ID A0A3P9D8T8_9CICH Unreviewed; 793 AA.
AC A0A3P9D8T8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005030983.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005030983.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005030983.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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 RefSeq; XP_004568688.1; XM_004568631.1.
DR AlphaFoldDB; A0A3P9D8T8; -.
DR STRING; 106582.ENSMZEP00005030983; -.
DR Ensembl; ENSMZET00005031981.1; ENSMZEP00005030983.1; ENSMZEG00005023096.1.
DR GeneID; 101485140; -.
DR KEGG; mze:101485140; -.
DR GeneTree; ENSGT00950000182892; -.
DR OrthoDB; 4552116at2759; -.
DR Proteomes; UP000265160; LG4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
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:UP000265160};
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 688..751
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 727..754
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 89441 MW; 183C8DB7D64613F9 CRC64;
MLHLKKYFTE GLIQMAILLS LCGVRVDVEL EPYLPSSLHD MILGPTSALT QTQFHNLRNH
LEEGLHPKNV ELDGFSTAQR LLGWVRSLDR LHVPHAELET WLVQREPEPL PIRSPDQASL
LERTPAEIER ELTALPAEPQ AELEDEEEKE DTETSLQECF RLLEETFPST EEQWLNDVVG
GMGDLERQPS DRDSLLFPTD NPSMDFELHW QDLLNIMEPE NTDMDMASSD HNLSSGPSGT
FRGNVSGTMS NCCDNPVTEA DQETHLQHGL LEPQSESEPV LLPLTPTAEL DDHNSALNTR
DTMNNINGHP LNSPPDQTDL LAEEPIEDFS MELMEEDNII SFLSQVDVGR MEPEHRPGID
VNFQSSNSTL PLDGNVMTQD LVGSPSSHLL GYEDNEDDLP VPLSDLLEDA AILDEIRLLD
QALEEGFSPE MAARLEDESC FNHELAEQEI GSDDDHLGSK IAVIENHGRP STHHHGNSTD
CEGELDSDSG LSLDFSHSLA SPCTSEASSC SSSSTSSSFY VSATGSSFSK DDDEDSEEDL
AGSDVEAVMM IKQEELEEED MGAVGGENHE NKLVPVDYSD HSLFHGFSWL EHIGHDHTYN
MPSSSACSIP LGKMHTKHAK STRQHDSVKP YPQSFSRSIS ENKIWSQDER RARTLKIPFS
NELIVNLPVE EFNSLLSNYQ LSEEQLTLIK DIRRRGKNKI AAQNCRKRKQ DVLLGLEDDV
SSLRRHRSRL LREKRETLRN LQEIRRHMER LYKEVFSRLT REEGSPMDAT EYMLHFKPNG
RNSKKQSQRD KKK
//
