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Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1]

 NF2L1_MOUSE             Reviewed;         741 AA.
Q61985; E9Q038; O70234;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
12-SEP-2018, entry version 156.
RecName: Full=Endoplasmic reticulum membrane sensor NFE2L1 {ECO:0000305};
AltName: Full=Locus control region-factor 1 {ECO:0000303|PubMed:9087432};
Short=LCR-F1 {ECO:0000303|PubMed:9087432};
AltName: Full=Nuclear factor erythroid 2-related factor 1 {ECO:0000305};
Short=NF-E2-related factor 1 {ECO:0000303|PubMed:9580677};
Short=NFE2-related factor 1 {ECO:0000303|PubMed:9580677};
AltName: Full=Nuclear factor, erythroid derived 2, like 1;
Contains:
RecName: Full=Transcription factor NRF1 {ECO:0000305};
Name=Nfe2l1 {ECO:0000303|PubMed:7759107, ECO:0000312|MGI:MGI:99421};
Synonyms=Nrf1 {ECO:0000303|PubMed:9580677};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=7759107; DOI=10.1016/0888-7543(95)80015-E;
McKie J., Johnstone K., Mattei M.-G., Scambler P.;
"Cloning and mapping of murine Nfe2l1.";
Genomics 25:716-719(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, AND
PHOSPHORYLATION BY CKII.
PubMed=9580677; DOI=10.1093/nar/26.10.2291;
Prieschl E.E., Novotny V., Csonga R., Jaksche D., Elbe-Buerger A.,
Thumb W., Auer M., Stingl G., Baumruker T.;
"A novel splice variant of the transcription factor Nrf1 interacts
with the TNFalpha promoter and stimulates transcription.";
Nucleic Acids Res. 26:2291-2297(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
DISRUPTION PHENOTYPE.
PubMed=9087432;
Farmer S.C., Sun C.W., Winnier G.E., Hogan B.L., Townes T.M.;
"The bZIP transcription factor LCR-F1 is essential for mesoderm
formation in mouse development.";
Genes Dev. 11:786-798(1997).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9501099; DOI=10.1093/emboj/17.6.1779;
Chan J.Y., Kwong M., Lu R., Chang J., Wang B., Yen T.S., Kan Y.W.;
"Targeted disruption of the ubiquitous CNC-bZIP transcription factor,
Nrf-1, results in anemia and embryonic lethality in mice.";
EMBO J. 17:1779-1787(1998).
[6]
FUNCTION, AND DNA-BINDING.
PubMed=10601325;
Kwong M., Kan Y.W., Chan J.Y.;
"The CNC basic leucine zipper factor, Nrf1, is essential for cell
survival in response to oxidative stress-inducing agents. Role for
Nrf1 in gamma-gcs(l) and gss expression in mouse fibroblasts.";
J. Biol. Chem. 274:37491-37498(1999).
[7]
FUNCTION, DNA-BINDING, AND INTERACTION WITH MAFG.
PubMed=11342101;
Myhrstad M.C., Husberg C., Murphy P., Nordstroem O., Blomhoff R.,
Moskaug J.O., Kolstoe A.B.;
"TCF11/Nrf1 overexpression increases the intracellular glutathione
level and can transactivate the gamma-glutamylcysteine synthetase
(GCS) heavy subunit promoter.";
Biochim. Biophys. Acta 1517:212-219(2001).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12968018; DOI=10.1074/jbc.M308439200;
Leung L., Kwong M., Hou S., Lee C., Chan J.Y.;
"Deficiency of the Nrf1 and Nrf2 transcription factors results in
early embryonic lethality and severe oxidative stress.";
J. Biol. Chem. 278:48021-48029(2003).
[9]
FUNCTION.
PubMed=12808106;
Chen L., Kwong M., Lu R., Ginzinger D., Lee C., Leung L., Chan J.Y.;
"Nrf1 is critical for redox balance and survival of liver cells during
development.";
Mol. Cell. Biol. 23:4673-4686(2003).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15738389; DOI=10.1073/pnas.0500660102;
Xu Z., Chen L., Leung L., Yen T.S., Lee C., Chan J.Y.;
"Liver-specific inactivation of the Nrf1 gene in adult mouse leads to
nonalcoholic steatohepatitis and hepatic neoplasia.";
Proc. Natl. Acad. Sci. U.S.A. 102:4120-4125(2005).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16872277; DOI=10.1042/BJ20060725;
Zhang Y., Crouch D.H., Yamamoto M., Hayes J.D.;
"Negative regulation of the Nrf1 transcription factor by its N-
terminal domain is independent of Keap1: Nrf1, but not Nrf2, is
targeted to the endoplasmic reticulum.";
Biochem. J. 399:373-385(2006).
