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Nuclear factor NF-kappa-B p105 subunit (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]

 NFKB1_CHICK             Reviewed;         983 AA.
Q04861; E1C613; F1NU28; O13075;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
18-APR-2012, sequence version 2.
05-DEC-2018, entry version 157.
RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
Name=NFKB1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1533881;
Capobianco A.J., Chang D., Mosialos G., Gilmore T.D.;
"p105, the NF-kappa B p50 precursor protein, is one of the cellular
proteins complexed with the v-Rel oncoprotein in transformed chicken
spleen cells.";
J. Virol. 66:3758-3767(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Spleen;
PubMed=7916720; DOI=10.1016/0378-1119(93)90645-J;
Ikeda T., Honjo K., Hirota Y., Onodera T.;
"Isolation of the chicken NF-kappa B p65 subunit-encoding cDNA and
characterization of its products.";
Gene 133:237-242(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Embryonic fibroblast;
PubMed=9233775; DOI=10.1038/sj.onc.1201162;
Cabannes E., Vives M.F., Bedard P.A.;
"Transcriptional and post-transcriptional regulation of kappaB-
controlled genes by pp60v-src.";
Oncogene 15:29-43(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl;
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
-!- FUNCTION: P105 is the precursor of the p50 subunit of the nuclear
factor NF-kappa-B, which binds to the kappa-B consensus sequence
5'-GGRNNYYCC-3', located in the enhancer region of genes involved
in immune response and acute phase reactions. The precursor
protein itself does not bind to DNA.
-!- SUBUNIT: Active NF-kappa-B is a heterodimer of an about 50 kDa
DNA-binding subunit and the weak DNA-binding subunit p65. Two
heterodimers might form a labile tetramer.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also
found in the cytoplasm in an inactive form complexed to an
inhibitor (I-kappa-B).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q04861-1; Sequence=Displayed;
Name=2;
IsoId=Q04861-2; Sequence=VSP_042871;
Name=3;
IsoId=Q04861-3; Sequence=VSP_042872;
-!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
retention, inhibition of DNA-binding by p50 homodimers, and/or
transcription activation.
-!- PTM: While translation occurs, the particular unfolded structure
after the GRR repeat promotes the generation of p50 making it an
acceptable substrate for the proteasome. This process is known as
cotranslational processing. The processed form is active and the
unprocessed form acts as an inhibitor (I kappa B-like), being able
to form cytosolic complexes with NF-kappa B, trapping it in the
cytoplasm. Complete folding of the region downstream of the GRR
repeat precludes processing (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation of Cys-66 affects DNA binding. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAB58343.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAB58343.1; Type=Erroneous translation; Note=Wrong genetic code used for translating the sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M86930; AAA49000.1; -; mRNA.
EMBL; D13719; BAA02872.1; -; mRNA.
EMBL; AF000241; AAB58343.1; ALT_SEQ; mRNA.
EMBL; AADN02031451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A41996; A41996.
RefSeq; NP_990465.1; NM_205134.1.
RefSeq; XP_015140901.1; XM_015285415.1. [Q04861-3]
UniGene; Gga.3531; -.
SMR; Q04861; -.
STRING; 9031.ENSGALP00000020084; -.
PaxDb; Q04861; -.
PRIDE; Q04861; -.
Ensembl; ENSGALT00000037607; ENSGALP00000036814; ENSGALG00000012304. [Q04861-3]
GeneID; 396033; -.
KEGG; gga:396033; -.
CTD; 4790; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000158625; -.
HOGENOM; HOG000004822; -.
HOVERGEN; HBG052613; -.
InParanoid; Q04861; -.
KO; K02580; -.
OMA; MTWIPRK; -.
OrthoDB; EOG091G03PF; -.
Reactome; R-GGA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-GGA-1227892; TRAF6 mediated NF-kB activation.
Reactome; R-GGA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-GGA-193692; Regulated proteolysis of p75NTR.
Reactome; R-GGA-202424; Downstream TCR signaling.
Reactome; R-GGA-209560; NF-kB is activated and signals survival.
Reactome; R-GGA-2871837; FCERI mediated NF-kB activation.
Reactome; R-GGA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-GGA-3214841; PKMTs methylate histone lysines.
Reactome; R-GGA-434001; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-GGA-434131; NFkB activation mediated by RIP1 complexed with activated TLR3.
Reactome; R-GGA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-GGA-448706; Interleukin-1 processing.
Reactome; R-GGA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-GGA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-GGA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-GGA-6798695; Neutrophil degranulation.
Reactome; R-GGA-9020702; Interleukin-1 signaling.
Reactome; R-GGA-933542; TRAF6 mediated NF-kB activation.
PRO; PR:Q04861; -.
Proteomes; UP000000539; Chromosome 4.
Bgee; ENSGALG00000012304; Expressed in 10 organ(s), highest expression level in female gonad.
ExpressionAtlas; Q04861; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00204; ANK; 2.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR030503; NF-kB_p105.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF9; PTHR24169:SF9; 1.
Pfam; PF12796; Ank_2; 2.
Pfam; PF00531; Death; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00248; ANK; 7.
SMART; SM00005; DEATH; 1.
