERPDEALVVH
GNVKIMGSLM HPSDIRAKES VEEVDTTEQL KRISQMRLVH YHYKPEFAST VGLDENAAET
GVIAQEVQEI LPEAVKESGD LVCANGETIE NFLVVNKERI FMENVGAVKE LCKLTDNLET
RIDELERWSH KLAKLRRLDS MKSTNSHTGS SQFSRAGSVP YKQRPPKVMG KTVPGPAHQS
CVSQRFLQAT IIALVIIMAF SVISMTTLYV LNLRSEDDML GIDGSLTPPG SCTLTFFRQI
HLTLPYALCT GSSQNFDTTQ LKGNTTPPPK ITKSPDWQQD PPLTINLCMD PPCEVVCCPH
ILSSESPTIT RKTSAASAET ISQTDPAPST IIRKAKSRNL DKNRNSLQTL PRPVSPLPPY
TQGKNKHSPN SLPVRDVRKR RSLEEESTPI TPMDRTQGNS NDSRYSLTSL RLLETDALIT
NRSCSSMDTC GSGNYTYKLP ISKYSPLSGS LSLELNSSSP VSVNFCETSK GKGCQEPAAV
TSPRDQSCPQ GTDVCVTQVS PTSHLWSLQL LPSQDFTFHL RVSPPGASGC DDLSIDPSQV
TDYYFRFYRL CD
