IKKB_RAT
ID IKKB_RAT Reviewed; 757 AA.
AC Q9QY78;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta;
DE Short=I-kappa-B-kinase beta;
DE Short=IKK-B;
DE Short=IKK-beta;
DE Short=IkBKB;
DE EC=2.7.11.10;
DE AltName: Full=I-kappa-B kinase 2;
DE Short=IKK2;
DE AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta;
DE Short=NFKBIKB;
DE AltName: Full=Serine/threonine protein kinase IKBKB;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:O14920};
GN Name=Ikbkb; Synonyms=Ikkb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Y., Sun S., Ravid K.;
RT "IKK beta in megakaryocyte differentiation.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IKK PHOSPHORYLATION.
RX PubMed=9819420; DOI=10.1128/mcb.18.12.7336;
RA Nemoto S., DiDonato J.A., Lin A.;
RT "Coordinate regulation of IkappaB kinases by mitogen-activated protein
RT kinase kinase kinase 1 and NF-kappaB-inducing kinase.";
RL Mol. Cell. Biol. 18:7336-7343(1998).
RN [3]
RP INTERACTION WITH SQSTM1; PRKCI AND TRAF6.
RX PubMed=16079148; DOI=10.1074/jbc.c500237200;
RA Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T.,
RA Moscat J.;
RT "The p62 scaffold regulates nerve growth factor-induced NF-kappaB
RT activation by influencing TRAF6 polyubiquitination.";
RL J. Biol. Chem. 280:35625-35629(2005).
RN [4]
RP REVIEW.
RX PubMed=10712233; DOI=10.1152/ajpcell.2000.278.3.c451;
RA Jobin C., Sartor R.B.;
RT "The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation
RT and protection.";
RL Am. J. Physiol. 278:C451-C462(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP INTERACTION WITH AKAP13.
RX PubMed=23090968; DOI=10.1128/mcb.00887-12;
RA del Vescovo C.D., Cotecchia S., Diviani D.;
RT "A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
RT interleukin-6-mediated cardiomyocyte hypertrophy.";
RL Mol. Cell. Biol. 33:14-27(2013).
CC -!- FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B
CC signaling pathway which is activated by multiple stimuli such as
CC inflammatory cytokines, bacterial or viral products, DNA damages or
CC other cellular stresses. Acts as part of the canonical IKK complex in
CC the conventional pathway of NF-kappa-B activation and phosphorylates
CC inhibitors of NF-kappa-B on 2 critical serine residues. These
CC modifications allow polyubiquitination of the inhibitors and subsequent
CC degradation by the proteasome. In turn, free NF-kappa-B is translocated
CC into the nucleus and activates the transcription of hundreds of genes
CC involved in immune response, growth control, or protection against
CC apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates
CC several other components of the signaling pathway including NEMO/IKBKG,
CC NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1
CC and IKBKE. IKK-related kinase phosphorylations may prevent the
CC overproduction of inflammatory mediators since they exert a negative
CC regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-
CC dependent inactivation of this pro-apoptotic transcription factor. Also
CC phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within
CC the nucleus, acts as an adapter protein for NFKBIA degradation in UV-
CC induced NF-kappa-B activation (By similarity). Phosphorylates RIPK1 at
CC 'Ser-25' which represses its kinase activity and consequently prevents
CC TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates
CC the C-terminus of IRF5, stimulating IRF5 homodimerization and
CC translocation into the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O14920, ECO:0000250|UniProtKB:O88351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-
CC seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-
CC COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:O14920};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14920};
CC -!- SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex
CC consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-
CC beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The
CC IKK core complex seems to associate with regulatory or adapter proteins
CC to form a IKK-signalosome holo-complex. The IKK complex associates with
CC TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of
CC RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB,
CC IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of
CC CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14. Found in a membrane
CC raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (By
CC similarity). Interacts with SQSTM1 through PRKCZ or PRKCI
CC (PubMed:16079148). Forms an NGF-induced complex with IKBKB, PRKCI and
CC TRAF6 (PubMed:16079148). May interact with MAVS/IPS1. Interacts with
CC NALP2. Interacts with TICAM1. Interacts with FAF1; the interaction
CC disrupts the IKK complex formation. Interacts with ATM. Part of a
CC ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with
CC NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2.
CC Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB
CC phosphorylation and kinase activity. Interacts with PDPK1. Interacts
CC with EIF2AK2/PKR. The phosphorylated form interacts with PPM1A and
CC PPM1B. Interacts with ZNF268 isoform 2; the interaction is further
CC increased in a TNF-alpha-dependent manner. Interacts with IKBKE.
CC Interacts with NAA10, leading to NAA10 degradation. Interacts with
CC FOXO3. Interacts with ZC3H12A (By similarity). Interacts with AKAP13
CC (PubMed:23090968). Interacts with LRRC14; disrupts IKBKB-IKBKG
CC interaction preventing I-kappa-B-kinase (IKK) core complex formation
CC and leading to a decrease of IKBKB phosphorylation and NF-kappaB
CC activation (By similarity). Interacts with SASH1 (By similarity).
CC Interacts with ARFIP2 (By similarity). Interacts with FKBP5 (By
CC similarity). {ECO:0000250|UniProtKB:O14920,
CC ECO:0000250|UniProtKB:O88351, ECO:0000269|PubMed:16079148,
CC ECO:0000269|PubMed:23090968}.
