NFKB1_MOUSE
ID NFKB1_MOUSE Reviewed; 971 AA.
AC P25799; B2RRQ6; Q3TZE8; Q3V2V6; Q6TDG8; Q75ZL1; Q80Y21; Q8C712;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
DE AltName: Full=DNA-binding factor KBF1;
DE AltName: Full=EBP-1;
DE AltName: Full=NF-kappa-B1 p84/NF-kappa-B1 p98;
DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
DE Contains:
DE RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
GN Name=Nfkb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Spleen;
RX PubMed=2203532; DOI=10.1016/0092-8674(90)90276-k;
RA Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P., Baltimore D.;
RT "Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and
RT dorsal.";
RL Cell 62:1019-1029(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
RX PubMed=1339305; DOI=10.1016/0092-8674(92)90082-n;
RA Inoue J., Kerr L.D., Kakizuka A., Verma I.M.;
RT "I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110
RT NF-kappa B: a new member of the I kappa B family.";
RL Cell 68:1109-1120(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8398903;
RA Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J.,
RA Grumont R.J.;
RT "The activity of a 70 kilodalton I kappa B molecule identical to the
RT carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein
RT kinase A.";
RL Cell Growth Differ. 4:617-627(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RX PubMed=7969179; DOI=10.1128/mcb.14.12.8460-8470.1994;
RA Grumont R.J., Fecondo J., Gerondakis S.;
RT "Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of the
RT p50 precursor NF-kappa B1 that can function as a transactivator of NF-kappa
RT B-regulated transcription.";
RL Mol. Cell. Biol. 14:8460-8470(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6CrSlc; TISSUE=Spleen;
RA Ohara O., Kitamura H., Nakagawa T.;
RT "Mus musculus transcription factor NF-kappa-B DNA binding subunit(p105)
RT mRNA, complete cds.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C3H/HeJBir, and C57BL/6J;
RA Bleich A., Hedrich H.J., Schlegelberger B., Maehler M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Embryo;
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).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-129.
RC STRAIN=C57BL/6J; TISSUE=Lung carcinoma;
RA Gerhauser I., Ulrich R., Baumgartner W.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), AND SUBCELLULAR LOCATION.
RX PubMed=8183915; DOI=10.1073/pnas.91.10.4367;
RA Grumont R.J., Gerondakis S.;
RT "Alternative splicing of RNA transcripts encoded by the murine p105 NF-
RT kappa B gene generates I kappa B gamma isoforms with different inhibitory
RT activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994).
RN [12]
RP COTRANSLATIONAL FOLDING OF P105.
RX PubMed=9529257; DOI=10.1016/s0092-8674(00)81409-9;
RA Lin L., DeMartino G.N., Greene W.C.;
RT "Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome.";
RL Cell 92:819-828(1998).
RN [13]
RP INTERACTION WITH NFKBIZ.
RX PubMed=11356851; DOI=10.1074/jbc.m103426200;
RA Yamazaki S., Muta T., Takeshige K.;
RT "A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli,
RT negatively regulates nuclear factor-kappaB in the nuclei.";
RL J. Biol. Chem. 276:27657-27662(2001).
RN [14]
RP INTERACTION WITH NFKBID.
RX PubMed=11931770; DOI=10.1016/s1097-2765(02)00469-0;
RA Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T.,
RA Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L.,
RA Clayton L.K.;
RT "Peptide-induced negative selection of thymocytes activates transcription
RT of an NF-kappa B inhibitor.";
RL Mol. Cell 9:637-648(2002).
RN [15]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
RX PubMed=15051764; DOI=10.1084/jem.20031272;
RA Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D.,
RA Willems F., Goldman M.;
RT "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription
RT in neonatal dendritic cells.";
RL J. Exp. Med. 199:1011-1016(2004).
RN [16]
RP INTERACTION WITH NFKBIZ.
RX PubMed=15241416; DOI=10.1038/nature02738;
RA Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K.,
RA Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S.,
RA Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.;
RT "Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible
RT nuclear protein IkappaBzeta.";
RL Nature 430:218-222(2004).
RN [17]
RP FUNCTION, AND INTERACTION WITH FEM1AA.
RX PubMed=18270204; DOI=10.1074/jbc.m709663200;
RA Minami M., Shimizu K., Okamoto Y., Folco E., Ilasaca M.L., Feinberg M.W.,
RA Aikawa M., Libby P.;
RT "Prostaglandin E receptor type 4-associated protein interacts directly with
RT NF-kappaB1 and attenuates macrophage activation.";
RL J. Biol. Chem. 283:9692-9703(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-940 AND THR-946, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364.