[12]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=17705787; DOI=10.1042/BJ20070761;
Zhang Y., Lucocq J.M., Yamamoto M., Hayes J.D.;
"The NHB1 (N-terminal homology box 1) sequence in transcription factor
Nrf1 is required to anchor it to the endoplasmic reticulum and also to
enable its asparagine-glycosylation.";
Biochem. J. 408:161-172(2007).
[13]
FUNCTION.
PubMed=17510056; DOI=10.1074/jbc.M702614200;
Xing W., Singgih A., Kapoor A., Alarcon C.M., Baylink D.J., Mohan S.;
"Nuclear factor-E2-related factor-1 mediates ascorbic acid induction
of osterix expression via interaction with antioxidant-responsive
element in bone cells.";
J. Biol. Chem. 282:22052-22061(2007).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18826952; DOI=10.1074/jbc.M804597200;
Ohtsuji M., Katsuoka F., Kobayashi A., Aburatani H., Hayes J.D.,
Yamamoto M.;
"Nrf1 and Nrf2 play distinct roles in activation of antioxidant
response element-dependent genes.";
J. Biol. Chem. 283:33554-33562(2008).
[15]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND SUBUNIT.
PubMed=18990090; DOI=10.1042/BJ20081575;
Zhang Y., Lucocq J.M., Hayes J.D.;
"The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription
factor that is activated by t-butyl hydroquinone but not by
endoplasmic reticulum stressors.";
Biochem. J. 418:293-310(2009).
[16]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=20629635; DOI=10.1042/BJ20100471;
Zhang Y., Hayes J.D.;
"Identification of topological determinants in the N-terminal domain
of transcription factor Nrf1 that control its orientation in the
endoplasmic reticulum membrane.";
Biochem. J. 430:497-510(2010).
[17]
FUNCTION.
PubMed=20385086; DOI=10.1016/j.molcel.2010.02.029;
Radhakrishnan S.K., Lee C.S., Young P., Beskow A., Chan J.Y.,
Deshaies R.J.;
"Transcription factor Nrf1 mediates the proteasome recovery pathway
after proteasome inhibition in mammalian cells.";
Mol. Cell 38:17-28(2010).
[18]
DISRUPTION PHENOTYPE.
PubMed=21554501; DOI=10.1111/j.1365-2443.2011.01522.x;
Kobayashi A., Tsukide T., Miyasaka T., Morita T., Mizoroki T.,
Saito Y., Ihara Y., Takashima A., Noguchi N., Fukamizu A., Hirotsu Y.,
Ohtsuji M., Katsuoka F., Yamamoto M.;
"Central nervous system-specific deletion of transcription factor Nrf1
causes progressive motor neuronal dysfunction.";
Genes Cells 16:692-703(2011).
[19]
UBIQUITINATION, INTERACTION WITH FBXW7, AND MUTAGENESIS OF
350-SER--GLU-354.
PubMed=21953459; DOI=10.1074/jbc.M111.253807;
Biswas M., Phan D., Watanabe M., Chan J.Y.;
"The Fbw7 tumor suppressor regulates nuclear factor E2-related factor
1 transcription factor turnover through proteasome-mediated
proteolysis.";
J. Biol. Chem. 286:39282-39289(2011).
[20]
FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH BTRC
AND SYVN1, AND MUTAGENESIS OF 448-SER--SER-451.
PubMed=21911472; DOI=10.1128/MCB.05663-11;
Tsuchiya Y., Morita T., Kim M., Iemura S., Natsume T., Yamamoto M.,
Kobayashi A.;
"Dual regulation of the transcriptional activity of Nrf1 by beta-
TrCP- and Hrd1-dependent degradation mechanisms.";
Mol. Cell. Biol. 31:4500-4512(2011).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21536885; DOI=10.1073/pnas.1019209108;
Lee C.S., Lee C., Hu T., Nguyen J.M., Zhang J., Martin M.V.,
Vawter M.P., Huang E.J., Chan J.Y.;
"Loss of nuclear factor E2-related factor 1 in the brain leads to
dysregulation of proteasome gene expression and neurodegeneration.";
Proc. Natl. Acad. Sci. U.S.A. 108:8408-8413(2011).
