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Nuclear factor erythroid 2-related factor 2 (NF-E2-related factor 2) (NFE2-related factor 2) (Nuclear factor, erythroid derived 2, like 2)

 NF2L2_BOVIN             Reviewed;         607 AA.
Q5NUA6; Q3T0S8;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
28-MAR-2018, entry version 89.
RecName: Full=Nuclear factor erythroid 2-related factor 2;
Short=NF-E2-related factor 2;
Short=NFE2-related factor 2;
AltName: Full=Nuclear factor, erythroid derived 2, like 2;
Name=NFE2L2; Synonyms=NRF2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Artery;
Hara S., Nishimoto M., Kunimoto M.;
"Characterization of bovine endothelial NF-E2-related factor-2.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-522.
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Transcription activator that binds to antioxidant
response (ARE) elements in the promoter regions of target genes.
Important for the coordinated up-regulation of genes in response
to oxidative stress. May be involved in the transcriptional
activation of genes of the beta-globin cluster by mediating
enhancer activity of hypersensitive site 2 of the beta-globin
locus control region (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer. Forms a ternary complex with PGAM5 and
KEAP1. Interacts via its leucine-zipper domain with the coiled-
coil domain of PMF1. Interacts with EEF1D at heat shock promoter
elements (HSE). Interacts (via the bZIP domain) with MAFK;
required for binding to antioxidant response (ARE) elements on
DNA. Interacts with CHD6; involved in activation of the
transcription (By similarity). Interacts with ESRRB; represses
NFE2L2 transcriptional activity (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q60795}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Cytosolic under
unstressed conditions, translocates into the nucleus upon
induction by electrophilic agents. {ECO:0000250}.
-!- DOMAIN: Acidic activation domain in the N-terminus, and DNA
binding domain in the C-terminus.
-!- PTM: Phosphorylation of Ser-40 by PKC in response to oxidative
stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1,
promoting its translocation into the nucleus.
{ECO:0000250|UniProtKB:O54968}.
-!- PTM: Acetylation at Lys-598 and Lys-601 increases nuclear
localization whereas deacetylation by SIRT1 enhances cytoplasmic
presence. {ECO:0000250}.
-!- PTM: Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase
complex and subject to proteasomal degradation. Ubiquitination is
inhibited by sulforaphane (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. CNC subfamily.
{ECO:0000305}.
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EMBL; AB162435; BAD81030.1; -; mRNA.
EMBL; BC102275; AAI02276.1; ALT_TERM; mRNA.
UniGene; Bt.17324; -.
ProteinModelPortal; Q5NUA6; -.
SMR; Q5NUA6; -.
STRING; 9913.ENSBTAP00000025637; -.
PaxDb; Q5NUA6; -.
PRIDE; Q5NUA6; -.
eggNOG; ENOG410ISV3; Eukaryota.
eggNOG; ENOG41100FB; LUCA.
HOGENOM; HOG000234410; -.
HOVERGEN; HBG052609; -.
InParanoid; Q5NUA6; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA binding transcription factor activity; IBA:GO_Central.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0071498; P:cellular response to fluid shear stress; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR029845; Nrf2.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR24411:SF3; PTHR24411:SF3; 1.
Pfam; PF03131; bZIP_Maf; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
2: Evidence at transcript level;
Acetylation; Activator; Complete proteome; Cytoplasm; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 607 Nuclear factor erythroid 2-related factor
2.
/FTId=PRO_0000286396.
DOMAIN 499 562 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 501 520 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 524 531 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 593 598 Mediates interaction with CHD6 and is
necessary to activate transcription.
{ECO:0000250}.
MOD_RES 40 40 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:O54968}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:Q16236}.
MOD_RES 598 598 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:Q16236}.
MOD_RES 601 601 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:Q16236}.
CONFLICT 287 287 A -> T (in Ref. 1; BAD81030).
{ECO:0000305}.
CONFLICT 423 423 Q -> H (in Ref. 1; BAD81030).
{ECO:0000305}.
SEQUENCE 607 AA; 67895 MW; E0C576DBAF2A1A21 CRC64;
MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRQKEHELEK QKKLEKERQE
QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIPSETSGSA NYSQVAPIPK ADDLYFDDCM
QLLAETFPFV DDNEVSSATF QSLVPDIPSH IESPVFTAPP QAQSPETLIV QVATAVLDDM
QDIEQVWEEL LSIPELQCLN IQNDKLAETS TVPSPETKLT EIDNYHFYSS MPSLDKEVGN
CSPHFLNAFE DSFNSILSTE DSSQLTVNSL NSSATVNTDF GDEFYSAFIA EPSTSNGMPS
SATLSQSLSE LLNGPIDLSD LSLCKAFNQN HPESTTAEFN DSDSGISLNT TSPSMASPDH
SVESSIYGDT LLGFSDSEME EIDSTPGNVK QKGPKTPSVW PPGDPVQPLS SSQGNSAAAR
DSQCENAPKK EVPVSPGHRK TPFTKDKHSS RLEAHLTRDE LRAKALHIPF PVEKIINLPV
EDFNEMMSKE QFNEAQLALI RDIRRRGKNK VAAQNCRKRK LENIVELEQD LDHLKDEKEK
LLKERGENDK SLHLLKKQLS TLYLEVFSML RDENGKPYSP SEYSLQQTSD GNVFLVPKSK
KPDTKKN


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