CC -!- INTERACTION:
CC Q9QY78; O70377: Snap23; NbExp=2; IntAct=EBI-1812464, EBI-1573765;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14920}. Nucleus
CC {ECO:0000250|UniProtKB:O14920}. Membrane raft
CC {ECO:0000250|UniProtKB:O14920}. Note=Colocalized with DPP4 in membrane
CC rafts. {ECO:0000250|UniProtKB:O14920}.
CC -!- DOMAIN: The kinase domain is located in the N-terminal region. The
CC leucine zipper is important to allow homo- and hetero-dimerization. At
CC the C-terminal region is located the region responsible for the
CC interaction with NEMO/IKBKG (By similarity). {ECO:0000250}.
CC -!- PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181
CC by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances
CC activity. Once activated, autophosphorylates on the C-terminal serine
CC cluster; which decreases activity and prevents prolonged activation of
CC the inflammatory response. Phosphorylated by the IKK-related kinases
CC TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB
CC activity and NF-kappa-B-dependent gene transcription. Dephosphorylated
CC at Ser-177 and Ser-181 by PPM1A and PPM1B.
CC {ECO:0000250|UniProtKB:O14920}.
CC -!- PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads to
CC inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may not serve
CC as a monoubiquitination site. Ubiquitination on 'Ser-163' may modulate
CC phosphorylation on C-terminal serine residues.
CC {ECO:0000250|UniProtKB:O14920}.
CC -!- PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic
CC conditions results in activation of NF-kappa-B.
CC {ECO:0000250|UniProtKB:O14920}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. I-kappa-B kinase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF115282; AAF21978.1; -; mRNA.
DR RefSeq; NP_445807.2; NM_053355.2.
DR AlphaFoldDB; Q9QY78; -.
DR SMR; Q9QY78; -.
DR BioGRID; 249911; 2.
DR CORUM; Q9QY78; -.
DR IntAct; Q9QY78; 4.
DR STRING; 10116.ENSRNOP00000025851; -.
DR ChEMBL; CHEMBL4524001; -.
DR iPTMnet; Q9QY78; -.
DR PhosphoSitePlus; Q9QY78; -.
DR PaxDb; Q9QY78; -.
DR PRIDE; Q9QY78; -.
DR GeneID; 84351; -.
DR KEGG; rno:84351; -.
DR UCSC; RGD:621375; rat.
DR CTD; 3551; -.
DR RGD; 621375; Ikbkb.
DR eggNOG; KOG4250; Eukaryota.
DR InParanoid; Q9QY78; -.
DR OrthoDB; 1013139at2759; -.
DR PhylomeDB; Q9QY78; -.
DR BRENDA; 2.7.11.10; 5301.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-209543; p75NTR recruits signalling complexes.
DR Reactome; R-RNO-209560; NF-kB is activated and signals survival.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR Reactome; R-RNO-933542; TRAF6 mediated NF-kB activation.
DR Reactome; R-RNO-937039; IRAK1 recruits IKK complex.
DR Reactome; R-RNO-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR PRO; PR:Q9QY78; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0035631; C:CD40 receptor complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0008385; C:IkappaB kinase complex; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008384; F:IkappaB kinase activity; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:1990459; F:transferrin receptor binding; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:2001259; P:positive regulation of cation channel activity; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:RGD.
DR GO; GO:0061847; P:response to cholecystokinin; IDA:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR Gene3D; 1.20.1270.250; -; 1.
DR InterPro; IPR041185; IKBKB_SDD.
DR InterPro; IPR046375; IKBKB_SDD_sf.
DR InterPro; IPR022007; IKKbetaNEMObind.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF18397; IKBKB_SDD; 1.
DR Pfam; PF12179; IKKbetaNEMObind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01239; IKKbetaNEMObind; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydroxylation; Isopeptide bond; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..757
FT /note="Inhibitor of nuclear factor kappa-B kinase subunit
FT beta"
FT /id="PRO_0000086015"
FT DOMAIN 15..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 458..479
FT /note="Leucine-zipper"
FT REGION 682..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..742
FT /note="NEMO-binding"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 177
FT /note="Phosphoserine; by TBK1 and PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 179
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 181
FT /note="Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 191
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 670
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 675
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 682
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 689
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 692
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 697
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 705
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 733
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT MOD_RES 740
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14920"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14920"
SQ SEQUENCE 757 AA; 86866 MW; 3AFFE46A7DF91F9C CRC64;
MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQVTGEQ IAIKQCRQEL SPKNRDRWCL
EIQIMRRLNH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ GGDLRRYLNQ FENCCGLREG
AILTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEKRL IHKIIDLGYA KELDQGSLCT
SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE
VDIVVSEDLN GTVKFSSSSP FPNNLNSVLA ERLEKWLQLM LTWQPRQRGV DPQYGPNGCF
RALDDILNLK LVHILNMVTG TIHTYPVMED ESLQSLKTRI REDTGILETD QELLQEAGLV
LLPDKPATQC ISDSKTNEGL TLDMDLVFLF DNSKMSYETQ ITPRPQPESV SCVLQEPKRN
LSFFQMRKVW GQVWHSIQTL KEDCNRLQQG QRAAMMNLLR NNSCLSKMKN AMASTAQQLK
AKLDFFKTSI QIDLEKYREQ TEFGITSDKL LLAWREMEQA VEQCGRENDV KVLVERMMAL
QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQDM VRLLLQAIQS
FEKKVRVIYS QLSKTVVCKQ KALELLPKVE EVVRLMNEDE KTVVRLQEKR QKELWNLLKI
ACSKVRGPVS GSPDSMNVSR LSHPGHLMSQ PSSACDSLPD SDKKSEELVA EAHALCSRLE
SALQDTVKQQ DRSFTTLDWS WLQMEDEERC GLEQACD
