RELB_MOUSE
ID RELB_MOUSE Reviewed; 558 AA.
AC Q04863; Q8VE46;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Transcription factor RelB;
GN Name=Relb;
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].
RX PubMed=1732739; DOI=10.1128/mcb.12.2.674-684.1992;
RA Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U., Dobrzanski P.,
RA Bravo R.;
RT "RelB, a new Rel family transcription activator that can interact with p50-
RT NF-kappa B.";
RL Mol. Cell. Biol. 12:674-684(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
RX PubMed=8441398; DOI=10.1128/mcb.13.3.1572-1582.1993;
RA Dobrzanski P., Ryseck R.P., Bravo R.;
RT "Both N- and C-terminal domains of RelB are required for full
RT transactivation: role of the N-terminal leucine zipper-like motif.";
RL Mol. Cell. Biol. 13:1572-1582(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-429.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=7845467; DOI=10.1038/373531a0;
RA Burkly L., Hession C., Ogata L., Reilly C., Marconi L.A., Olson D.,
RA Tizard R., Cate R., Lo D.;
RT "Expression of relB is required for the development of thymic medulla and
RT dendritic cells.";
RL Nature 373:531-536(1995).
RN [6]
RP PHOSPHORYLATION AT THR-84 AND SER-552.
RX PubMed=11781828; DOI=10.1038/sj.onc.1204884;
RA Marienfeld R., Berberich-Siebelt F., Berberich I., Denk A., Serfling E.,
RA Neumann M.;
RT "Signal-specific and phosphorylation-dependent RelB degradation: a
RT potential mechanism of NF-kappaB control.";
RL Oncogene 20:8142-8147(2001).
RN [7]
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 [8]
RP SELF-ASSOCIATION, INTERACTION WITH NFKB1 AND NFKB2, AND MUTAGENESIS OF
RP SER-368.
RX PubMed=12874295; DOI=10.1074/jbc.m301521200;
RA Maier H.J., Marienfeld R., Wirth T., Baumann B.;
RT "Critical role of RelB serine 368 for dimerization and p100
RT stabilization.";
RL J. Biol. Chem. 278:39242-39250(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH ARNTL.
RX PubMed=22894897; DOI=10.4161/cc.21669;
RA Bellet M.M., Zocchi L., Sassone-Corsi P.;
RT "The RelB subunit of NFkappaB acts as a negative regulator of circadian
RT gene expression.";
RL Cell Cycle 11:3304-3311(2012).
RN [10]
RP FUNCTION.
RX PubMed=22565310; DOI=10.1172/jci60144;
RA Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
RA Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
RA Iovanna J.L.;
RT "Nuclear protein 1 promotes pancreatic cancer development and protects
RT cells from stress by inhibiting apoptosis.";
RL J. Clin. Invest. 122:2092-2103(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 277-378.
RX PubMed=16154093; DOI=10.1016/j.str.2005.06.018;
RA Huang D.B., Vu D., Ghosh G.;
RT "NF-kappaB RelB forms an intertwined homodimer.";
RL Structure 13:1365-1373(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH NFKB1.
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 which is
CC present in almost all cell types and is involved in many biological
CC processed such as inflammation, immunity, differentiation, cell growth,
CC tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric
CC complex formed by the Rel-like domain-containing proteins RELA/p65,
CC RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at
CC kappa-B sites in the DNA of their target genes and the individual
CC dimers have distinct preferences for different kappa-B sites that they
CC can bind with distinguishable affinity and specificity. Different dimer
CC combinations act as transcriptional activators or repressors,
CC respectively. NF-kappa-B is controlled by various mechanisms of post-
CC translational modification and subcellular compartmentalization as well
CC as by interactions with other cofactors or corepressors. NF-kappa-B
CC complexes are held in the cytoplasm in an inactive state complexed with
CC members of the NF-kappa-B inhibitor (I-kappa-B) family. In a
CC conventional activation pathway, I-kappa-B is phosphorylated by I-
CC kappa-B kinases (IKKs) in response to different activators,
CC subsequently degraded thus liberating the active NF-kappa-B complex
CC which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50
CC and RelB-p52 complexes are transcriptional activators. RELB neither
CC associates with DNA nor with RELA/p65 or REL. Stimulates promoter
CC activity in the presence of NFKB2/p49 (By similarity). As a member of
CC the NUPR1/RELB/IER3 survival pathway, may allow the development of
CC pancreatic intraepithelial neoplasias. Regulates the circadian clock by
CC repressing the transcriptional activator activity of the CLOCK-
CC ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased
CC repression of the heterodimer is seen in the presence of NFKB2/p52. Is
CC required for both T and B lymphocyte maturation and function (By
CC similarity). {ECO:0000250|UniProtKB:Q01201,
CC ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22894897}.
