NF2L3_HUMAN
ID NF2L3_HUMAN Reviewed; 694 AA.
AC Q9Y4A8; Q6NUS0; Q7Z498; Q86UJ4; Q86VR5; Q9UQA4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Nuclear factor erythroid 2-related factor 3;
DE Short=NF-E2-related factor 3;
DE Short=NFE2-related factor 3;
DE AltName: Full=Nuclear factor, erythroid derived 2, like 3;
GN Name=NFE2L3; Synonyms=NRF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH MAFG.
RA Blank V., Andrews N.C.;
RT "NRF3, a basic leucine zipper protein interacting with MAFG.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Stoesz S.P., Liu S., Pickett C.B.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-694, CHARACTERIZATION, INTERACTION WITH
RP MAFK, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10037736; DOI=10.1074/jbc.274.10.6443;
RA Kobayashi A., Ito E., Toki T., Kogame K., Takahashi S., Igarashi K.,
RA Hayashi N., Yamamoto M.;
RT "Molecular cloning and functional characterization of a new Cap'n' collar
RT family transcription factor Nrf3.";
RL J. Biol. Chem. 274:6443-6452(1999).
CC -!- FUNCTION: Activates erythroid-specific, globin gene expression.
CC -!- SUBUNIT: Heterodimer with MAFG, MAFK and other small MAF proteins that
CC binds to the MAF recognition elements (MARE).
CC {ECO:0000269|PubMed:10037736, ECO:0000269|Ref.1}.
CC -!- INTERACTION:
CC Q9Y4A8; Q9ULX9: MAFF; NbExp=3; IntAct=EBI-10890629, EBI-721128;
CC Q9Y4A8; O15525: MAFG; NbExp=5; IntAct=EBI-10890629, EBI-713514;
CC Q9Y4A8; Q16621: NFE2; NbExp=4; IntAct=EBI-10890629, EBI-726369;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Highly expressed in human placenta and also in B-
CC cell and monocyte cell lines. Low expression in heart, brain, lung,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10037736}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP22344.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA76288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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 EMBL; AF133059; AAG43275.1; -; mRNA.
DR EMBL; AF134891; AAF61404.1; -; mRNA.
DR EMBL; AF135116; AAF61415.1; -; Genomic_DNA.
DR EMBL; AC004520; AAP22344.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC049219; AAH49219.1; -; mRNA.
DR EMBL; BC056142; AAH56142.1; -; mRNA.
DR EMBL; BC068455; AAH68455.1; -; mRNA.
DR EMBL; AB010812; BAA76288.1; ALT_INIT; mRNA.
DR CCDS; CCDS5396.1; -.
DR RefSeq; NP_004280.5; NM_004289.6.
DR AlphaFoldDB; Q9Y4A8; -.
DR SMR; Q9Y4A8; -.
DR BioGRID; 114967; 16.
DR ComplexPortal; CPX-2471; bZIP transcription factor complex, BACH2-NFE2L3.
DR ComplexPortal; CPX-6572; bZIP transcription factor complex, ATF4-NFE2L3.
DR IntAct; Q9Y4A8; 13.
DR STRING; 9606.ENSP00000056233; -.
DR iPTMnet; Q9Y4A8; -.
DR PhosphoSitePlus; Q9Y4A8; -.
DR BioMuta; NFE2L3; -.
DR DMDM; 56404677; -.
DR EPD; Q9Y4A8; -.
DR MassIVE; Q9Y4A8; -.
DR PaxDb; Q9Y4A8; -.
DR PeptideAtlas; Q9Y4A8; -.
DR PRIDE; Q9Y4A8; -.
DR ProteomicsDB; 86144; -.
DR Antibodypedia; 12307; 184 antibodies from 27 providers.
DR DNASU; 9603; -.
DR Ensembl; ENST00000056233.4; ENSP00000056233.3; ENSG00000050344.9.
DR GeneID; 9603; -.