RX PubMed=7530332; DOI=10.1038/373303a0;
RA Ghosh G., van Duyne G., Ghosh S., Sigler P.B.;
RT "Structure of NF-kappa B p50 homodimer bound to a kappa B site.";
RL Nature 373:303-310(1995).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350.
RX PubMed=9384558; DOI=10.1016/s0969-2126(97)00293-1;
RA Huang D.B., Huxford T., Chen Y.Q., Ghosh G.;
RT "The role of DNA in the mechanism of NFkappaB dimer formation: crystal
RT structures of the dimerization domains of the p50 and p65 subunits.";
RL Structure 5:1427-1436(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363.
RX PubMed=9865694; DOI=10.1016/s0092-8674(00)81699-2;
RA Huxford T., Huang D.B., Malek S., Ghosh G.;
RT "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals
RT mechanisms of NF-kappaB inactivation.";
RL Cell 95:759-770(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350.
RX PubMed=9450761; DOI=10.1038/34956;
RA Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.;
RT "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB
RT bound to DNA.";
RL Nature 391:410-413(1998).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350.
RX PubMed=11970948; DOI=10.1074/jbc.m200006200;
RA Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G.;
RT "The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to
RT the interferon beta -kappa B site.";
RL J. Biol. Chem. 277:24694-24700(2002).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350.
RX PubMed=11970949; DOI=10.1074/jbc.m200007200;
RA Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G.;
RT "The kappa B DNA sequence from the HIV long terminal repeat functions as an
RT allosteric regulator of HIV transcription.";
RL J. Biol. Chem. 277:24701-24708(2002).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED WITH
RP RNA APTAMER.
RX PubMed=12886018; DOI=10.1073/pnas.1632011100;
RA Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III, Ghosh G.;
RT "Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA
RT aptamer.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB.
RX PubMed=17869269; DOI=10.1016/j.jmb.2007.08.039;
RA Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.;
RT "X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of
RT multiple dimers on tandem kappaB sites.";
RL J. Mol. Biol. 373:723-734(2007).
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 and the heterodimeric p65-p50 complex appears to be most
CC abundant one. The dimers bind at kappa-B sites in the DNA of their
CC target genes and the individual dimers have distinct preferences for
CC different kappa-B sites that they can bind with distinguishable
CC affinity and specificity. Different dimer combinations act as
CC transcriptional activators or repressors, respectively. NF-kappa-B is
CC controlled by various mechanisms of post-translational modification and
CC subcellular compartmentalization as well as by interactions with other
CC cofactors or corepressors. NF-kappa-B complexes are held in the
CC cytoplasm in an inactive state complexed with members of the NF-kappa-B
CC inhibitor (I-kappa-B) family. In a conventional activation pathway, I-
CC kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to
CC different activators, subsequently degraded thus liberating the active
CC NF-kappa-B complex which translocates to the nucleus. NF-kappa-B
CC heterodimeric p65-p50 and RelB-p50 complexes are transcriptional
CC activators. The NF-kappa-B p50-p50 homodimer is a transcriptional
CC repressor, but can act as a transcriptional activator when associated
CC with BCL3. NFKB1 appears to have dual functions such as cytoplasmic
CC retention of attached NF-kappa-B proteins by p105 and generation of p50
CC by a cotranslational processing. The proteasome-mediated process
CC ensures the production of both p50 and p105 and preserves their
CC independent function, although processing of NFKB1/p105 also appears to
CC occur post-translationally. p50 binds to the kappa-B consensus sequence
CC 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in
CC immune response and acute phase reactions. Plays a role in the
CC regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as
CC inhibitors of transactivation of p50 NF-kappa-B subunit, probably by
CC sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105)
CC acts as a transactivator of NF-kappa-B-regulated gene expression. In a
CC complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK
CC signaling; active MAP3K8 is released by proteasome-dependent
CC degradation of NFKB1/p105. {ECO:0000269|PubMed:18270204}.
CC -!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex (By similarity).
CC Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity).
CC Component of the NF-kappa-B p105-p50 complex (By similarity). Component
CC of the NF-kappa-B p50-c-Rel complex (By similarity). Component of a
CC complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By
CC similarity). Also interacts with MAP3K8 (By similarity). NF-kappa-B p50
CC subunit interacts with NCOA3 coactivator, which may coactivate NF-
CC kappa-B dependent expression via its histone acetyltransferase activity
CC (By similarity). Interacts with DSIPI; this interaction prevents
CC nuclear translocation and DNA-binding (By similarity). Interacts with
CC SPAG9 and UNC5CL (By similarity). NFKB1/p105 interacts with CFLAR; the
CC interaction inhibits p105 processing into p50 (By similarity).