[22]
FUNCTION.
PubMed=22586274; DOI=10.1128/MCB.06706-11;
Hirotsu Y., Hataya N., Katsuoka F., Yamamoto M.;
"NF-E2-related factor 1 (Nrf1) serves as a novel regulator of hepatic
lipid metabolism through regulation of the Lipin1 and PGC-1beta
genes.";
Mol. Cell. Biol. 32:2760-2770(2012).
[23]
ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2, FUNCTION,
INTERACTION WITH MAFG, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23144760; DOI=10.1371/journal.pone.0048404;
Kwong E.K., Kim K.M., Penalosa P.J., Chan J.Y.;
"Characterization of Nrf1b, a novel isoform of the nuclear factor-
erythroid-2 related transcription factor-1 that activates antioxidant
response element-regulated genes.";
PLoS ONE 7:E48404-E48404(2012).
[24]
FUNCTION, PHOSPHORYLATION AT SER-497, AND MUTAGENESIS OF SER-496;
SER-497; SER-499 AND THR-501.
PubMed=23816881; DOI=10.1128/MCB.01271-12;
Tsuchiya Y., Taniguchi H., Ito Y., Morita T., Karim M.R., Ohtake N.,
Fukagai K., Ito T., Okamuro S., Iemura S., Natsume T., Nishida E.,
Kobayashi A.;
"The casein kinase 2-nrf1 axis controls the clearance of ubiquitinated
proteins by regulating proteasome gene expression.";
Mol. Cell. Biol. 33:3461-3472(2013).
[25]
FUNCTION.
PubMed=25041126; DOI=10.1111/gtc.12165;
Hirotsu Y., Higashi C., Fukutomi T., Katsuoka F., Tsujita T.,
Yagishita Y., Matsuyama Y., Motohashi H., Uruno A., Yamamoto M.;
"Transcription factor NF-E2-related factor 1 impairs glucose
metabolism in mice.";
Genes Cells 19:650-665(2014).
[26]
SUBCELLULAR LOCATION.
PubMed=26268886; DOI=10.1038/srep12983;
Zhang Y., Li S., Xiang Y., Qiu L., Zhao H., Hayes J.D.;
"The selective post-translational processing of transcription factor
Nrf1 yields distinct isoforms that dictate its ability to
differentially regulate gene expression.";
Sci. Rep. 5:12983-12983(2015).
[27]
REVIEW.
PubMed=26947393; DOI=10.1016/j.gene.2016.03.002;
Kim H.M., Han J.W., Chan J.Y.;
"Nuclear factor erythroid-2 like 1 (NFE2L1): structure, function and
regulation.";
Gene 584:17-25(2016).
[28]
FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, DOMAIN,
CHOLESTEROL-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=29149604; DOI=10.1016/j.cell.2017.10.003;
Widenmaier S.B., Snyder N.A., Nguyen T.B., Arduini A., Lee G.Y.,
Arruda A.P., Saksi J., Bartelt A., Hotamisligil G.S.;
"NRF1 is an ER membrane sensor that is central to cholesterol
homeostasis.";
Cell 171:1094-1109(2017).
-!- FUNCTION: Endoplasmic reticulum membrane sensor NFE2L1:
Endoplasmic reticulum membrane sensor that translocates into the
nucleus in response to various stresses to act as a transcription
factor (PubMed:20385086, PubMed:21536885, PubMed:23816881,
PubMed:29149604). Constitutes a precursor of the transcription
factor NRF1. Able to detect various cellular stresses, such as
cholesterol excess, oxidative stress or proteasome inhibition
(PubMed:20385086, PubMed:21536885, PubMed:23816881,
PubMed:29149604). In response to stress, it is released from the
endoplasmic reticulum membrane following cleavage by the protease
DDI2 and translocates into the nucleus to form the transcription
factor NRF1 (PubMed:29149604). Acts as a key sensor of cholesterol
excess: in excess cholesterol conditions, the endoplasmic
reticulum membrane form of the protein directly binds cholesterol
via its CRAC motif, preventing cleavage and release of the
transcription factor NRF1, thereby allowing expression of genes
promoting cholesterol removal, such as CD36 (PubMed:29149604).
