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 14-OCT-2015, entry version 129. DE RecName: Full=Transcription factor RelB; GN Name=Relb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1732739; RA Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U., RA Dobrzanski P., Bravo R.; RT "RelB, a new Rel family transcription activator that can interact with RT p50-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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-116. RX PubMed=8441398; 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/6; 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 RT and 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., RA Serfling E., 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., RA Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., RA Reinherz E.L., Clayton L.K.; RT "Peptide-induced negative selection of thymocytes activates RT transcription 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 RT circadian 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 RP 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 RT of 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 CC is present in almost all cell types and is involved in many CC biological processed such as inflammation, immunity, CC differentiation, cell growth, tumorigenesis and apoptosis. NF- CC kappa-B is a homo- or heterodimeric complex formed by the Rel-like CC domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, CC REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of CC their target genes and the individual dimers have distinct CC preferences for different kappa-B sites that they can bind with CC 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 CC post-translational modification and subcellular CC 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- CC kappa-B inhibitor (I-kappa-B) family. In a conventional activation CC pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) CC in response to different activators, subsequently degraded thus CC liberating the active NF-kappa-B complex which translocates to the CC nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes CC are transcriptional activators. RELB neither associates with DNA CC nor with RELA/p65 or REL. Stimulates promoter activity in the CC presence of NFKB2/p49 (By similarity). As a member of the CC NUPR1/RELB/IER3 survival pathway, may allow the development of CC pancreatic intraepithelial neoplasias. Regulates the circadian CC clock by repressing the transcriptional activator activity of the CC CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. CC Increased repression of the heterodimer is seen in the presence of CC NFKB2/p52. {ECO:0000250, ECO:0000269|PubMed:22565310, CC ECO:0000269|PubMed:22894897}. CC -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component CC of the NF-kappa-B RelB-p52 complex (By similarity). Self- CC associates; the interaction seems to be transient and may prevent CC degradation allowing for heterodimer formation p50 or p52. CC Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with CC NFKBID. Interacts with ARNTL/BMAL1 and the interaction is enhanced CC in the presence of CLOCK. {ECO:0000250, CC ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:12874295, CC ECO:0000269|PubMed:17869269, ECO:0000269|PubMed:22894897}. CC -!- INTERACTION: CC P25799:Nfkb1; NbExp=2; IntAct=EBI-1209145, EBI-1209141; CC Q9WTK5:Nfkb2; NbExp=2; IntAct=EBI-1209145, EBI-1209166; CC Q9Z1E3:Nfkbia; NbExp=4; IntAct=EBI-1209145, EBI-644427; CC O54910:Nfkbie; NbExp=2; IntAct=EBI-1209145, EBI-6688774; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome {ECO:0000250}. CC Note=Colocalizes with NEK6 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 CC transcriptional activation. CC -!- PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by CC proteasomal degradation. {ECO:0000269|PubMed:11781828}. CC -!- SIMILARITY: Contains 1 RHD (Rel-like) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00265}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.1741; -. 