NFKB2_CHICK
ID NFKB2_CHICK Reviewed; 906 AA.
AC P98150;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Nuclear factor NF-kappa-B p100 subunit;
DE AltName: Full=DNA-binding factor KBF2;
DE AltName: Full=Lyt-10;
DE AltName: Full=Nuclear factor NF-kappa-B p97 subunit;
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;
DE AltName: Full=Nuclear factor NF-kappa-B p50B subunit;
GN Name=NFKB2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8230480; DOI=10.1128/jvi.67.12.7612-7617.1993;
RA Sif S., Gilmore T.D.;
RT "NF-kappa B p100 is one of the high-molecular-weight proteins complexed
RT with the v-Rel oncoprotein in transformed chicken spleen cells.";
RL J. Virol. 67:7612-7617(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=7510259; DOI=10.1016/0378-1119(94)90806-0;
RA Ikeda T., Hirota Y., Onodera T.;
RT "Isolation of a cDNA encoding the chicken p50B/p97 (Lyt-10) transcription
RT factor.";
RL Gene 138:193-196(1994).
RN [3]
RP IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
RX PubMed=11529676; DOI=10.1006/mcbr.2001.0290;
RA Piffat K.A., Hrdlickova R., Nehyba J., Ikeda T., Liss A., Huang S., Sif S.,
RA Gilmore T.D., Bose H.R. Jr.;
RT "The chicken RelB transcription factor has transactivation sequences and a
RT tissue-specific expression pattern that are distinct from mammalian RelB.";
RL Mol. Cell Biol. Res. Commun. 4:266-275(2001).
CC -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in
CC almost all cell types and is the endpoint of a series of signal
CC transduction events that are initiated by a vast array of stimuli
CC related to many biological processes such as inflammation, immunity,
CC differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B
CC is a homo- or heterodimeric complex formed by the Rel-like domain-
CC containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and
CC NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target
CC genes and the individual dimers have distinct preferences for different
CC kappa-B sites that they can bind with distinguishable affinity and
CC specificity. Different dimer combinations act as transcriptional
CC activators or repressors, respectively. NF-kappa-B is controlled by
CC various mechanisms of post-translational modification and subcellular
CC compartmentalization as well as by interactions with other cofactors or
CC corepressors. NF-kappa-B complexes are held in the cytoplasm in an
CC inactive state complexed with members of the NF-kappa-B inhibitor (I-
CC kappa-B) family. In a conventional activation pathway, I-kappa-B is
CC phosphorylated by I-kappa-B kinases (IKKs) in response to different
CC activators, subsequently degraded thus liberating the active NF-kappa-B
CC complex which translocates to the nucleus. In a non-canonical
CC activation pathway, the MAP3K14-activated CHUK/IKKA homodimer
CC phosphorylates NFKB2/p100 associated with RelB, inducing its
CC proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B
CC RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a
CC transcriptional activator. NFKB2 appears to have dual functions such as
CC cytoplasmic retention of attached NF-kappa-B proteins by p100 and
CC generation of p52 by a cotranslational processing. The proteasome-
CC mediated process ensures the production of both p52 and p100 and
CC preserves their independent function. p52 binds to the kappa-B
CC consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of
CC genes involved in immune response and acute phase reactions. In concert
CC with RELB, may play a role in the regulation of the circadian clock (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NF-kappa-B RelB-p52 complex.
CC {ECO:0000269|PubMed:11529676}.
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 -!- 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. {ECO:0000250}.
CC -!- MISCELLANEOUS: NF-kappa-B p100 is one of the high-molecular-weight
CC proteins complexed with the v-rel oncoprotein in transformed chicken
CC spleen cells.
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DR EMBL; U00111; AAA03717.1; -; mRNA.
DR EMBL; D16367; BAA03868.1; -; mRNA.
DR PIR; I50404; I50404.
DR RefSeq; NP_989744.1; NM_204413.1.
DR AlphaFoldDB; P98150; -.
DR SMR; P98150; -.
DR STRING; 9031.ENSGALP00000042025; -.
DR PaxDb; P98150; -.
