ID D4A349_RAT Unreviewed; 728 AA.
AC D4A349;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Endoplasmic reticulum membrane sensor NFE2L1 {ECO:0000256|ARBA:ARBA00020485};
DE AltName: Full=Nuclear factor erythroid 2-related factor 1 {ECO:0000256|ARBA:ARBA00031659};
DE AltName: Full=Nuclear factor, erythroid derived 2, like 1 {ECO:0000256|ARBA:ARBA00030985};
GN Name=Nfe2l1 {ECO:0000313|Ensembl:ENSRNOP00000061935.3,
GN ECO:0000313|RGD:1311972};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000061935.3, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000061935.3, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061935.3,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000061935.3}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061935.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004643}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Membrane
CC {ECO:0000256|ARBA:ARBA00004183}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004183}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily.
CC {ECO:0000256|ARBA:ARBA00008157}.
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DR AlphaFoldDB; D4A349; -.
DR STRING; 10116.ENSRNOP00000061935; -.
DR PhosphoSitePlus; D4A349; -.
DR PaxDb; 10116-ENSRNOP00000061935; -.
DR Ensembl; ENSRNOT00000067542.4; ENSRNOP00000061935.3; ENSRNOG00000008830.8.
DR AGR; RGD:1311972; -.
DR RGD; 1311972; Nfe2l1.
DR VEuPathDB; HostDB:ENSRNOG00000008830; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00950000182892; -.
DR HOGENOM; CLU_024173_1_0_1; -.
DR InParanoid; D4A349; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000008830; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:RGD.
DR GO; GO:0019725; P:cellular homeostasis; ISO:RGD.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:RGD.
DR GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042883; P:cysteine transport; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:RGD.
DR GO; GO:0021781; P:glial cell fate commitment; ISO:RGD.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:1903353; P:regulation of nucleus organization; ISO:RGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; ISO:RGD.
DR CDD; cd14720; bZIP_NFE2-like; 1.
DR Gene3D; 1.10.880.10; Transcription factor, Skn-1-like, DNA-binding domain; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR047167; NFE2-like.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR24411:SF31; ENDOPLASMIC RETICULUM MEMBRANE SENSOR NFE2L1; 1.
DR PANTHER; PTHR24411; NUCLEAR FACTOR ERYTHROID 2-RELATED FACTOR; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 610..673
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 108..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..669
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 79914 MW; 7A5A2D6EAEDC599F CRC64;
MLSLKKYLTE GLLQFTILLS LIGVRVDVDT YLTSQLPPLR EIILGPSSAY TQTQFHNLRN
TLDGYGIHPK SIDLDNYFTA RRLLSQVRAL DRFQVPTTEV NAWLVHRDPE GSVSGSQPNS
GLALESSSGL QDVTVPDNGV RESEPEQGFS EDLEDLGAVA PPVSGDLTKE DIDLGAGREV
FDYSHRQKEQ DVDKELQDGG EREDTWSGEG AEALARDLLV DGETGESFPA QFPADVSSIT
EAVPSESESP ALQNSLLSPL LTGTESPFDL EQQWQDLMSI MEMQAMEVNT SASEILYSAP
PGDPLTTNYS LAPNTPINQN VSLHQASLGG CSQDFSLFSP EVESLPVASS STLLPLVPSN
STSLNSTFGS TNLAGLFFPS QLNGTANDTS GPELPDPLGG LLDEAMLDEI SLMDLAIEEG
FNPGQASQLE EEFDSDSGLS LDSSHSPSSL SSSEGSSSSS SSSSSASSSA SSSFSEEGAV
GYSSDSETLD LEEAEGAVGY QPEYSKFCRM SYQDPSQLSC LPYLEHVGHN HTYNMAPSAL
DSADLPPPST LKKGSKEKQA DFLDKQMSRD EHRARAMKIP FTNDKIINLP VEEFNELLSK
YQLSEAQLSL IRDIRRRGKN KMAAQNCRKR KLDTILNLER DVEDLQRDKA RLLREKVEFL
RSLRQMKQKV QSLYQEVFGR LRDENGRPYS PSQYALQYAG DGSVLLIPRT MADQQARRQE
RKPKDRRK
//
