NFE2_BOVIN
ID NFE2_BOVIN Reviewed; 374 AA.
AC Q5EAD3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transcription factor NF-E2 45 kDa subunit;
DE AltName: Full=Leucine zipper protein NF-E2;
DE AltName: Full=Nuclear factor, erythroid-derived 2 45 kDa subunit;
DE AltName: Full=p45 NF-E2;
GN Name=NFE2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Component of the NF-E2 complex essential for regulating
CC erythroid and megakaryocytic maturation and differentiation. Binds to
CC the hypersensitive site 2 (HS2) of the beta-globin control region
CC (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-
CC like core palindrome present in a number of erythroid and
CC megakaryocytic gene promoters. Requires MAFK or other small MAF
CC proteins for binding to the NF-E2 motif. May play a role in all aspects
CC of hemoglobin production from globin and heme synthesis to procurement
CC of iron (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; can bind DNA as a homodimer (By similarity).
CC Erythroid transcription activator nuclear factor erythroid-derived 2
CC (NF-E2), composed of a heterodimer of NFE2 and MAFK, possesses
CC transactivation activity on beta-globin. Also forms high affinity
CC heterodimer with MAFG; the interaction promotes erythropoiesis.
CC Interacts (via the PXY motif 1) with ITCH (via the WW 1 domain); the
CC interaction promotes 'Lys63'-linked ubiquitination of NFE2,
CC translocates it to the cytoplasm and inhibits its transactivation
CC activity. Interacts with KMT2D/MLL2; the interaction promotes
CC transactivation of the beta-globin locus. Interacts with MAPK8
CC (phosphorylated form); the interaction leads to phosphorylation of NFE2
CC in undifferentiated cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Cytoplasm {ECO:0000250}. Note=The sumoylated form locates to the
CC nuclear bodies PML oncogenic domains (PODs). Translocated to the
CC cytoplasm through interaction with ITCH. {ECO:0000250}.
CC -!- DOMAIN: The PXY motifs are required for binding WW domains. PXY1 is
CC required to promote transactivation of beta-globin and for
CC hyperacetylation of histone H3, but not for binding to the HS2 promoter
CC site. {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues. In undifferentiated
CC erythrocytes, phosphorylated by MAPK8 which then leads to
CC ubiquitination and protein degradation. {ECO:0000250}.
CC -!- PTM: Sumoylated. Sumoylation is required for translocation to nuclear
CC bodies PODs, anchoring to the gene loci, and transactivation of the
CC beta-globin gene. {ECO:0000250}.
CC -!- PTM: Ubiquitinated mainly by 'Lys63'-linked ubiquitin.
CC Polyubiquitination with 'Lys63'-linked ubiquitin by ITCH retains NFE2
CC in the cytoplasm preventing its transactivation activity. In
CC undifferentiated erythrocyte, is ubiquitinated after MAPK8-mediatd
CC phosphorylation leading to protein degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR EMBL; BT020636; AAX08653.1; -; mRNA.
DR EMBL; BT021174; AAX31356.1; -; mRNA.
DR RefSeq; NP_001014923.1; NM_001014923.1.
DR RefSeq; XP_005206207.1; XM_005206150.3.
DR RefSeq; XP_005206208.1; XM_005206151.3.
DR RefSeq; XP_005206211.1; XM_005206154.3.
DR RefSeq; XP_015326431.1; XM_015470945.1.
DR AlphaFoldDB; Q5EAD3; -.
DR BMRB; Q5EAD3; -.
DR SMR; Q5EAD3; -.
DR STRING; 9913.ENSBTAP00000002043; -.
DR PaxDb; Q5EAD3; -.
DR Ensembl; ENSBTAT00000002043; ENSBTAP00000002043; ENSBTAG00000001562.
DR Ensembl; ENSBTAT00000047424; ENSBTAP00000044631; ENSBTAG00000001562.
DR Ensembl; ENSBTAT00000066479; ENSBTAP00000059395; ENSBTAG00000001562.
DR GeneID; 514006; -.
DR KEGG; bta:514006; -.
DR CTD; 4778; -.
DR VEuPathDB; HostDB:ENSBTAG00000001562; -.
DR VGNC; VGNC:32034; NFE2.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00950000182892; -.
DR HOGENOM; CLU_058451_0_0_1; -.
DR InParanoid; Q5EAD3; -.
DR OMA; ELYCDIF; -.
DR OrthoDB; 1095280at2759; -.
DR TreeFam; TF326681; -.
DR Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000001562; Expressed in neutrophil and 73 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029853; NF-E2_p45.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR24411:SF26; PTHR24411:SF26; 1.
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 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..374
FT /note="Transcription factor NF-E2 45 kDa subunit"
FT /id="PRO_0000244495"
FT DOMAIN 267..330
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..207
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT REGION 1..83
FT /note="Required for interaction with MAPK8"
FT /evidence="ECO:0000250"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..288
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 292..299
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 61..65
FT /note="PXY motif 1"
FT MOTIF 79..83
FT /note="PXY motif 2"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:Q07279"
FT MOD_RES 171
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q07279"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16621"
SQ SEQUENCE 374 AA; 41390 MW; 05A3AAA79437B5A6 CRC64;
MSPCPPQQSR NRVTQLPIPE PGEMELTWQE IMSITELQGL NAPSEPSFEP PAPVPYPGPP
PPPSYCPCSI HSEPGFPLPA PPYELPAPTS HVPDPPYSYG SNMTVPVSKP LTLSGLLSDP
LPDPLALLDI GLSAGPSKPQ EDPESDSGLS LNYSDAESLE LEGTEAGRRR SEYVEMYPVE
YPYSLMPNSL THPNYALPPA ETPLALEPSS GPVRAKPTAR GEAGSRDERR ALAMKIPFPT
DKIVNLPVDD FNELLARYPL TESQLALVRD IRRRGKNKVA AQNCRKRKLE TIVQLERELE
RLGSERERLL RARGEADRTL EVMRQQLTDL YRDIFQHLRD EAGNSYSPED YALHQAADGA
IFLVPRGTKM EATD
