RELB_HUMAN
ID RELB_HUMAN Reviewed; 579 AA.
AC Q01201; Q6GTX7; Q9UEI7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Transcription factor RelB;
DE AltName: Full=I-Rel;
GN Name=RELB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=1577270; DOI=10.1101/gad.6.5.745;
RA Ruben S.M., Klement J.F., Maher M., Coleman T.A., Chen C.H., Rosen C.A.;
RT "I-Rel: a novel rel-related protein that inhibits NF-kappa B
RT transcriptional activity.";
RL Genes Dev. 6:745-760(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [5]
RP FUNCTION, AND IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX.
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 [6]
RP FUNCTION.
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 [7]
RP FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX, AND
RP IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
RX PubMed=7925301; DOI=10.1002/j.1460-2075.1994.tb06782.x;
RA Dobrzanski P., Ryseck R.P., Bravo R.;
RT "Differential interactions of Rel-NF-kappa B complexes with I kappa B alpha
RT determine pools of constitutive and inducible NF-kappa B activity.";
RL EMBO J. 13:4608-4616(1994).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION, AND INDUCTION BY NUPR1.
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 [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP FUNCTION, INVOLVEMENT IN IMD53, AND VARIANT IMD53 397-TYR--THR-579 DEL.
RX PubMed=26385063; DOI=10.1016/j.jaut.2015.09.001;
RA Sharfe N., Merico D., Karanxha A., Macdonald C., Dadi H., Ngan B.,
RA Herbrick J.A., Roifman C.M.;
RT "The effects of RelB deficiency on lymphocyte development and function.";
RL J. Autoimmun. 65:90-100(2015).
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. As a member of the
CC NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal
CC adenocarcinoma with remarkable resistance to cell stress, such as
CC starvation or gemcitabine treatment. 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
CC (PubMed:26385063). {ECO:0000269|PubMed:1732739,
CC ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:26385063,
CC ECO:0000269|PubMed:7925301, ECO:0000269|PubMed:8441398}.
CC -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component of the
CC NF-kappa-B RelB-p52 complex. Self-associates; the interaction seems to
CC be transient and may prevent degradation allowing for heterodimer
CC formation with p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and
CC NFKB2/p100. Interacts with NFKBID. Interacts with ARNTL/BMAL1 and the
CC interaction is enhanced in the presence of CLOCK (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q01201; Q8N668: COMMD1; NbExp=2; IntAct=EBI-357837, EBI-1550112;
CC Q01201; P49841: GSK3B; NbExp=4; IntAct=EBI-357837, EBI-373586;
CC Q01201; P19838: NFKB1; NbExp=5; IntAct=EBI-357837, EBI-300010;
CC Q01201; Q00653: NFKB2; NbExp=2; IntAct=EBI-357837, EBI-307326;
CC Q01201; Q04206-2: RELA; NbExp=2; IntAct=EBI-357837, EBI-289947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20873783}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:20873783}. Note=Colocalizes with NEK6 in the
CC centrosome.
CC -!- INDUCTION: Up-regulated by mitogens and NUPR1.
CC {ECO:0000269|PubMed:22565310}.
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:0000250}.
CC -!- DISEASE: Immunodeficiency 53 (IMD53) [MIM:617585]: An autosomal
CC recessive primary immunodeficiency apparent from early infancy and
CC resulting in recurrent infections, severe autoimmune skin disease
CC rheumatoid arthritis, and failure to thrive. Immunologic workup shows
CC increased CD4+/CD8+ ratio, impaired T-cell proliferative response to
CC multiple antigen, T-cell developmental and functional defects, and
CC impaired ability to produce specific immunoglobulins.
CC {ECO:0000269|PubMed:26385063}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- CAUTION: Was originally thought to inhibit the transcriptional activity
CC of nuclear factor NF-kappa-B. {ECO:0000305|PubMed:1577270}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RELBID324.html";
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DR EMBL; M83221; AAA36127.1; -; mRNA.
DR EMBL; AF043463; AAC82346.1; -; Genomic_DNA.
DR EMBL; AF043454; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043455; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043456; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043457; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043458; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043459; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043460; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043461; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; AF043462; AAC82346.1; JOINED; Genomic_DNA.
DR EMBL; DQ314887; ABC40746.1; -; Genomic_DNA.
DR EMBL; BC028013; AAH28013.1; -; mRNA.
DR CCDS; CCDS46110.1; -.
DR PIR; A42617; A42617.
DR RefSeq; NP_006500.2; NM_006509.3.