DR GeneID; 386574; -.
DR KEGG; gga:386574; -.
DR CTD; 4791; -.
DR VEuPathDB; HostDB:geneid_386574; -.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; P98150; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; P98150; -.
DR PRO; PR:P98150; -.
DR Proteomes; UP000000539; Unplaced.
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; 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 1: Evidence at protein level;
KW Activator; ANK repeat; Biological rhythms; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..906
FT /note="Nuclear factor NF-kappa-B p100 subunit"
FT /id="PRO_0000030325"
FT CHAIN 1..439
FT /note="Nuclear factor NF-kappa-B p52 subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030326"
FT DOMAIN 34..223
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REPEAT 472..501
FT /note="ANK 1"
FT REPEAT 511..540
FT /note="ANK 2"
FT REPEAT 544..573
FT /note="ANK 3"
FT REPEAT 582..611
FT /note="ANK 4"
FT REPEAT 616..646
FT /note="ANK 5"
FT REPEAT 650..679
FT /note="ANK 6"
FT DOMAIN 771..857
FT /note="Death"
FT REGION 345..374
FT /note="GRR"
FT REGION 677..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 336..340
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 857..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 439..440
FT /note="Cleavage (when cotranslationally processed)"
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="V -> G (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="S -> F (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="N -> K (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="C -> G (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> SG (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="R -> A (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="E -> Q (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> G (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="T -> A (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 690..693
FT /note="VRVP -> SEA (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="L -> RC (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 759..774
FT /note="SPPILSCPPPPSRNHL -> RPDTELPTTPRAGNV (in Ref. 2;
FT BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="T -> S (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="Y -> D (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="T -> D (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 821..823
FT /note="ASA -> SVSL (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="P -> A (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="R -> A (in Ref. 2; BAA03868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 99667 MW; 0E0CE20DB4F30E62 CRC64;
MDEHFQPCLD GIDYDDFSFG SHMVEQKEPL METAVGPYLV IIEQPKQRGF RFRYVCEGPS
HGGLPGASSE KGHKTYPTVK ICNYEGMARI EVDLVTHSDP PRVHAHSLVG KQCNEAGNCV
AIVGPKDMTA QFSNLGVLHV TKKNMMEIMK EKLKKQKTRN TNGLLTEAEL REIELEAKEL
KKVMDLSIVR LRFTAYLRDS SGNFTLALQP VISDPIHDSK SPGASNLKIS RMDKTAGSVR
GGDEVYLLCD KVQKDDIEVR FYEDDENGWQ ASGDFSPTDV HKQYAIVFRT PPYHKPKIDR
PVTVFLQLKR KRGGDVSDSK QFTYYPVVED KEEVERNRKK VLPQFPQHFG GGSHMGGAGG
AGGFGAGGGG NLSFPYSSGL GYNNLYSSSP HPVGCGYQGG VQMKAASERD GDDRQAPTES
TYCRELQRHR HLCHLWLLAR RNAHALLDYS VTADPRMLLA VQRHLAASQD ENGDTPLHLA
IIHEQTAVIK QLIEVVVSIP SQQIINITNN LQQTPLHLAV ITKQPQVVQL LLEAHANPTL
LDRYGNSLLH LALQAADEEM LRMLLAHLAS ATPYLLHLPN FQGLLPVHLA VKAKSPACLD
LLVRKGADVN GVERQGGRTP LHLAVEMENL NMATHLVKKL GANVNSRTFA GNTPLHLAAG
LGSPTLTKLL LKAGADVQRE NDEPVSPSSV RVPSSDTDGD PEEQEQEQAM ELGEPALSPH
PTPEEEQEEA GPRQRLHTAL DLTRSQKVRD ILLQASQPSP PILSCPPPPS RNHLLSLDTD
ALQGLEQLLN QYGSGSDWME LAKRLGLCSL VETYKTTPSP ASALRSYELP GGSLGGLLEA
LDSMGLRGAV RMLRKPEPLE KLQSTEVKED SAYGSESVEE EQAARLKPRP VPEGELPHSQ
QQQQVH