Involved in proteasome homeostasis: in response to proteasome
inhibition, it is released from the endoplasmic reticulum
membrane, translocates to the nucleus and activates expression of
genes encoding proteasome subunits (PubMed:20385086,
PubMed:21536885, PubMed:23816881). {ECO:0000269|PubMed:20385086,
ECO:0000269|PubMed:21536885, ECO:0000269|PubMed:23816881,
ECO:0000269|PubMed:29149604}.
-!- FUNCTION: Transcription factor NRF1: CNC-type bZIP family
transcription factor that translocates to the nucleus and
regulates expression of target genes in response to various
stresses (PubMed:10601325, PubMed:11342101, PubMed:23144760,
PubMed:16872277, PubMed:21911472, PubMed:23816881,
PubMed:29149604). Heterodimerizes with small-Maf proteins (MAFF,
MAFG or MAFK) and binds DNA motifs including the antioxidant
response elements (AREs), which regulate expression of genes
involved in oxidative stress response (PubMed:12808106,
PubMed:15738389, PubMed:23144760, PubMed:16872277,
PubMed:21911472, PubMed:23816881). Activates or represses
expression of target genes, depending on the context
(PubMed:12808106, PubMed:15738389, PubMed:23144760,
PubMed:16872277, PubMed:21911472, PubMed:23816881). Plays a key
role in cholesterol homeostasis by acting as a sensor of
cholesterol excess: in low cholesterol conditions, translocates
into the nucleus and represses expression of genes involved in
defense against cholesterol excess, such as CD36
(PubMed:29149604). In excess cholesterol conditions, the
endoplasmic reticulum membrane form of the protein directly binds
cholesterol via its CRAC motif, preventing cleavage and release of
the transcription factor NRF1, thereby allowing expression of
genes promoting cholesterol removal (PubMed:29149604). Critical
for redox balance in response to oxidative stress: acts by binding
the AREs motifs on promoters and mediating activation of oxidative
stress response genes, such as GCLC, GCLM, GSS, MT1 and MT2
(PubMed:10601325, PubMed:11342101, PubMed:12968018,
PubMed:15738389, PubMed:18826952). Plays an essential role during
fetal liver hematopoiesis: probably has a protective function
against oxidative stress and is involved in lipid homeostasis in
the liver (PubMed:9501099, PubMed:12808106, PubMed:15738389,
PubMed:18826952, PubMed:22586274). Involved in proteasome
homeostasis: in response to proteasome inhibition, mediates the
'bounce-back' of proteasome subunits by translocating into the
nucleus and activating expression of genes encoding proteasome
subunits (PubMed:20385086, PubMed:21536885, PubMed:23816881). Also
involved in regulating glucose flux (PubMed:25041126). Together
with CEBPB; represses expression of DSPP during odontoblast
differentiation (By similarity). In response to ascorbic acid
induction, activates expression of SP7/Osterix in osteoblasts
(PubMed:17510056). {ECO:0000250|UniProtKB:Q14494,
ECO:0000269|PubMed:10601325, ECO:0000269|PubMed:11342101,
ECO:0000269|PubMed:12808106, ECO:0000269|PubMed:12968018,
ECO:0000269|PubMed:15738389, ECO:0000269|PubMed:16872277,
ECO:0000269|PubMed:17510056, ECO:0000269|PubMed:18826952,
ECO:0000269|PubMed:20385086, ECO:0000269|PubMed:21536885,
ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:22586274,
ECO:0000269|PubMed:23144760, ECO:0000269|PubMed:23816881,
ECO:0000269|PubMed:25041126, ECO:0000269|PubMed:29149604,
ECO:0000269|PubMed:9501099}.
-!- FUNCTION: Isoform 2: Transcription factor that binds the
antioxidant response elements (ARE) consensus sequence on
promoters and activates their expression.
{ECO:0000269|PubMed:23144760, ECO:0000269|PubMed:9580677}.
-!- FUNCTION: Isoform 3: Transcription factor that binds the extended
kappa 3 site of the TNF-alpha promoter after Fc gamma RIII
stimulation and participates in the induction of this cytokine
(PubMed:9580677). {ECO:0000269|PubMed:9580677}.