CC NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By
CC similarity). Interacts with GSK3B; the interaction prevents processing
CC of p105 to p50 (By similarity). NFKB1/p50 interacts with NFKBIE (By
CC similarity). NFKB1/p50 interacts with NFKBIZ (PubMed:11356851,
CC PubMed:15241416). Nuclear factor NF-kappa-B p50 subunit interacts with
CC NFKBID (PubMed:11931770). Directly interacts with MEN1 (By similarity).
CC Interacts with HIF1AN (By similarity). Interacts with FEM1AA;
CC interaction is direct (PubMed:18270204). {ECO:0000250|UniProtKB:P19838,
CC ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:11931770,
CC ECO:0000269|PubMed:15241416, ECO:0000269|PubMed:18270204}.
CC -!- INTERACTION:
CC P25799; Q9DBR0: Akap8; NbExp=4; IntAct=EBI-643958, EBI-4285802;
CC P25799; O09106: Hdac1; NbExp=2; IntAct=EBI-643958, EBI-301912;
CC P25799; Q04207: Rela; NbExp=6; IntAct=EBI-643958, EBI-644400;
CC P25799; Q15788: NCOA1; Xeno; NbExp=2; IntAct=EBI-643958, EBI-455189;
CC P25799-1; Q04207: Rela; NbExp=6; IntAct=EBI-643974, EBI-644400;
CC PRO_0000030312; Q04207: Rela; NbExp=3; IntAct=EBI-1209193, EBI-644400;
CC PRO_0000030313; Q3V096: Ankrd42; NbExp=3; IntAct=EBI-1209141, EBI-15861272;
CC PRO_0000030313; Q04863: Relb; NbExp=2; IntAct=EBI-1209141, EBI-1209145;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found
CC in the cytoplasm in an inactive form complexed to an inhibitor (I-
CC kappa-B).
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus. Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=p105;
CC IsoId=P25799-1; Sequence=Displayed;
CC Name=2; Synonyms=p84;
CC IsoId=P25799-2; Sequence=VSP_005583;
CC Name=3; Synonyms=p98;
CC IsoId=P25799-3; Sequence=VSP_005584;
CC Name=4;
CC IsoId=P25799-4; Sequence=VSP_017237, VSP_017238;
CC Name=5; Synonyms=P70, I-kappa-B gamma;
CC IsoId=P25799-5; Sequence=VSP_017236;
CC Name=6; Synonyms=p63, I-kappa-B gamma-1;
CC IsoId=P25799-6; Sequence=VSP_017236, VSP_005584;
CC Name=7; Synonyms=p55, I-kappa-B gamma-2;
CC IsoId=P25799-7; Sequence=VSP_017236, VSP_005583;
CC -!- INDUCTION: By phorbol ester and TNF-alpha.
CC -!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
CC retention, inhibition of DNA-binding, and transcription activation.
CC -!- DOMAIN: Glycine-rich region (GRR) appears to be a critical element in
CC the generation of p50.
CC -!- PTM: While translation occurs, the particular unfolded structure after
CC the GRR repeat promotes the generation of p50 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
CC processing.
CC -!- PTM: Phosphorylation at 'Ser-930' and 'Ser-935' are required for
CC BTRC/BTRCP-mediated proteolysis. {ECO:0000250}.
CC -!- PTM: Polyubiquitination seems to allow p105 processing.
CC -!- PTM: S-nitrosylation of Cys-59 affects DNA binding. {ECO:0000250}.
CC -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
CC prostaglandin-J2 is autocatalytic and reversible. It may occur as an
CC alternative to other cysteine modifications, such as S-nitrosylation
CC and S-palmitoylation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 7]: Inhibits the activity of the p50 NF-kappa-B
CC subunit. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M57999; AAA40415.1; -; mRNA.
DR EMBL; S89033; AAB21851.1; -; mRNA.
DR EMBL; S66656; AAB28573.1; -; mRNA.
DR EMBL; AB119195; BAC84979.1; -; mRNA.
DR EMBL; AY521462; AAS00547.1; -; mRNA.
DR EMBL; AY521463; AAS00548.1; -; mRNA.
DR EMBL; CH466532; EDL12143.1; -; Genomic_DNA.
DR EMBL; BC050841; AAH50841.1; -; mRNA.
DR EMBL; BC138535; AAI38536.1; -; mRNA.
DR EMBL; BC138536; AAI38537.1; -; mRNA.
DR EMBL; AY423849; AAR00341.1; -; mRNA.
