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Myelin regulatory factor homolog 2 (EC 3.4.-.-) [Cleaved into: Myelin regulatory factor homolog 2, N-terminal; Myelin regulatory factor homolog 2, C-terminal]

 MYRF2_CAEEL             Reviewed;        1009 AA.
D9PTN5; D9PTN4; G5EF12; Q8MQ67; Q9U3I3;
30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 1.
22-NOV-2017, entry version 58.
RecName: Full=Myelin regulatory factor homolog 2 {ECO:0000303|PubMed:28441531};
EC=3.4.-.- {ECO:0000250|UniProtKB:Q9Y2G1};
Contains:
RecName: Full=Myelin regulatory factor homolog 2, N-terminal {ECO:0000305};
Contains:
RecName: Full=Myelin regulatory factor homolog 2, C-terminal {ECO:0000305};
Name=myrf-2 {ECO:0000303|PubMed:28441531,
ECO:0000312|WormBase:F21A10.2e};
ORFNames=F21A10.2 {ECO:0000312|WormBase:F21A10.2e};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=28441531; DOI=10.1016/j.devcel.2017.03.022;
Meng J., Ma X., Tao H., Jin X., Witvliet D., Mitchell J., Zhu M.,
Dong M.Q., Zhen M., Jin Y., Qi Y.B.;
"Myrf ER-bound transcription factors drive C. elegans synaptic
plasticity via cleavage-dependent nuclear translocation.";
Dev. Cell 41:180-194(2017).
-!- FUNCTION: Myelin regulatory factor homolog 2: Constitutes a
precursor of the transcription factor (PubMed:28441531). Mediates
the autocatalytic cleavage that releases the Myelin regulatory
factor homolog 2, N-terminal component that specifically activates
transcription of genes involved in synaptic rewiring during
nervous system maturation (PubMed:28441531).
{ECO:0000269|PubMed:28441531}.
-!- FUNCTION: Myelin regulatory factor homolog 2, C-terminal:
Membrane-bound part that has no transcription factor activity and
remains attached to the endoplasmic reticulum membrane following
cleavage. {ECO:0000250|UniProtKB:Q9Y2G1}.
-!- FUNCTION: Myelin regulatory factor homolog 2, N-terminal:
Transcription factor that specifically activates expression of
genes involved in synaptic rewiring during nervous system
maturation (PubMed:28441531). Specifically required for dorsal D
(DD) GABAergic motor neurons synaptic rewiring (PubMed:28441531).
Acts in complex with myrf-1 paralog (PubMed:28441531).
{ECO:0000269|PubMed:28441531}.
-!- SUBUNIT: Homotrimer (By similarity). Interacts with myrf-1
(PubMed:28441531). {ECO:0000250|UniProtKB:Q9Y2G1,
ECO:0000269|PubMed:28441531}.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor homolog 2:
Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531};
Single-pass membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor homolog 2, N-
terminal: Nucleus {ECO:0000269|PubMed:28441531}. Cytoplasm
{ECO:0000269|PubMed:28441531}. Note=Translocates from the
cytoplasm to the nucleus upon autocatalytic cleavage.
{ECO:0000269|PubMed:28441531}.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor homolog 2, C-
terminal: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:28441531}; Single-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=e;
IsoId=D9PTN5-1; Sequence=Displayed;
Name=a;
IsoId=D9PTN5-2; Sequence=VSP_059061;
Name=b;
IsoId=D9PTN5-3; Sequence=VSP_059062;
Name=c;
IsoId=D9PTN5-4; Sequence=VSP_059063;
Name=d;
IsoId=D9PTN5-5; Sequence=VSP_059064;
-!- DOMAIN: Myelin regulatory factor: The peptidase S74 domain, also
named Intramolecular Chaperone Auto-processed (ICA) domain or
Intramolecuar Chaperone Domain (ICD), has protease activity and
mediates autocatalytic processing of the protein to generate the
Myelin regulatory factor, N-terminal active transcription factor
and the Myelin regulatory factor, C-terminal components.
{ECO:0000250|UniProtKB:Q9Y2G1}.
-!- PTM: Myelin regulatory factor: Follows autocatalytic cleavage via
the peptidase S74 domain. Autoprocessing is apparently
constitutive and is essential for transcriptional activity.
{ECO:0000250|UniProtKB:G5EFI7}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Worms show normal
dorsal D (DD) GABAergic motor neurons rewiring. Worms lacking both
myrf-1 and myrf-2 display defective DD neurons rewiring.
{ECO:0000269|PubMed:28441531}.
-!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BX284606; CAA16508.2; -; Genomic_DNA.
EMBL; BX284606; CAD44121.1; -; Genomic_DNA.
EMBL; BX284606; CAD44122.1; -; Genomic_DNA.
EMBL; BX284606; CBW44371.1; -; Genomic_DNA.
EMBL; BX284606; CBW44372.1; -; Genomic_DNA.
PIR; A89624; A89624.
PIR; T21179; T21179.
