MYRF2_CAEEL
ID MYRF2_CAEEL Reviewed; 1009 AA.
AC D9PTN5; D9PTN4; G5EF12; Q8MQ67; Q9U3I3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Myelin regulatory factor homolog 2 {ECO:0000303|PubMed:28441531};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q9Y2G1};
DE Contains:
DE RecName: Full=Myelin regulatory factor homolog 2, N-terminal {ECO:0000305};
DE Contains:
DE RecName: Full=Myelin regulatory factor homolog 2, C-terminal {ECO:0000305};
GN Name=myrf-2 {ECO:0000303|PubMed:28441531, ECO:0000312|WormBase:F21A10.2e};
GN ORFNames=F21A10.2 {ECO:0000312|WormBase:F21A10.2e};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [3]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 729-LYS--VAL-1009.
RX PubMed=33950834; DOI=10.7554/elife.67628;
RA Xia S.L., Li M., Chen B., Wang C., Yan Y.H., Dong M.Q., Qi Y.B.;
RT "The LRR-TM protein PAN-1 interacts with MYRF to promote its nuclear
RT translocation in synaptic remodeling.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: [Myelin regulatory factor homolog 2]: Constitutes a precursor
CC of the transcription factor (PubMed:28441531). Mediates the
CC autocatalytic cleavage that releases the Myelin regulatory factor
CC homolog 2, N-terminal component that specifically activates
CC transcription of genes involved in synaptic rewiring during nervous
CC system maturation (PubMed:28441531). {ECO:0000269|PubMed:28441531}.
CC -!- FUNCTION: [Myelin regulatory factor homolog 2, C-terminal]: Membrane-
CC bound part that has no transcription factor activity and remains
CC attached to the endoplasmic reticulum membrane following cleavage.
CC {ECO:0000250|UniProtKB:Q9Y2G1}.
CC -!- FUNCTION: [Myelin regulatory factor homolog 2, N-terminal]:
CC Transcription factor that specifically activates expression of genes
CC involved in synaptic rewiring during nervous system maturation
CC (PubMed:28441531). Specifically required for dorsal D (DD) GABAergic
CC motor neurons synaptic rewiring (PubMed:28441531). Acts in complex with
CC myrf-1 paralog (PubMed:28441531). {ECO:0000269|PubMed:28441531}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with myrf-1
CC (PubMed:28441531). {ECO:0000250|UniProtKB:Q9Y2G1,
CC ECO:0000269|PubMed:28441531}.
CC -!- INTERACTION:
CC D9PTN5; G5EFI7: myrf-1; NbExp=2; IntAct=EBI-6727439, EBI-6731843;
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2]: Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane
CC protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:33950834}. Apical
CC cell membrane {ECO:0000269|PubMed:33950834}; Single-pass membrane
CC protein {ECO:0000255}. Note=In early L1 larvae, localizes to the cell
CC membrane, but then localizes to the nucleus in late L1 larvae
CC (PubMed:33950834). Cell membrane localization is promoted by pan-1
CC (PubMed:33950834). {ECO:0000269|PubMed:33950834}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, N-terminal]:
CC Nucleus {ECO:0000269|PubMed:28441531}. Cytoplasm
CC {ECO:0000269|PubMed:28441531}. Note=Translocates from the cytoplasm to
CC the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:28441531}.
CC -!- SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, C-terminal]:
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=e {ECO:0000312|WormBase:F21A10.2e};
CC IsoId=D9PTN5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F21A10.2a};
CC IsoId=D9PTN5-2; Sequence=VSP_059061;
CC Name=b {ECO:0000312|WormBase:F21A10.2b};
CC IsoId=D9PTN5-3; Sequence=VSP_059062;
CC Name=c {ECO:0000312|WormBase:F21A10.2c};
CC IsoId=D9PTN5-4; Sequence=VSP_059063;
CC Name=d {ECO:0000312|WormBase:F21A10.2d};
CC IsoId=D9PTN5-5; Sequence=VSP_059064;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in L1 stage larvae.
CC {ECO:0000269|PubMed:33950834}.