DR EMBL; AK052726; BAC35117.1; ALT_INIT; mRNA.
DR EMBL; AK089660; BAE43399.1; -; mRNA.
DR EMBL; AK157915; BAE34261.1; -; mRNA.
DR CCDS; CCDS17858.1; -. [P25799-1]
DR PIR; A35697; A35697.
DR RefSeq; NP_032715.2; NM_008689.2. [P25799-1]
DR RefSeq; XP_006501169.1; XM_006501106.2. [P25799-3]
DR PDB; 1BFS; X-ray; 2.20 A; A=245-350.
DR PDB; 1IKN; X-ray; 2.30 A; C=245-363.
DR PDB; 1LE5; X-ray; 2.75 A; B/F=39-350.
DR PDB; 1LE9; X-ray; 3.00 A; B/F=39-350.
DR PDB; 1LEI; X-ray; 2.70 A; B=39-350.
DR PDB; 1NFK; X-ray; 2.30 A; A/B=39-363.
DR PDB; 1OOA; X-ray; 2.45 A; A/B=39-363.
DR PDB; 1U36; X-ray; 1.89 A; A=245-350.
DR PDB; 1U3J; X-ray; 1.90 A; A=245-350.
DR PDB; 1U3Y; X-ray; 1.90 A; A=245-350.
DR PDB; 1U3Z; X-ray; 1.90 A; A=245-350.
DR PDB; 1U41; X-ray; 2.20 A; A/B/C/D=245-350.
DR PDB; 1U42; X-ray; 2.70 A; A=245-350.
DR PDB; 1VKX; X-ray; 2.90 A; B=39-350.
DR PDB; 2I9T; X-ray; 2.80 A; B=39-350.
DR PDB; 2V2T; X-ray; 3.05 A; B=38-363.
DR PDB; 3JV4; X-ray; 3.15 A; B/D/F=245-359.
DR PDBsum; 1BFS; -.
DR PDBsum; 1IKN; -.
DR PDBsum; 1LE5; -.
DR PDBsum; 1LE9; -.
DR PDBsum; 1LEI; -.
DR PDBsum; 1NFK; -.
DR PDBsum; 1OOA; -.
DR PDBsum; 1U36; -.
DR PDBsum; 1U3J; -.
DR PDBsum; 1U3Y; -.
DR PDBsum; 1U3Z; -.
DR PDBsum; 1U41; -.
DR PDBsum; 1U42; -.
DR PDBsum; 1VKX; -.
DR PDBsum; 2I9T; -.
DR PDBsum; 2V2T; -.
DR PDBsum; 3JV4; -.
DR AlphaFoldDB; P25799; -.
DR SMR; P25799; -.
DR BioGRID; 201751; 15.
DR CORUM; P25799; -.
DR DIP; DIP-85N; -.
DR IntAct; P25799; 24.
DR MINT; P25799; -.
DR STRING; 10090.ENSMUSP00000029812; -.
DR ChEMBL; CHEMBL1949489; -.
DR iPTMnet; P25799; -.
DR PhosphoSitePlus; P25799; -.
DR EPD; P25799; -.
DR jPOST; P25799; -.
DR MaxQB; P25799; -.
DR PaxDb; P25799; -.
DR PeptideAtlas; P25799; -.
DR PRIDE; P25799; -.
DR ProteomicsDB; 287411; -. [P25799-1]
DR ProteomicsDB; 287412; -. [P25799-2]
DR ProteomicsDB; 287413; -. [P25799-3]
DR ProteomicsDB; 287414; -. [P25799-4]
DR ProteomicsDB; 287415; -. [P25799-5]
DR ProteomicsDB; 287416; -. [P25799-6]
DR ProteomicsDB; 287417; -. [P25799-7]
DR ABCD; P25799; 1 sequenced antibody.
DR Antibodypedia; 3415; 2446 antibodies from 51 providers.
DR DNASU; 18033; -.
DR Ensembl; ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
DR Ensembl; ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
DR GeneID; 18033; -.
DR KEGG; mmu:18033; -.
DR UCSC; uc008rlw.1; mouse. [P25799-1]
DR UCSC; uc008rly.1; mouse. [P25799-4]
DR UCSC; uc012cyf.1; mouse. [P25799-6]
DR CTD; 4790; -.
DR MGI; MGI:97312; Nfkb1.
DR VEuPathDB; HostDB:ENSMUSG00000028163; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000158625; -.
DR HOGENOM; CLU_004343_1_0_1; -.
DR InParanoid; P25799; -.
DR OMA; MTWIPRK; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; P25799; -.