RefSeq; NP_001257095.1; NM_001270166.1. [D9PTN5-1]
RefSeq; NP_001257096.1; NM_001270167.1. [D9PTN5-5]
RefSeq; NP_509709.2; NM_077308.4. [D9PTN5-4]
RefSeq; NP_741883.1; NM_171761.1. [D9PTN5-3]
RefSeq; NP_741884.1; NM_171762.3. [D9PTN5-2]
UniGene; Cel.23054; -.
SMR; D9PTN5; -.
IntAct; D9PTN5; 4.
STRING; 6239.F21A10.2e; -.
EPD; D9PTN5; -.
PaxDb; D9PTN5; -.
PeptideAtlas; D9PTN4; -.
EnsemblMetazoa; F21A10.2a.1; F21A10.2a.1; WBGene00008999. [D9PTN5-2]
EnsemblMetazoa; F21A10.2a.2; F21A10.2a.2; WBGene00008999. [D9PTN5-2]
EnsemblMetazoa; F21A10.2a.3; F21A10.2a.3; WBGene00008999. [D9PTN5-2]
EnsemblMetazoa; F21A10.2b; F21A10.2b; WBGene00008999. [D9PTN5-3]
EnsemblMetazoa; F21A10.2c; F21A10.2c; WBGene00008999. [D9PTN5-4]
EnsemblMetazoa; F21A10.2d; F21A10.2d; WBGene00008999. [D9PTN5-5]
EnsemblMetazoa; F21A10.2e; F21A10.2e; WBGene00008999. [D9PTN5-1]
GeneID; 181229; -.
CTD; 181229; -.
WormBase; F21A10.2a; CE23678; WBGene00008999; myrf-2.
WormBase; F21A10.2b; CE31488; WBGene00008999; myrf-2.
WormBase; F21A10.2c; CE31489; WBGene00008999; myrf-2.
WormBase; F21A10.2d; CE18624; WBGene00008999; myrf-2.
WormBase; F21A10.2e; CE45261; WBGene00008999; myrf-2.
eggNOG; KOG3661; Eukaryota.
eggNOG; ENOG410XPRK; LUCA.
GeneTree; ENSGT00530000063626; -.
HOGENOM; HOG000016756; -.
InParanoid; D9PTN5; -.
OMA; LKWQPYQ; -.
OrthoDB; EOG091G0213; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00008999; -.
ExpressionAtlas; D9PTN5; baseline.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1904799; P:regulation of neuron remodeling; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.40.1390; -; 2.
InterPro; IPR026932; MRF_C1.
InterPro; IPR025719; MRF_C2.
InterPro; IPR024061; NDT80_DNA-bd_dom.
InterPro; IPR037141; NDT80_DNA-bd_dom_sf.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030392; S74_ICA.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF13887; MRF_C1; 1.
Pfam; PF13888; MRF_C2; 1.
Pfam; PF05224; NDT80_PhoG; 1.
Pfam; PF13884; Peptidase_S74; 1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51688; ICA; 1.
PROSITE; PS51517; NDT80; 1.
3: Inferred from homology;
Activator; Alternative splicing; Autocatalytic cleavage;
Complete proteome; Cytoplasm; Differentiation; DNA-binding;
Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Nucleus;
Protease; Reference proteome; Transcription; Transcription regulation;
Transmembrane; Transmembrane helix.
CHAIN 1 1009 Myelin regulatory factor homolog 2.
/FTId=PRO_0000441328.
CHAIN 1 559 Myelin regulatory factor homolog 2, N-
terminal. {ECO:0000250|UniProtKB:G5EFI7}.
/FTId=PRO_0000441329.
CHAIN 560 1009 Myelin regulatory factor homolog 2, C-
terminal. {ECO:0000250|UniProtKB:G5EFI7}.
/FTId=PRO_0000441330.
TOPO_DOM 1 736 Cytoplasmic. {ECO:0000305}.
TRANSMEM 737 757 Helical. {ECO:0000255}.
TOPO_DOM 758 1009 Lumenal. {ECO:0000305}.
DOMAIN 560 659 Peptidase S74. {ECO:0000255|PROSITE-
ProRule:PRU01025}.
DNA_BIND 223 514 NDT80. {ECO:0000255|PROSITE-
ProRule:PRU00850}.
COMPBIAS 123 151 Gln-rich. {ECO:0000255|PROSITE-
ProRule:PRU00006}.
COMPBIAS 169 174 Poly-Ser. {ECO:0000255}.
SITE 559 560 Cleavage; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU01025}.
CARBOHYD 999 999 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1002 1002 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
VAR_SEQ 1 111 Missing (in isoform a).
/FTId=VSP_059061.
VAR_SEQ 1 74 MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTN
LSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKN -> MVRR
PVATRPPK (in isoform b).
/FTId=VSP_059062.
VAR_SEQ 1 74 MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTN
LSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKN -> MLPR
NGYPPGYEEF (in isoform c).
/FTId=VSP_059063.
VAR_SEQ 1 74 MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTN
LSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKN -> MNSC
STPVS (in isoform d).
/FTId=VSP_059064.
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


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