CC -!- DOMAIN: Myelin regulatory factor: The peptidase S74 domain, also named
CC Intramolecular Chaperone Auto-processed (ICA) domain or Intramolecular
CC Chaperone Domain (ICD), has protease activity and mediates
CC 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: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:G5EFI7}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Worms show normal dorsal D
CC (DD) GABAergic motor neurons rewiring. Worms lacking both myrf-1 and
CC myrf-2 display defective DD neurons rewiring.
CC {ECO:0000269|PubMed:28441531}.
CC -!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284606; CAA16508.2; -; Genomic_DNA.
DR EMBL; BX284606; CAD44121.1; -; Genomic_DNA.
DR EMBL; BX284606; CAD44122.1; -; Genomic_DNA.
DR EMBL; BX284606; CBW44371.1; -; Genomic_DNA.
DR EMBL; BX284606; CBW44372.1; -; Genomic_DNA.
DR PIR; A89624; A89624.
DR PIR; T21179; T21179.
DR RefSeq; NP_001257095.1; NM_001270166.1. [D9PTN5-1]
DR RefSeq; NP_001257096.1; NM_001270167.1.
DR RefSeq; NP_509709.2; NM_077308.4. [D9PTN5-4]
DR RefSeq; NP_741883.1; NM_171761.1.
DR RefSeq; NP_741884.1; NM_171762.3.
DR AlphaFoldDB; D9PTN5; -.
DR SMR; D9PTN5; -.
DR ComplexPortal; CPX-3521; myrf-1-myrf-2 complex.
DR IntAct; D9PTN5; 5.
DR STRING; 6239.F21A10.2e; -.
DR EPD; D9PTN5; -.
DR PaxDb; D9PTN5; -.
DR EnsemblMetazoa; F21A10.2a.1; F21A10.2a.1; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.2; F21A10.2a.2; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.3; F21A10.2a.3; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.4; F21A10.2a.4; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.5; F21A10.2a.5; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.6; F21A10.2a.6; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2a.7; F21A10.2a.7; WBGene00008999. [D9PTN5-2]
DR EnsemblMetazoa; F21A10.2b.1; F21A10.2b.1; WBGene00008999. [D9PTN5-3]
DR EnsemblMetazoa; F21A10.2c.1; F21A10.2c.1; WBGene00008999. [D9PTN5-4]
DR EnsemblMetazoa; F21A10.2d.1; F21A10.2d.1; WBGene00008999. [D9PTN5-5]
DR EnsemblMetazoa; F21A10.2e.1; F21A10.2e.1; WBGene00008999. [D9PTN5-1]
DR GeneID; 181229; -.
DR KEGG; cel:CELE_F21A10.2; -.
DR UCSC; F21A10.2a.2; c. elegans.
DR CTD; 181229; -.
DR WormBase; F21A10.2a; CE23678; WBGene00008999; myrf-2. [D9PTN5-2]
DR WormBase; F21A10.2b; CE31488; WBGene00008999; myrf-2. [D9PTN5-3]
DR WormBase; F21A10.2c; CE31489; WBGene00008999; myrf-2. [D9PTN5-4]
DR WormBase; F21A10.2d; CE18624; WBGene00008999; myrf-2. [D9PTN5-5]
DR WormBase; F21A10.2e; CE45261; WBGene00008999; myrf-2. [D9PTN5-1]
DR eggNOG; KOG3661; Eukaryota.
DR GeneTree; ENSGT00530000063626; -.
DR InParanoid; D9PTN5; -.
DR OMA; SCERDGT; -.
DR OrthoDB; 311898at2759; -.
DR PhylomeDB; D9PTN5; -.
DR SignaLink; D9PTN5; -.
DR PRO; PR:D9PTN5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008999; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IC:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR GO; GO:1904799; P:regulation of neuron remodeling; IMP:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:ComplexPortal.
DR Gene3D; 2.60.40.1390; -; 2.