-!- SUBUNIT: Interacts with KEAP1 (By similarity). Endoplasmic
reticulum membrane sensor NFE2L1: Interacts (via CPD region) with
FBXW7; leading to its ubiquitination and degradation
(PubMed:21953459). Endoplasmic reticulum membrane sensor NFE2L1:
Interacts with SYVN1/HRD1; leading to its ubiquitination and
degradation (PubMed:21911472). Endoplasmic reticulum membrane
sensor NFE2L1: Interacts (when ubiquitinated) with DDI2; leading
to its cleavage (By similarity). Transcription factor NRF1:
Interacts (via the bZIP domain) with small MAF protein (MAFF, MAFG
or MAFK); required for binding to antioxidant response elements
(AREs) on DNA (PubMed:11342101, PubMed:23144760). Transcription
factor NRF1: Interacts (via Destruction motif) with BTRC; leading
to its ubiquitination and degradation (PubMed:21911472).
Transcription factor NRF1: Interacts with CEBPB; the heterodimer
represses expression of DSPP during odontoblast differentiation
(By similarity). {ECO:0000250|UniProtKB:Q14494,
ECO:0000269|PubMed:11342101, ECO:0000269|PubMed:18990090,
ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:21953459,
ECO:0000269|PubMed:23144760}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane sensor
NFE2L1: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16872277, ECO:0000269|PubMed:17705787,
ECO:0000269|PubMed:18990090, ECO:0000269|PubMed:20629635,
ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:29149604}; Single-
pass type II membrane protein {ECO:0000250|UniProtKB:Q14494}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:16872277,
ECO:0000269|PubMed:17705787, ECO:0000269|PubMed:18990090,
ECO:0000269|PubMed:20629635, ECO:0000269|PubMed:21911472,
ECO:0000269|PubMed:29149604}; Single-pass type III membrane
protein {ECO:0000250|UniProtKB:Q14494}. Note=In normal conditions,
probably has a single-pass type II membrane protein topology, with
the DNA-binding domain facing the endoplasmic reticulum lumen (By
similarity). Following cellular stress, it is rapidly and
efficiently retrotranslocated to the cytosolic side of the
membrane, a process dependent on p97/VCP, to have a single-pass
type III membrane protein topology with the major part of the
protein facing the cytosol (By similarity). Retrotranslocated
proteins are normally rapidly degraded by the proteasome and
active species do not accumulate (By similarity). However,
retrotranslocated protein NFE2L1 escapes degradation and is
cleaved at Leu-104 by DDI2, releasing the protein from the
endoplasmic reticulum membrane and forming the transcription
factor NRF1 that translocates into the nucleus (By similarity).
{ECO:0000250|UniProtKB:Q14494}.
-!- SUBCELLULAR LOCATION: Transcription factor NRF1: Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00978,
ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:23144760,
ECO:0000269|PubMed:29149604}. Note=Translocates into the nucleus
following cleavage of Endoplasmic reticulum membrane sensor NFE2L1
by aspartyl protease DDI2. {ECO:0000305|PubMed:29149604}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:23144760}. Nucleus
{ECO:0000269|PubMed:23144760}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long {ECO:0000303|PubMed:9580677}, Nrf1a
{ECO:0000303|PubMed:23144760};
IsoId=Q61985-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=Nrf1b {ECO:0000303|PubMed:23144760};
IsoId=Q61985-3; Sequence=VSP_000580, VSP_046524;
Note=Produced by alternative promoter usage.;
Name=3; Synonyms=Short {ECO:0000303|PubMed:9580677};
IsoId=Q61985-2; Sequence=VSP_000580, VSP_046523, VSP_000581;
Note=Produced by alternative splicing of isoform 1.;
-!- TISSUE SPECIFICITY: Isoform 1: Widely expressed including kidney,
brown fat, white fat, large intestine, small intestine, stomach,
lung, brain and liver (PubMed:23144760). Isoform 1: Expressed in
mouse embryonic fibroblasts (MEF) (PubMed:23144760). Isoform 2:
Widely expressed including kidney, brown fat, white fat, large
intestine, small intestine, stomach, lung, brain and liver
(PubMed:23144760). Isoform 2: levels in white fat, lung and liver
are increased compared to isoform 1 (at protein level)
(PubMed:23144760). Isoform 2: levels are elevated in brown fat and
brain, but are reduced in liver compared to isoform 1 levels
(PubMed:23144760). Isoform 2: Expressed in mouse embryonic
fibroblasts (MEF) (PubMed:23144760).
