NFKB2_XENLA
ID NFKB2_XENLA Reviewed; 958 AA.
AC O73630;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear factor NF-kappa-B p100 subunit;
DE AltName: Full=DNA-binding factor KBF2;
DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2;
DE Contains:
DE RecName: Full=Nuclear factor NF-kappa-B p52 subunit;
GN Name=nfkb2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=9461408; DOI=10.1016/s0378-1119(97)00561-1;
RA Suzuki K., Tsuchida J., Yamamoto T., Inoue J.;
RT "Identification and expression of the Xenopus homolog of mammalian p100-
RT NFkappaB2.";
RL Gene 206:1-9(1998).
CC -!- FUNCTION: Appears to have dual functions such as cytoplasmic retention
CC of attached NF-kappa-B proteins and generation of p52 by a
CC cotranslational processing. The proteasome-mediated process ensures the
CC production of both p52 and p100 and preserves their independent
CC function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3',
CC located in the enhancer region of genes involved in immune response and
CC acute phase reactions. In concert with RELB, may play a role in the
CC regulation of the circadian clock (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Active NF-kappa-B is a heterodimer of an about 52 kDa DNA-
CC binding subunit and the weak DNA-binding subunit p65. Two heterodimers
CC might form a labile tetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Nuclear, but also found in the cytoplasm in an inactive form
CC complexed to an inhibitor (I-kappa-B). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen. {ECO:0000269|PubMed:9461408}.
CC -!- DOMAIN: The C-terminus of p100 might be involved in cytoplasmic
CC retention, inhibition of DNA-binding by p52 homodimers, and/or
CC transcription activation. {ECO:0000250}.
CC -!- DOMAIN: The glycine-rich region (GRR) appears to be a critical element
CC in the generation of p52. {ECO:0000250}.
CC -!- PTM: While translation occurs, the particular unfolded structure after
CC the GRR repeat promotes the generation of p52 making it an acceptable
CC substrate for the proteasome. This process is known as cotranslational
CC processing. The processed form is active and the unprocessed form acts
CC as an inhibitor (I kappa B-like), being able to form cytosolic
CC complexes with NF-kappa B, trapping it in the cytoplasm. Complete
CC folding of the region downstream of the GRR repeat precludes processing
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Constitutive processing is tightly suppressed by its C-terminal
CC processing inhibitory domain, named PID, which contains the death
CC domain.
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DR EMBL; AB002629; BAA25919.1; -; mRNA.
DR RefSeq; NP_001081181.1; NM_001087712.1.
DR AlphaFoldDB; O73630; -.
DR SMR; O73630; -.
DR BioGRID; 99038; 1.
DR IntAct; O73630; 1.
DR GeneID; 397698; -.
DR KEGG; xla:397698; -.
DR CTD; 397698; -.
DR Xenbase; XB-GENE-970090; nfkb2.S.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 397698; Expressed in spleen and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR033926; IPT_NFkappaB.
DR InterPro; IPR000451; NFkB/Dor.
DR InterPro; IPR030497; NFkB_p100.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030492; RHD_CS.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR24169; PTHR24169; 1.
DR PANTHER; PTHR24169:SF21; PTHR24169:SF21; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS01204; REL_1; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 2: Evidence at transcript level;
KW Activator; ANK repeat; Biological rhythms; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..958
FT /note="Nuclear factor NF-kappa-B p100 subunit"
FT /id="PRO_0000030327"
FT CHAIN 1..467
FT /note="Nuclear factor NF-kappa-B p52 subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030328"
FT DOMAIN 40..230
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REPEAT 500..529
FT /note="ANK 1"
FT REPEAT 539..568
FT /note="ANK 2"
FT REPEAT 572..603
FT /note="ANK 3"
FT REPEAT 610..639
FT /note="ANK 4"
FT REPEAT 644..674
FT /note="ANK 5"
FT REPEAT 678..707
FT /note="ANK 6"
FT DOMAIN 815..901
FT /note="Death"
FT REGION 350..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..390
FT /note="GRR"
FT REGION 411..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 343..347
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 411..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 467..468
FT /note="Cleavage (when cotranslationally processed)"
SQ SEQUENCE 958 AA; 105854 MW; 192F5EDA791DCBC5 CRC64;
MMSVLKIENF DPYSCNGIED RNGMGYSTAL LNPIVLGQDL LMSYLSIIEQ PKQRGFRFRY
VCEGPSHRGL PGASSEKGKK TFPTVKIFNY VGMARIEVDL VTHTDPPRVH AHSLVGKHSN
KTGNCIVTVG PEDMTAQFNN LGIVHVTKKS QTEILKEKMK RNILRNTGRN TLTEVEERKI
EQEVKDLKKV TDLSIVRLKF TAYLPDSNGA YTLALPPVIS DPIHDSKSPG ASNLRISRMD
KTAGSVKGGD EVYLLCDKVQ KDDIEVQFYE DDENGWHAFG DFAPTDVHKQ YAIVFRTPPY
HTQKIDRPVT VFLQLKRKKG GDVSDSKQFT YYPLEQDKEE VERKRRKDLP TFNNHFYGGG
SPMGGAPPGS SFGQGGGSNI NYQYTGMNSA FYMSSPAGGG YHSSGHMMKH CSATNSSEKN
QQPSISIKKE GEEASACSQT DSATTAQKEA QCQMIMRQAN LRMLSLTQRT SRALLDYATT
ADPRMLLAVQ RHLTATQDEN GDTPLHLAVI HGQSSVIEQL VQIILSIPNQ QILNMSNHLQ
QTPLHLGVIT KQYSVVAFLL KAGADPTILD RYGNSVLHLA VQSEDDKMLG VLLKYPSVGQ
KNLINMPDYH GLSPVHWSVK MKNEKCLVLL VKAGANVNSA ERKSGKSPLH IAVEMDNLNL
AVFLVKKLHA DINAKTYGGN TPLHLAASRG SPMLTRMLVN EGANVLSEND EPVNKLPSCN
SDTSESDSDV QMDTDSDHHG DSDTDSSTAV DSECEHSAEE MHRREQRNIR PHCAMKRRYS
GHTAVDLTKS QKVRDILSKH TPGSASWKQK GPEPVNVLAL ETNTVQRLEK LLNEGQTGAD
WTELASRLRL QSLVETYKNT SSPTESLLRN YELAGGNLKE LINTLQSMGL NEGVELLCKS
ETYAKHHSPA ESKNDSAYES QSMEVDQSSG NLMDDSQKQT IPVSAAELCP TTEPTIGQ