DR KEGG; hsa:9603; -.
DR MANE-Select; ENST00000056233.4; ENSP00000056233.3; NM_004289.7; NP_004280.5.
DR UCSC; uc003sxq.4; human.
DR CTD; 9603; -.
DR DisGeNET; 9603; -.
DR GeneCards; NFE2L3; -.
DR HGNC; HGNC:7783; NFE2L3.
DR HPA; ENSG00000050344; Tissue enhanced (brain, placenta).
DR MIM; 604135; gene.
DR neXtProt; NX_Q9Y4A8; -.
DR OpenTargets; ENSG00000050344; -.
DR PharmGKB; PA31589; -.
DR VEuPathDB; HostDB:ENSG00000050344; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00950000182892; -.
DR HOGENOM; CLU_024173_1_0_1; -.
DR InParanoid; Q9Y4A8; -.
DR OMA; LKRWWSA; -.
DR OrthoDB; 1095280at2759; -.
DR PhylomeDB; Q9Y4A8; -.
DR TreeFam; TF337360; -.
DR PathwayCommons; Q9Y4A8; -.
DR SignaLink; Q9Y4A8; -.
DR BioGRID-ORCS; 9603; 88 hits in 1100 CRISPR screens.
DR ChiTaRS; NFE2L3; human.
DR GeneWiki; NFE2L3; -.
DR GenomeRNAi; 9603; -.
DR Pharos; Q9Y4A8; Tbio.
DR PRO; PR:Q9Y4A8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y4A8; protein.
DR Bgee; ENSG00000050344; Expressed in placenta and 131 other tissues.
DR ExpressionAtlas; Q9Y4A8; baseline and differential.
DR Genevisible; Q9Y4A8; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..694
FT /note="Nuclear factor erythroid 2-related factor 3"
FT /id="PRO_0000076452"
FT DOMAIN 578..641
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 133..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..599
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 606..620
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 192..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 441
FT /note="V -> E (in dbSNP:rs2072129)"
FT /id="VAR_055562"
FT CONFLICT 286
FT /note="P -> L (in Ref. 4; AAH68455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 694 AA; 76154 MW; DAD6D883FCCBA982 CRC64;
MKHLKRWWSA GGGLLHLTLL LSLAGLRVDL DLYLLLPPPT LLQDELLFLG GPASSAYALS
PFSASGGWGR AGHLHPKGRE LDPAAPPEGQ LLREVRALGV PFVPRTSVDA WLVHSVAAGS
ADEAHGLLGA AAASSTGGAG ASVDGGSQAV QGGGGDPRAA RSGPLDAGEE EKAPAEPTAQ
VPDAGGCASE ENGVLREKHE AVDHSSQHEE NEERVSAQKE NSLQQNDDDE NKIAEKPDWE
AEKTTESRNE RHLNGTDTSF SLEDLFQLLS SQPENSLEGI SLGDIPLPGS ISDGMNSSAH
YHVNFSQAIS QDVNLHEAIL LCPNNTFRRD PTARTSQSQE PFLQLNSHTT NPEQTLPGTN
LTGFLSPVDN HMRNLTSQDL LYDLDINIFD EINLMSLATE DNFDPIDVSQ LFDEPDSDSG
LSLDSSHNNT SVIKSNSSHS VCDEGAIGYC TDHESSSHHD LEGAVGGYYP EPSKLCHLDQ
SDSDFHGDLT FQHVFHNHTY HLQPTAPEST SEPFPWPGKS QKIRSRYLED TDRNLSRDEQ
RAKALHIPFS VDEIVGMPVD SFNSMLSRYY LTDLQVSLIR DIRRRGKNKV AAQNCRKRKL
DIILNLEDDV CNLQAKKETL KREQAQCNKA INIMKQKLHD LYHDIFSRLR DDQGRPVNPN
HYALQCTHDG SILIVPKELV ASGHKKETQK GKRK