DR AlphaFoldDB; Q01201; -.
DR SMR; Q01201; -.
DR BioGRID; 111903; 72.
DR ComplexPortal; CPX-5831; NF-kappaB DNA-binding transcription factor complex, p52/RelB.
DR ComplexPortal; CPX-5833; NF-kappaB DNA-binding transcription factor complex, p50/RelB.
DR CORUM; Q01201; -.
DR DIP; DIP-27531N; -.
DR IntAct; Q01201; 45.
DR MINT; Q01201; -.
DR STRING; 9606.ENSP00000221452; -.
DR ChEMBL; CHEMBL4523273; -.
DR iPTMnet; Q01201; -.
DR PhosphoSitePlus; Q01201; -.
DR BioMuta; RELB; -.
DR DMDM; 92090634; -.
DR EPD; Q01201; -.
DR jPOST; Q01201; -.
DR MassIVE; Q01201; -.
DR MaxQB; Q01201; -.
DR PaxDb; Q01201; -.
DR PeptideAtlas; Q01201; -.
DR PRIDE; Q01201; -.
DR ProteomicsDB; 57938; -.
DR Antibodypedia; 3573; 684 antibodies from 43 providers.
DR DNASU; 5971; -.
DR Ensembl; ENST00000221452.13; ENSP00000221452.7; ENSG00000104856.14.
DR Ensembl; ENST00000625761.2; ENSP00000485826.1; ENSG00000104856.14.
DR GeneID; 5971; -.
DR KEGG; hsa:5971; -.
DR MANE-Select; ENST00000221452.13; ENSP00000221452.7; NM_006509.4; NP_006500.2.
DR UCSC; uc060zvi.1; human.
DR CTD; 5971; -.
DR DisGeNET; 5971; -.
DR GeneCards; RELB; -.
DR HGNC; HGNC:9956; RELB.
DR HPA; ENSG00000104856; Low tissue specificity.
DR MalaCards; RELB; -.
DR MIM; 604758; gene.
DR MIM; 617585; phenotype.
DR neXtProt; NX_Q01201; -.
DR OpenTargets; ENSG00000104856; -.
DR PharmGKB; PA34322; -.
DR VEuPathDB; HostDB:ENSG00000104856; -.
DR eggNOG; ENOG502QV8A; Eukaryota.
DR GeneTree; ENSGT00940000160230; -.
DR InParanoid; Q01201; -.
DR OMA; NQYREGA; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; Q01201; -.
DR TreeFam; TF325632; -.
DR PathwayCommons; Q01201; -.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR SignaLink; Q01201; -.
DR SIGNOR; Q01201; -.
DR BioGRID-ORCS; 5971; 19 hits in 1094 CRISPR screens.
DR ChiTaRS; RELB; human.
DR GeneWiki; RELB; -.
DR GenomeRNAi; 5971; -.
DR Pharos; Q01201; Tbio.
DR PRO; PR:Q01201; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q01201; protein.
DR Bgee; ENSG00000104856; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q01201; baseline and differential.
DR Genevisible; Q01201; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0071159; C:NF-kappaB complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0019882; P:antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS: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; IMP:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:CACAO.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
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; IEA:Ensembl.
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 Activator; Biological rhythms; Cytoplasm; Cytoskeleton; Disease variant;
KW DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..579
FT /note="Transcription factor RelB"
FT /id="PRO_0000205173"
FT DOMAIN 125..440
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..68
FT /note="Leucine-zipper"
FT MOTIF 433..438
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VARIANT 396
FT /note="T -> M (in dbSNP:rs2230682)"
FT /id="VAR_051782"
FT VARIANT 397..579
FT /note="Missing (in IMD53)"
FT /evidence="ECO:0000269|PubMed:26385063"
FT /id="VAR_079201"
FT CONFLICT 139
FT /note="R -> P (in Ref. 1; AAA36127)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="R -> A (in Ref. 1; AAA36127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 62134 MW; C2C61C2C8640513E CRC64;
MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS TDELEIIDEY
IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP PATPPPWGCP LGRLVSPAPG
PGPQPHLVIT EQPKQRGMRF RYECEGRSAG SILGESSTEA SKTLPAIELR DCGGLREVEV
TACLVWKDWP HRVHPHSLVG KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE
RKIQLGIDPY NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT
SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ ADVHRQIAIV
FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR DHDSYGVDKK RKRGMPDVLG
ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG
GPDLLDDGFA YDPTAPTLFT MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ
APGPGDGGTA SLVGSNMFPN HYREAAFGGG LLSPGPEAT