{ECO:0000269|PubMed:23144760}.
-!- DOMAIN: The cholesterol recognition/amino acid consensus (CRAC)
region directly binds cholesterol, as well as campesterol and 27-
hydroxycholesterol (PubMed:29149604). Has much lower affinity for
epicholesterol (PubMed:29149604). {ECO:0000269|PubMed:29149604}.
-!- PTM: Endoplasmic reticulum membrane sensor NFE2L1: Cleaved at Leu-
104 by the aspartyl protease DDI2 following retrotranslocation,
releasing the protein from the endoplasmic reticulum membrane and
forming the transcription factor NRF1 that translocates into the
nucleus. Ubiquitination is prerequisite for cleavage by aspartyl
protease DDI2. {ECO:0000250|UniProtKB:Q14494}.
-!- PTM: Endoplasmic reticulum membrane sensor NFE2L1: N-glycosylated
in normal conditions, when it has a single-pass type II membrane
protein topology, with the DNA-binding domain facing the
endoplasmic reticulum lumen (PubMed:17705787, PubMed:18990090).
Deglycosylated during retrotranslocation to the cytosolic side of
the membrane, to have a single-pass type III membrane protein
topology with the major part of the protein facing the cytosol (By
similarity). {ECO:0000250|UniProtKB:Q14494,
ECO:0000269|PubMed:17705787, ECO:0000269|PubMed:18990090}.
-!- PTM: Endoplasmic reticulum membrane sensor NFE2L1: Ubiquitinated
by the SCF(FBXW7) complex and SYVN1/HRD1, leading to its
degradation by the proteasome (PubMed:21953459, PubMed:21911472).
Ubiquitinated during retrotranslocation to the cytosolic side of
the membrane: ubiquitination does not lead to degradation and is
required for processing by the aspartyl protease DDI2 and
subsequent release from the endoplasmic reticulum membrane (By
similarity). {ECO:0000250|UniProtKB:Q14494,
ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:21953459}.
-!- PTM: Transcription factor NRF1: Phosphorylation by CK2 at Ser-497
inhibits transcription factor activity, possibly by affecting DNA-
binding activity (PubMed:9580677, PubMed:23816881).
Phosphorylation at Ser-568 is required for interaction with CEBPB
(By similarity). {ECO:0000250|UniProtKB:Q14494,
ECO:0000269|PubMed:23816881, ECO:0000269|PubMed:9580677}.
-!- PTM: Transcription factor NRF1: Ubiquitinated by the SCF(BTRC)
complex in the nucleus, leading to its degradation by the
proteasome. {ECO:0000269|PubMed:21911472}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality: embryos progress
normally to the late egg cylinder stage at approximately 6.5 days
post coitus (dpc), but development is arrested before 7.5 dpc
(PubMed:9087432, PubMed:9501099). Mutant embryos fail to form a
primitive streak and lack detectable mesoderm (PubMed:9087432).
Homozygous embryos suffer from anemia as a result of abnormal
fetal liver erythropoiesis (PubMed:9501099). No defect in globin
gene expression are detected; abnormal red cell production being
the result of a defect in the fetal liver microenvironment
specific for erythroid cells (PubMed:9501099). Mice lacking both
Nfe2l1 and Nfe2l2 die early between embryonic days 9 and 10 and
exhibit extensive apoptosis due to marked oxidative stress in
cells that is indicated by elevated intracellular reactive oxygen
species levels and cell death (PubMed:12968018). Conditional
knockout mice lacking Nfe2l1 in the liver do not show any liver
damage when they are maintained in an unstressed condition
(PubMed:15738389). In oxidative stress condition, they develop
hepatic cancer following steatosis, apoptosis, necrosis,
inflammation, and fibrosis (PubMed:15738389). Hepatocyte-specific
deletion causes liver damage resembling the human disease non-
alcoholic steatohepatitis (PubMed:18826952). Liver of conditional
knockout mice lacking Nfe2l1 show massive hepatic cholesterol
accumulation and damage due to inability to mediate response to
cholesterol excess (PubMed:29149604). Conditional knockout mice
lacking Nfe2l1 in the brain show proteasome impairment and
progressive degeneration in cortical neurons (PubMed:21554501,
PubMed:21536885). {ECO:0000269|PubMed:12968018,
ECO:0000269|PubMed:15738389, ECO:0000269|PubMed:18826952,
ECO:0000269|PubMed:21536885, ECO:0000269|PubMed:21554501,
ECO:0000269|PubMed:29149604, ECO:0000269|PubMed:9087432,
ECO:0000269|PubMed:9501099}.
