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NFE2_RAT
ID   NFE2_RAT                Reviewed;         373 AA.
AC   Q6AYT2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
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   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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=The sumoylated form locates to the nuclear bodies
CC       PML oncogenic domains (PODs). Translocated to the cytoplasm through
CC       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, 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; BC078925; AAH78925.1; -; mRNA.
DR   RefSeq; NP_001012224.1; NM_001012224.1.
DR   RefSeq; XP_006242494.1; XM_006242432.3.
DR   RefSeq; XP_006242495.1; XM_006242433.3.
DR   RefSeq; XP_017450513.1; XM_017595024.1.
DR   AlphaFoldDB; Q6AYT2; -.
DR   SMR; Q6AYT2; -.
DR   STRING; 10116.ENSRNOP00000052156; -.
DR   PaxDb; Q6AYT2; -.
DR   Ensembl; ENSRNOT00000055281; ENSRNOP00000052156; ENSRNOG00000036837.
DR   GeneID; 366998; -.
DR   KEGG; rno:366998; -.
DR   UCSC; RGD:1306888; rat.
DR   CTD; 4778; -.
DR   RGD; 1306888; Nfe2.
DR   eggNOG; KOG3863; Eukaryota.
DR   GeneTree; ENSGT00950000182892; -.
DR   HOGENOM; CLU_058451_0_0_1; -.
DR   InParanoid; Q6AYT2; -.
DR   OMA; ELYCDIF; -.
DR   OrthoDB; 1095280at2759; -.
DR   PhylomeDB; Q6AYT2; -.
DR   Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q6AYT2; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000036837; Expressed in spleen and 14 other tissues.
DR   Genevisible; Q6AYT2; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0050699; F:WW domain binding; ISO:RGD.
DR   GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0034242; P:negative regulation of syncytium formation by plasma membrane fusion; ISO:RGD.
DR   GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
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..373
FT                   /note="Transcription factor NF-E2 45 kDa subunit"
FT                   /id="PRO_0000320079"
FT   DOMAIN          266..329
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..206
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..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..287
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          291..298
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   MOD_RES         157
FT                   /note="Phosphoserine; by MAPK8"
FT                   /evidence="ECO:0000250|UniProtKB:Q07279"
FT   MOD_RES         170
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q07279"
FT   CROSSLNK        368
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        368
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16621"
SQ   SEQUENCE   373 AA;  41496 MW;  D9140F9F23CAC23C CRC64;
     MPPCPPQPNR NRLPQLPTGE LGEMELTWQE IMSITELQGL NVPSEPSFEP QAPTPYPGPL
     PPPTYCPCSI HPDAGFTLPP PPYELPASTP HAPDLPYSYG NIAIPVSKPL TLSGLLNEPL
     PDPLALLDIG LPVGQPKPQE DPESDSGLSL NYSDAESLEL EGTEAGRRRS EYVDMYPVEY
     PYSLMPNSLA HPNYTLPPTE TPLVLESSSG PVRAKPAVRG EAGSRDERRA LAMKIPFPTD
     KIVNLPVDDF NELLAQYPLT ESQLALVRDI RRRGKNKVAA QNCRKRKLET IVQLERELER
     LGSERERLLR ARGEADRTLE VMRQQLTELY HDIFQHLRDE SGNSYSPEEY VLQQAADGAI
     FLVPRGTKME ATD
 
 
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