DR TreeFam; TF325632; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-209560; NF-kB is activated and signals survival.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-448706; Interleukin-1 processing.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 18033; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Nfkb1; mouse.
DR EvolutionaryTrace; P25799; -.
DR PRO; PR:P25799; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P25799; protein.
DR Bgee; ENSMUSG00000028163; Expressed in granulocyte and 264 other tissues.
DR ExpressionAtlas; P25799; baseline and differential.
DR Genevisible; P25799; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0071159; C:NF-kappaB complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISO:MGI.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; ISO:MGI.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:1904630; P:cellular response to diterpene; ISO:MGI.
DR GO; GO:0071359; P:cellular response to dsRNA; IMP:MGI.
DR GO; GO:1904632; P:cellular response to glucoside; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:1901653; P:cellular response to peptide; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
DR GO; GO:0048535; P:lymph node development; TAS:MGI.
DR GO; GO:0060056; P:mammary gland involution; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; ISO:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:MGI.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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; IPR030503; NF-kB_p105.
DR InterPro; IPR000451; NFkB/Dor.
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:SF9; PTHR24169:SF9; 1.
DR Pfam; PF00023; Ank; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; ANK repeat;
KW Apoptosis; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Hydroxylation; Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-nitrosylation; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..971
FT /note="Nuclear factor NF-kappa-B p105 subunit"
FT /id="PRO_0000030312"
FT CHAIN 1..431
FT /note="Nuclear factor NF-kappa-B p50 subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030313"
FT DOMAIN 40..365
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REPEAT 538..567
FT /note="ANK 1"
FT REPEAT 577..606
FT /note="ANK 2"
FT REPEAT 610..639
FT /note="ANK 3"
FT REPEAT 646..675
FT /note="ANK 4"
FT REPEAT 680..710
FT /note="ANK 5"
FT REPEAT 714..743
FT /note="ANK 6"
FT REPEAT 767..797
FT /note="ANK 7"
FT DOMAIN 801..888
FT /note="Death"
FT REGION 370..392
FT /note="GRR"
FT REGION 433..971
FT /note="Interaction with CFLAR"
FT /evidence="ECO:0000250"
FT REGION 439..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..680
FT /note="Essential for interaction with HIF1AN"
FT /evidence="ECO:0000250"
FT MOTIF 358..363
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT SITE 431..432
FT /note="Cleavage (when cotranslationally processed)"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 335
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 674
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63369"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 910
FT /note="Phosphoserine; by GSK3-beta; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 930
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 935
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 946
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 59
FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9-
FT yl)cysteine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19838"
FT VAR_SEQ 1..364
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:1339305,
FT ECO:0000303|PubMed:8398903"
FT /id="VSP_017236"
FT VAR_SEQ 353..356
FT /note="DKEE -> GTWV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017237"
FT VAR_SEQ 357..971
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017238"
FT VAR_SEQ 780..971
FT /note="VFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLEIPDPDKNWATL
FT AQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQAAFRT
FT PATTASSPVTTAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDS
FT PLLSLNKMPHGYGQEGPIEGKI -> GT (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:7969179"
FT /id="VSP_005583"
FT VAR_SEQ 860..971
FT /note="VSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTAQVHCLPLSS
FT SSTRQHIDELRDSDSVCDSGVETSFRKLSFTESLTGDSPLLSLNKMPHGYGQEGPIEGK
FT I -> MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL (in isoform 3 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:7969179"
FT /id="VSP_005584"
FT CONFLICT 111
FT /note="L -> P (in Ref. 9; AAR00341)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="E -> G (in Ref. 10; BAC35117)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="H -> D (in Ref. 10; BAE34261)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="A -> G (in Ref. 10; BAE34261)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="A -> P (in Ref. 1; AAA40415, 2; AAB21851 and 3;
FT AAB28573)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="A -> T (in Ref. 10; BAE34261)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="P -> A (in Ref. 10; BAE43399)"
FT /evidence="ECO:0000305"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1NFK"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1VKX"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1OOA"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1LE9"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1NFK"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1OOA"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1VKX"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:1NFK"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1OOA"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1NFK"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:1OOA"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1VKX"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1OOA"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1U36"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1NFK"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:1U36"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1BFS"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1U36"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1U36"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:1U36"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:1U36"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1IKN"
SQ SEQUENCE 971 AA; 105615 MW; 91EA9C595E375C30 CRC64;
MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE
GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV
CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG
GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS
KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP
TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK
RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG
VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA
STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD
SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV
GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL
PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH
IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV
FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL
NNAFRLSPAP SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT
TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP LLSLNKMPHG
YGQEGPIEGK I