-!- SIMILARITY: Belongs to the bZIP family. CNC subfamily.
{ECO:0000305}.
-!- CAUTION: Endoplasmic reticulum membrane sensor NFE2L1: its
topology is subject to discussion. According to some groups, it
has a single-pass type II membrane protein in normal conditions
and is retrotranslocated into a single-pass type III membrane
protein in response to stress. According to other reports, it is
integrated into the endoplasmic reticulum membrane via multiple
membrane-spanning alpha-helices (PubMed:20629635,
PubMed:26268886). {ECO:0000269|PubMed:20629635,
ECO:0000269|PubMed:26268886}.
-!- CAUTION: Endoplasmic reticulum membrane sensor NFE2L1: Was
initially thought to be either inactive as transcription factor or
to repress transcriptional activation mediated by other isoforms
(PubMed:9580677). The presence of the transmembrane region at the
N-terminus may explain the inability to observe transcription
factor activity. {ECO:0000269|PubMed:9580677}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X78709; CAA55362.1; -; mRNA.
EMBL; AF015881; AAC40108.1; -; Genomic_DNA.
EMBL; AL596384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS25304.1; -. [Q61985-1]
CCDS; CCDS48894.1; -. [Q61985-3]
PIR; I48694; I48694.
RefSeq; NP_001123922.1; NM_001130450.1. [Q61985-1]
RefSeq; NP_032712.2; NM_008686.3. [Q61985-1]
UniGene; Mm.6743; -.
ProteinModelPortal; Q61985; -.
SMR; Q61985; -.
STRING; 10090.ENSMUSP00000080467; -.
iPTMnet; Q61985; -.
PhosphoSitePlus; Q61985; -.
PaxDb; Q61985; -.
PRIDE; Q61985; -.
Ensembl; ENSMUST00000081775; ENSMUSP00000080467; ENSMUSG00000038615. [Q61985-1]
Ensembl; ENSMUST00000107657; ENSMUSP00000103284; ENSMUSG00000038615. [Q61985-1]
Ensembl; ENSMUST00000107658; ENSMUSP00000103285; ENSMUSG00000038615. [Q61985-1]
Ensembl; ENSMUST00000167110; ENSMUSP00000127804; ENSMUSG00000038615. [Q61985-3]
Ensembl; ENSMUST00000167149; ENSMUSP00000128527; ENSMUSG00000038615. [Q61985-1]
GeneID; 18023; -.
KEGG; mmu:18023; -.
UCSC; uc007lcq.2; mouse. [Q61985-1]
UCSC; uc011ydl.1; mouse. [Q61985-3]
CTD; 4779; -.
MGI; MGI:99421; Nfe2l1.
eggNOG; KOG3863; Eukaryota.
eggNOG; ENOG410ZGMS; LUCA.
GeneTree; ENSGT00920000148991; -.
HOGENOM; HOG000185844; -.
HOVERGEN; HBG052609; -.
InParanoid; Q61985; -.
KO; K09040; -.
ChiTaRS; Nfe2l1; mouse.
PRO; PR:Q61985; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000038615; Expressed in 320 organ(s), highest expression level in soleus muscle.
CleanEx; MM_NFE2L1; -.
CleanEx; MM_NRF1; -.
ExpressionAtlas; Q61985; baseline and differential.
Genevisible; Q61985; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0030176; C:integral component of 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:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IDA:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
GO; GO:0071397; P:cellular response to cholesterol; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
GO; GO:1901329; P:regulation of odontoblast differentiation; ISS:UniProtKB.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR029847; Nrf1_NFE2L1.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR24411:SF31; PTHR24411:SF31; 2.
Pfam; PF03131; bZIP_Maf; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Alternative promoter usage; Alternative splicing;
Cholesterol metabolism; Complete proteome; Cytoplasm; DNA-binding;
Endoplasmic reticulum; Glycoprotein; Lipid metabolism; Lipid-binding;
Membrane; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Signal-anchor; Steroid metabolism; Sterol metabolism; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 741 Endoplasmic reticulum membrane sensor
NFE2L1.