CC -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component of the
CC NF-kappa-B RelB-p52 complex (By similarity). Self-associates; the
CC interaction seems to be transient and may prevent degradation allowing
CC for heterodimer formation p50 or p52. Interacts with NFKB1/p50,
CC NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Interacts with
CC ARNTL/BMAL1 and the interaction is enhanced in the presence of CLOCK.
CC {ECO:0000250, ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:12874295,
CC ECO:0000269|PubMed:17869269, ECO:0000269|PubMed:22894897}.
CC -!- INTERACTION:
CC Q04863; PRO_0000030313 [P25799]: Nfkb1; NbExp=2; IntAct=EBI-1209145, EBI-1209141;
CC Q04863; Q9WTK5: Nfkb2; NbExp=3; IntAct=EBI-1209145, EBI-1209166;
CC Q04863; Q9Z1E3: Nfkbia; NbExp=4; IntAct=EBI-1209145, EBI-644427;
CC Q04863; O54910: Nfkbie; NbExp=2; IntAct=EBI-1209145, EBI-6688774;
CC Q04863; Q04863: Relb; NbExp=3; IntAct=EBI-1209145, EBI-1209145;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Note=Colocalizes with NEK6
CC in the centrosome. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, thymus and spleen.
CC Undetectable in liver, bome marrow, kidney and testis.
CC -!- DOMAIN: Both N- and C-terminal domains are required for transcriptional
CC activation.
CC -!- PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by
CC proteasomal degradation. {ECO:0000269|PubMed:11781828}.
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DR EMBL; M83380; AAA40041.1; -; mRNA.
DR EMBL; AK146932; BAE27543.1; -; mRNA.
DR EMBL; BC019765; AAH19765.1; -; mRNA.
DR EMBL; BC117793; AAI17794.1; -; mRNA.
DR EMBL; S56076; AAB25493.2; -; mRNA.
DR EMBL; S76754; AAB33259.1; -; Genomic_DNA.
DR CCDS; CCDS39799.1; -.
DR PIR; A42023; A42023.
DR PIR; I58091; I58091.
DR RefSeq; NP_001277386.1; NM_001290457.1.
DR RefSeq; NP_033072.2; NM_009046.2.
DR PDB; 1ZK9; X-ray; 2.18 A; A=277-378.
DR PDB; 1ZKA; X-ray; 2.20 A; A=277-378.
DR PDB; 2V2T; X-ray; 3.05 A; A=91-378.
DR PDB; 3DO7; X-ray; 3.05 A; A=88-383.
DR PDB; 3JSS; X-ray; 2.60 A; A=278-378.
DR PDB; 3JUZ; X-ray; 2.51 A; A=278-378.
DR PDB; 3JV0; X-ray; 2.65 A; A=278-378.
DR PDB; 3JV4; X-ray; 3.15 A; A/C/E=278-378.
DR PDB; 3JV6; X-ray; 2.78 A; A/C/E=278-378.
DR PDB; 4JGM; X-ray; 3.00 A; A=277-378.
DR PDB; 4JHB; X-ray; 2.44 A; A=277-378.
DR PDBsum; 1ZK9; -.
DR PDBsum; 1ZKA; -.
DR PDBsum; 2V2T; -.
DR PDBsum; 3DO7; -.
DR PDBsum; 3JSS; -.
DR PDBsum; 3JUZ; -.
DR PDBsum; 3JV0; -.
DR PDBsum; 3JV4; -.
DR PDBsum; 3JV6; -.
DR PDBsum; 4JGM; -.
DR PDBsum; 4JHB; -.
DR AlphaFoldDB; Q04863; -.