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 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 Activator; Alternative splicing; Autocatalytic cleavage; Cell membrane;
KW Cytoplasm; Differentiation; DNA-binding; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Membrane; Nucleus; Protease; Reference proteome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1009
FT /note="Myelin regulatory factor homolog 2"
FT /id="PRO_0000441328"
FT CHAIN 1..559
FT /note="Myelin regulatory factor homolog 2, N-terminal"
FT /evidence="ECO:0000250|UniProtKB:G5EFI7"
FT /id="PRO_0000441329"
FT CHAIN 560..1009
FT /note="Myelin regulatory factor homolog 2, C-terminal"
FT /evidence="ECO:0000250|UniProtKB:G5EFI7"
FT /id="PRO_0000441330"
FT TOPO_DOM 1..736
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..1009
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 560..659
FT /note="Peptidase S74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT DNA_BIND 223..514
FT /note="NDT80"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00850"
FT REGION 161..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 559..560
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform a)"
FT /id="VSP_059061"
FT VAR_SEQ 1..74
FT /note="MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTN
FT LFYITLLQNKLNKYTQQLLKKN -> MVRRPVATRPPK (in isoform b)"
FT /id="VSP_059062"
FT VAR_SEQ 1..74
FT /note="MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTN
FT LFYITLLQNKLNKYTQQLLKKN -> MLPRNGYPPGYEEF (in isoform c)"
FT /id="VSP_059063"
FT VAR_SEQ 1..74
FT /note="MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTN
FT LFYITLLQNKLNKYTQQLLKKN -> MNSCSTPVS (in isoform d)"
FT /id="VSP_059064"
FT MUTAGEN 729..1009
FT /note="Missing: Localizes to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:33950834"
SQ SEQUENCE 1009 AA; 113212 MW; BDD1047BAEC20F9D CRC64;
MGDLNPAETP EPKKNPVAKI ASNLYSTQIV KPVPSVSNST NLSPCQNPNM TNLFYITLLQ
NKLNKYTQQL LKKNEEGLND PLANVEQFNI IQFLQNDVDF NLPIEAFEQG NMDQNIRIDP
ILQRQQMANQ PMLMPQHMLQ QLHQQQIYEQ QLASMPMTPA ITDLTRHGSS SSPSTTNSDP
PYSPEGLNNF GLGTQRPNHG VIPNDISNVP QHINRQFNPR MGPNTSPNPP SFPQFLNSNH
PTPGSYVQSI SPDSNGQGFA QSNLYNALNV SSDESINGSD DIPNRKRPRM DQNMDPSFIM
HAPVSGKLGA EVTEEGGQPN IRFFKYQEEQ WCPMYDANGE ELGRLQVHVL ADKGFNYSTN
DNCFVNQKKN HFQVTVKIEA IDPSPPQCFK INGVCKPIEN FQLSFVGAKS ESQNSEIPIR
QSTTERKPIL HTPVLFKIVE RRMTIVTVPR LHFSETTLNN QRKNLRPNPD QKYFNLVVRL
YATATDGTTV LMQAFASERV IVRATNPGSF EPPEMVDASW NKNGGILSTN GPVVIGKSEP
RAQLTVDGDI YSSGRVMYPS DIRLKDNITE KGAKDALENL QKLRIVDYFY KPEVASKWGL
TEDQRKRTGV IAQELAAVLP DAVKDLGDYL TVNESRVFYE TVLATQELCR LTGDLDQKID
DKVAEISQRL TQYAQKKKML NSMASGLNSE GRSLNASRTS LDSSASALTL TNTKKNRRSS
RKDKKDAPKS KMTHGTVIGL VGVMAFCLLA MSALYILDWH NRNFGYHHFT PSATTSGPKE
GPGNVVIPLD HYVPLRQPDA PPLVPFCPME TCRGYCCMEY DKDHAELEIT EYDPNTATDN
DFGFKADTRS DFTLKGFGNN VKISLPELGM QIDERYCIEK SCVKKRKVYS LFIPMTRYLP
NVPLEVQIDV PSSKVVNNCG YIQEFDNRKC DETGSSSTET DAPRSIQLFD NTFQVSAGQW
TQSAYRFRVG YSTELCSIDD THFGGFYEEY NLIFYRACNR TNSTAINVV