/FTId=PRO_0000076448.
CHAIN 104 741 Transcription factor NRF1.
{ECO:0000250|UniProtKB:Q14494}.
/FTId=PRO_0000443104.
TRANSMEM 7 24 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
DOMAIN 623 686 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 191 199 Cholesterol recognition/amino acid
consensus (CRAC) region.
{ECO:0000269|PubMed:29149604}.
REGION 350 354 CPD. {ECO:0000269|PubMed:21953459}.
REGION 625 644 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 651 665 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 447 451 Destruction motif.
{ECO:0000269|PubMed:21911472}.
MOTIF 730 737 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 125 259 Asp/Glu-rich (acidic).
COMPBIAS 414 447 Asp/Glu-rich (acidic).
COMPBIAS 467 486 Poly-Ser.
SITE 103 104 Cleavage; by DDI2.
{ECO:0000250|UniProtKB:Q14494}.
MOD_RES 497 497 Phosphoserine; by CK2.
{ECO:0000269|PubMed:23816881}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000250|UniProtKB:Q14494}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 158 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_000580.
VAR_SEQ 159 291 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046523.
VAR_SEQ 159 170 VAPPVSGDLTKE -> MGWESRLTAASA (in isoform
2). {ECO:0000305}.
/FTId=VSP_046524.
VAR_SEQ 447 583 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_000581.
MUTAGEN 350 354 Missing: Abolishes interaction with
FBXW7. {ECO:0000269|PubMed:21953459}.
MUTAGEN 448 451 SGLS->AGLA: Abolishes ubiquitination and
degradation by the SCF(BTRC) complex.
{ECO:0000269|PubMed:21911472}.
MUTAGEN 496 496 S->A: Does not affect phosphorylation by
CK2. {ECO:0000269|PubMed:23816881}.
MUTAGEN 497 497 S->A: Abolishes phosphorylation by CK2.
{ECO:0000269|PubMed:23816881}.
MUTAGEN 499 499 S->A: Does not affect phosphorylation by
CK2. {ECO:0000269|PubMed:23816881}.
MUTAGEN 501 501 T->A: Does not affect phosphorylation by
CK2. {ECO:0000269|PubMed:23816881}.
CONFLICT 318 318 T -> S (in Ref. 1; CAA55362).
{ECO:0000305}.
CONFLICT 387 387 L -> P (in Ref. 1; CAA55362).
{ECO:0000305}.
SEQUENCE 741 AA; 81575 MW; DDB267F32CD2A92C CRC64;
MLSLKKYLTE GLLQFTILLS LIGVRVDVDT YLTSQLPPLR EIILGPSSAY TQTQFHNLRN
TLDGYGIHPK SIDLDNYFTA RRLLSQVRAL DRFQVPTTEV NAWLVHRDPE GSVSGSQPNS
GLALESSSGL QDVTGPDNGV RESETEQGFG EDLEDLGAVA PPVSGDLTKE DIDLIDILWR
QDIDLGAGRE VFDYSHRQKE QDVDKELQDG REREDTWSGE GAEALARDLL VDGETGESFP
AQFPADVSSI PEAVPSESES PALQNSLLSP LLTGTESPFD LEQQWQDLMS IMEMQAMEVN
TSASEILYNA PPGDPLSTNY SLAPNTPINQ NVSLHQASLG GCSQDFSLFS PEVESLPVAS
SSTLLPLVPS NSTSLNSTFG STNLAGLFFP SQLNGTANDT SGPELPDPLG GLLDEAMLDE
ISLMDLAIEE GFNPVQASQL EEEFDSDSGL SLDSSHSPSS LSSSEGSSSS SSSSSSSSAS
SSASSSFSEE GAVGYSSDSE TLDLEEAEGA VGYQPEYSKF CRMSYQDPSQ LSCLPYLEHV
GHNHTYNMAP SALDSADLPP PSTLKKGSKE KQADFLDKQM SRDEHRARAM KIPFTNDKII
NLPVEEFNEL LSKYQLSEAQ LSLIRDIRRR GKNKMAAQNC RKRKLDTILN LERDVEDLQR
DKARLLREKV EFLRSLRQMK QKVQSLYQEV FGRLRDEHGR PYSPSQYALQ YAGDGSVLLI
PRTMADQQAR RQERKPKDRR K


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