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 ProteinModelPortal; Q04863; -. DR SMR; Q04863; 88-383. DR BioGrid; 202854; 3. DR DIP; DIP-39585N; -. DR IntAct; Q04863; 4. DR MINT; MINT-225343; -. DR STRING; 10090.ENSMUSP00000092355; -. DR PhosphoSite; Q04863; -. DR MaxQB; Q04863; -. DR PRIDE; Q04863; -. 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 eggNOG; NOG119056; -. DR GeneTree; ENSGT00500000044765; -. DR HOGENOM; HOG000148598; -. DR HOVERGEN; HBG017021; -. DR InParanoid; Q04863; -. DR KO; K09253; -. DR OMA; DDGFAYD; -. DR OrthoDB; EOG7VHSWT; -. 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 EvolutionaryTrace; Q04863; -. DR NextBio; 297052; -. DR PRO; PR:Q04863; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; Q04863; -. DR ExpressionAtlas; Q04863; baseline and differential. DR Genevisible; Q04863; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central. DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI. DR GO; GO:0071470; P:cellular response to osmotic stress; IEA:Ensembl. 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:0043011; P:myeloid dendritic cell differentiation; IMP:MGI. DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. 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:0010628; P:positive regulation of gene expression; IMP:MGI. 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 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. 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. DR InterPro; IPR000451; NFkB/Dor. DR InterPro; IPR008967; p53-like_TF_DNA-bd. DR InterPro; IPR030496; RelB. DR InterPro; IPR030492; RHD_CS. DR InterPro; IPR011539; RHD_DNA_bind_dom. DR PANTHER; PTHR24169; PTHR24169; 1. DR PANTHER; PTHR24169:SF18; PTHR24169:SF18; 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; Complete proteome; KW Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 558 Transcription factor RelB. FT /FTId=PRO_0000205174. FT DOMAIN 103 418 RHD. {ECO:0000255|PROSITE- FT ProRule:PRU00265}. FT REGION 22 50 Leucine-zipper. FT MOTIF 387 391 Nuclear localization signal. FT {ECO:0000255}. FT MOTIF 411 416 Nuclear localization signal. FT {ECO:0000255}. FT MOD_RES 19 19 Phosphoserine. FT {ECO:0000250|UniProtKB:Q01201}. FT MOD_RES 84 84 Phosphothreonine. FT {ECO:0000269|PubMed:11781828}. FT MOD_RES 552 552 Phosphoserine. FT {ECO:0000269|PubMed:11781828}. FT MUTAGEN 368 368 S->A,E: Strongly reduces transcriptional FT activity and interaction with NFKB1/p50 FT and NFKB2/p52. FT {ECO:0000269|PubMed:12874295}. FT CONFLICT 51 51 D -> V (in Ref. 1; AAA40041). FT {ECO:0000305}. FT CONFLICT 142 142 L -> Q (in Ref. 1; AAA40041). FT {ECO:0000305}. FT STRAND 95 97 {ECO:0000244|PDB:3DO7}. FT STRAND 104 109 {ECO:0000244|PDB:2V2T}. FT STRAND 113 116 {ECO:0000244|PDB:3DO7}. FT HELIX 121 123 {ECO:0000244|PDB:2V2T}. FT STRAND 132 134 {ECO:0000244|PDB:2V2T}. FT STRAND 137 139 {ECO:0000244|PDB:3DO7}. FT STRAND 145 149 {ECO:0000244|PDB:2V2T}. FT STRAND 156 160 {ECO:0000244|PDB:2V2T}. FT STRAND 165 168 {ECO:0000244|PDB:2V2T}. FT STRAND 173 178 {ECO:0000244|PDB:2V2T}. FT STRAND 182 184 {ECO:0000244|PDB:2V2T}. FT STRAND 186 190 {ECO:0000244|PDB:2V2T}. FT TURN 192 194 {ECO:0000244|PDB:2V2T}. FT STRAND 197 199 {ECO:0000244|PDB:3DO7}. FT STRAND 204 207 {ECO:0000244|PDB:2V2T}. FT TURN 210 212 {ECO:0000244|PDB:2V2T}. FT HELIX 213 222 {ECO:0000244|PDB:2V2T}. FT STRAND 234 236 {ECO:0000244|PDB:3DO7}. FT STRAND 241 245 {ECO:0000244|PDB:2V2T}. FT STRAND 250 252 {ECO:0000244|PDB:2V2T}. FT STRAND 255 257 {ECO:0000244|PDB:2V2T}. FT STRAND 270 274 {ECO:0000244|PDB:3DO7}. FT HELIX 276 278 {ECO:0000244|PDB:2V2T}. FT STRAND 279 281 {ECO:0000244|PDB:1ZKA}. FT STRAND 283 287 {ECO:0000244|PDB:1ZK9}. FT STRAND 289 292 {ECO:0000244|PDB:4JHB}. FT STRAND 297 299 {ECO:0000244|PDB:3DO7}. FT STRAND 301 304 {ECO:0000244|PDB:1ZK9}. FT HELIX 308 310 {ECO:0000244|PDB:1ZKA}. FT STRAND 314 317 {ECO:0000244|PDB:1ZK9}. FT STRAND 320 323 {ECO:0000244|PDB:1ZK9}. FT HELIX 328 330 {ECO:0000244|PDB:1ZK9}. FT TURN 333 335 {ECO:0000244|PDB:4JHB}. FT STRAND 336 340 {ECO:0000244|PDB:4JHB}. FT STRAND 353 357 {ECO:0000244|PDB:1ZK9}. FT TURN 362 364 {ECO:0000244|PDB:1ZK9}. FT STRAND 371 375 {ECO:0000244|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 //