DR SMR; Q04863; -.
DR BioGRID; 202854; 4.
DR DIP; DIP-39585N; -.
DR IntAct; Q04863; 10.
DR MINT; Q04863; -.
DR STRING; 10090.ENSMUSP00000092355; -.
DR iPTMnet; Q04863; -.
DR PhosphoSitePlus; Q04863; -.
DR jPOST; Q04863; -.
DR MaxQB; Q04863; -.
DR PaxDb; Q04863; -.
DR PeptideAtlas; Q04863; -.
DR PRIDE; Q04863; -.
DR ProteomicsDB; 253203; -.
DR Antibodypedia; 3573; 684 antibodies from 43 providers.
DR DNASU; 19698; -.
DR Ensembl; ENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983.
DR Ensembl; ENSMUST00000098754; ENSMUSP00000096350; ENSMUSG00000002983.
DR GeneID; 19698; -.
DR KEGG; mmu:19698; -.
DR UCSC; uc012fbg.1; mouse.
DR CTD; 5971; -.
DR MGI; MGI:103289; Relb.
DR VEuPathDB; HostDB:ENSMUSG00000002983; -.
DR eggNOG; ENOG502QV8A; Eukaryota.
DR GeneTree; ENSGT00940000160230; -.
DR InParanoid; Q04863; -.
DR OMA; NQYREGA; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; Q04863; -.
DR TreeFam; TF325632; -.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR BioGRID-ORCS; 19698; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Relb; mouse.
DR EvolutionaryTrace; Q04863; -.
DR PRO; PR:Q04863; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q04863; protein.
DR Bgee; ENSMUSG00000002983; Expressed in peripheral lymph node and 136 other tissues.
DR ExpressionAtlas; Q04863; baseline and differential.
DR Genevisible; Q04863; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA: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:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0071470; P:cellular response to osmotic stress; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0030098; P:lymphocyte differentiation; ISO:MGI.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IMP:MGI.
DR GO; GO:0042088; P:T-helper 1 type immune response; IMP:MGI.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
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; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030496; RelB.
DR InterPro; IPR032399; RelB_leu_zip.
DR InterPro; IPR032400; RelB_transact.
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:SF18; PTHR24169:SF18; 1.
DR Pfam; PF16180; RelB_leu_zip; 1.
DR Pfam; PF16181; RelB_transactiv; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS01204; REL_1; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Biological rhythms; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..558
FT /note="Transcription factor RelB"
FT /id="PRO_0000205174"
FT DOMAIN 103..418
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 22..50
FT /note="Leucine-zipper"
FT MOTIF 387..391
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 411..416
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01201"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11781828"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11781828"
FT MUTAGEN 368
FT /note="S->A,E: Strongly reduces transcriptional activity
FT and interaction with NFKB1/p50 and NFKB2/p52."
FT /evidence="ECO:0000269|PubMed:12874295"
FT CONFLICT 51
FT /note="D -> V (in Ref. 1; AAA40041)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="L -> Q (in Ref. 1; AAA40041)"
FT /evidence="ECO:0000305"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3DO7"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3DO7"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3DO7"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2V2T"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3DO7"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2V2T"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2V2T"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3DO7"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:3DO7"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2V2T"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1ZKA"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1ZK9"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4JHB"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3DO7"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1ZK9"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1ZKA"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1ZK9"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1ZK9"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1ZK9"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:4JHB"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:4JHB"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1ZK9"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1ZK9"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:1ZK9"
SQ SEQUENCE 558 AA; 60305 MW; AA49781A891ED7B8 CRC64;
MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL DGTQLSEMPR
LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC PRPYLVITEQ PKQRGMRFRY
ECEGRSAGSI LGESSTEASK TLPAIELRDC GGLREVEVTA CLVWKDWPHR VHPHSLVGKD
CTDGVCRVRL RPHVSPRHSF NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD
MNVVRICFQA SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY
LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS EPVTVNVFLQ
RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL SSSDPHGIES KRRKKKPVFL
DHFLPGHSSG LFLPPSALQP ADSDFFPASI SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM
LDLLPPAPPL ASAVVGSGGA GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ
YREAAFGGGL LSPGPEAT