SMART; SM00429; IPT; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
2: Evidence at transcript level;
Activator; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
Repeat; S-nitrosylation; Transcription; Transcription regulation.
CHAIN 1 983 Nuclear factor NF-kappa-B p105 subunit.
/FTId=PRO_0000030316.
CHAIN 1 ? Nuclear factor NF-kappa-B p50 subunit.
{ECO:0000250}.
/FTId=PRO_0000030317.
DOMAIN 47 372 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 540 569 ANK 1.
REPEAT 579 608 ANK 2.
REPEAT 612 641 ANK 3.
REPEAT 648 677 ANK 4.
REPEAT 682 712 ANK 5.
REPEAT 716 745 ANK 6.
REPEAT 769 799 ANK 7.
DOMAIN 804 891 Death.
REGION 377 397 GRR.
MOTIF 365 370 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 378 414 Gly-rich.
MOD_RES 66 66 S-nitrosocysteine. {ECO:0000250}.
MOD_RES 342 342 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 938 938 Phosphoserine. {ECO:0000250}.
VAR_SEQ 970 970 Y -> YG (in isoform 2).
{ECO:0000303|PubMed:1533881,
ECO:0000303|PubMed:9233775}.
/FTId=VSP_042871.
VAR_SEQ 971 983 RKAQCKAVIYLTR -> GQESSVQSSYIPN (in
isoform 3). {ECO:0000303|PubMed:7916720}.
/FTId=VSP_042872.
CONFLICT 111 111 V -> R (in Ref. 1; AAA49000).
{ECO:0000305}.
CONFLICT 513 513 A -> R (in Ref. 1; AAA49000 and 3;
AAB58343). {ECO:0000305}.
CONFLICT 696 696 V -> I (in Ref. 2; BAA02872).
{ECO:0000305}.
CONFLICT 708 710 ADV -> VDA (in Ref. 2; BAA02872).
{ECO:0000305}.
CONFLICT 774 774 L -> H (in Ref. 3; AAB58343).
{ECO:0000305}.
CONFLICT 848 848 R -> Q (in Ref. 1; AAA49000).
{ECO:0000305}.
CONFLICT 868 868 V -> G (in Ref. 1; AAA49000).
{ECO:0000305}.
CONFLICT 875 875 L -> F (in Ref. 1; AAA49000).
{ECO:0000305}.
CONFLICT 898 899 SH -> IY (in Ref. 2; BAA02872).
{ECO:0000305}.
CONFLICT 903 903 N -> K (in Ref. 1; AAA49000).
{ECO:0000305}.
CONFLICT 938 938 S -> T (in Ref. 3; AAB58343).
{ECO:0000305}.
SEQUENCE 983 AA; 107992 MW; B8885C7716393285 CRC64;
MAGEDPYIMG VSDPQMFAMD QLMGMSTIFN NTGYITSDLP LRTADGPYLQ IIEQPKQRGF
RFRYVCEGPS HGGLPGASSE KNKKSYPQVK ICNYVGPAKV IVQLVTNGKY VHLHAHSLVG
KFCEDGVCTV NAGPKDMVVG FANLGILHVT KKKVFETLET RMIDACKKGY NPGLLVHPEL
GYLQAEGCGD RQLTEREREI IRQAAVQQTK EMDLSVVRLM FTAFLPDSNG GFTRRLDPVI
SDAIYDSKAP NASNLKIVRM DRTAGCVTGG EEIYLLCDKV QKDDIQIRFY EEDENGGMWE
GFGDFSPTDV HRQFAIVFKT PKYRDVNITK PASVFVQLRR KSDLETSEPK PFLYYPEIKD
KEEVQRKRQK LMPNFSDGYG GGSGAGGGGM FGGGGGGAGS GFSYPSYGYS AFGGMHFHPG
TTKSNAGMKH ELSNSTVKKD EESSDKQSDK WDTKHDVKVE TVEKNECRTS GHNEEKEDAS
LCCKDEGNKP KCGCQDGLFL EKAMQLAKRH CNALFDYAVT GDVRMLLAVQ RHLTAVQDDN
GDNVLHLSII HLHRELVKNL LEVMPDMNYN NIINMRNDLY QTPLHLAVIT KQAEVVEDLL
KAGANVNLLD RHGNSVLHLA AAEGDDKILS LLLKHQKASS MIDLSNGEGL SAIHMVVTAN
SLSCLKLLIA AGVDVNAQEQ KSGRTALHLA VEQENVPLAG CLLLEGDADV DSTTYDGTTP
LHIAAGRGFT KLAAVLKAAG ADPHVENFEP LFDVEEDVKD DDDDEGIVPG TTPLDMAANW
EVYDILNGKP YIAAAAVSED LLSQGPLREL NESSKQQLYK LLETPDPSKN WSTLAEKLGL
GILNNAFRLS PSPSKTLLDN YKISGGTVQE LIAALTQMDH TEAIEVIQKA LSSSQRQSHQ
EDNTIEAFPS LSPTSFAKEE TGELYNHKFQ DPESTCDSGV ETSFRKLSFT YSDSLNSKSS
ITLSKMTLGY RKAQCKAVIY LTR


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