ID KPCB_BOVIN Reviewed; 671 AA. AC P05126; A5D7N0; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 27-MAR-2024, entry version 219. DE RecName: Full=Protein kinase C beta type; DE Short=PKC-B; DE Short=PKC-beta; DE EC=2.7.11.13; GN Name=PRKCB; Synonyms=PRKCB1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II). RX PubMed=3755548; DOI=10.1126/science.3755548; RA Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., RA Waterfield M.D., Francke U., Ullrich A.; RT "Multiple, distinct forms of bovine and human protein kinase C suggest RT diversity in cellular signaling pathways."; RL Science 233:859-866(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-I). RC STRAIN=Hereford; TISSUE=Fetal pons; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP REVIEW. RX PubMed=3045562; DOI=10.1038/334661a0; RA Nishizuka Y.; RT "The molecular heterogeneity of protein kinase C and its implications for RT cellular regulation."; RL Nature 334:661-665(1988). CC -!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)- CC dependent serine/threonine-protein kinase involved in various cellular CC processes such as regulation of the B-cell receptor (BCR) signalosome, CC oxidative stress-induced apoptosis, androgen receptor-dependent CC transcription regulation, insulin signaling and endothelial cells CC proliferation. Plays a key role in B-cell activation by regulating BCR- CC induced NF-kappa-B activation. Mediates the activation of the canonical CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 CC at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CC CARD11/CARMA1 association with lipid rafts and recruitment of the CC BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK CC complex, resulting in nuclear translocation and activation of NFKB1. CC Plays a direct role in the negative feedback regulation of the BCR CC signaling, by down-modulating BTK function via direct phosphorylation CC of BTK at 'Ser-180', which results in the alteration of BTK plasma CC membrane localization and in turn inhibition of BTK activity. Involved CC in apoptosis following oxidative damage: in case of oxidative CC conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of CC SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc CC acts as a reactive oxygen species producer. Acts as a coactivator of CC androgen receptor (ANDR)-dependent transcription, by being recruited to CC ANDR target genes and specifically mediating phosphorylation of 'Thr-6' CC of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional CC activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) CC by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in CC muscle cells and mediate insulin-dependent DNA synthesis through the CC RAF1-MAPK/ERK signaling cascade. Participates in the regulation of CC glucose transport in adipocytes by negatively modulating the insulin- CC stimulated translocation of the glucose transporter SLC2A4/GLUT4. CC Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1. CC Under high glucose in pancreatic beta-cells, is probably involved in CC the inhibition of the insulin gene transcription, via regulation of MYC CC expression. In endothelial cells, activation of PRKCB induces increased CC phosphorylation of RB1, increased VEGFA-induced cell proliferation, and CC inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) CC regulation by insulin, which causes endothelial dysfunction. Also CC involved in triglyceride homeostasis. Phosphorylates ATF2 which CC promotes cooperation between ATF2 and JUN, activating transcription (By CC similarity). Phosphorylates KLHL3 in response to angiotensin II CC signaling, decreasing the interaction between KLHL3 and WNK4 (By CC similarity). {ECO:0000250|UniProtKB:P05771, CC ECO:0000250|UniProtKB:P68404}. 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=2.7.11.13; 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=2.7.11.13; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 CC domain. {ECO:0000250|UniProtKB:P68403}; CC -!- ACTIVITY REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB and CC PRKCG) are activated by calcium and diacylglycerol (DAG) in the CC presence of phosphatidylserine. Three specific sites; Thr-500 CC (activation loop of the kinase domain), Thr-642 (turn motif) and Ser- CC 661 (hydrophobic region), need to be phosphorylated for its full CC activation. Specifically inhibited by enzastaurin (LY317615) (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with PDK1. Interacts in vitro with PRKCBP1. CC Interacts with PHLPP1 and PHLPP2; both proteins mediate its CC dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta-I; Synonyms=PRKCB1; CC IsoId=P05126-1; Sequence=Displayed; CC Name=Beta-II; Synonyms=PRKCB2; CC IsoId=P05126-2; Sequence=VSP_039222; CC -!- PTM: Phosphorylation on Thr-500 within the activation loop renders it CC competent to autophosphorylate. Subsequent autophosphorylation of Thr- CC 642 maintains catalytic competence, and autophosphorylation on Ser-661 CC appears to release the kinase into the cytosol. Autophosphorylation on CC other sites i.e. in the N-terminal and hinge regions have no effect on CC enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with CC GRB2 and contributes to the activation of MAPK/ERK signaling cascade CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. {ECO:0000305}. 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; M13974; AAA30703.1; -; mRNA. DR EMBL; BC140620; AAI40621.1; -; mRNA. DR PIR; A24664; KIBOC2. DR RefSeq; NP_777012.1; NM_174587.1. DR RefSeq; XP_005224747.1; XM_005224690.3. [P05126-1] DR AlphaFoldDB; P05126; -. DR SMR; P05126; -. DR BioGRID; 159587; 1. DR STRING; 9913.ENSBTAP00000027870; -. DR PaxDb; 9913-ENSBTAP00000027870; -. DR Ensembl; ENSBTAT00000027870.5; ENSBTAP00000027870.4; ENSBTAG00000020921.6. [P05126-2] DR Ensembl; ENSBTAT00000084339.1; ENSBTAP00000065659.1; ENSBTAG00000020921.6. [P05126-1] DR GeneID; 282325; -. DR KEGG; bta:282325; -. DR CTD; 5579; -. DR VEuPathDB; HostDB:ENSBTAG00000020921; -. DR eggNOG; KOG0696; Eukaryota. DR GeneTree; ENSGT00940000155217; -. DR HOGENOM; CLU_000288_54_2_1; -. DR InParanoid; P05126; -. DR OMA; VVXQLKE; -. DR OrthoDB; 841660at2759; -. DR TreeFam; TF351133; -. DR BRENDA; 2.7.11.13; 908. DR Reactome; R-BTA-114516; Disinhibition of SNARE formation. DR Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-BTA-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-BTA-4419969; Depolymerization of the Nuclear Lamina. DR Reactome; R-BTA-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-BTA-5218921; VEGFR2 mediated cell proliferation. DR Reactome; R-BTA-5668599; RHO GTPases Activate NADPH Oxidases. DR Reactome; R-BTA-76005; Response to elevated platelet cytosolic Ca2+. DR Proteomes; UP000009136; Chromosome 25. DR Bgee; ENSBTAG00000020921; Expressed in occipital lobe and 104 other cell types or tissues. DR ExpressionAtlas; P05126; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0042393; F:histone binding; ISS:UniProtKB. DR GO; GO:0035403; F:histone H3T6 kinase activity; ISS:UniProtKB. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:UniProtKB. DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB. DR GO; GO:0010827; P:regulation of glucose transmembrane transport; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR CDD; cd20833; C1_cPKC_rpt1; 1. DR CDD; cd20836; C1_cPKC_rpt2; 1. DR CDD; cd04026; C2_PKC_alpha_gamma; 1. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR020454; DAG/PE-bd. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014375; Protein_kinase_C_a/b/g. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24356:SF158; PROTEIN KINASE C BETA TYPE; 1. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00168; C2; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000550; PKC_alpha; 1. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00008; DAGPEDOMAIN. DR SMART; SM00109; C1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 2. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. PE 2: Evidence at transcript level; KW Acetylation; Adaptive immunity; Alternative splicing; Apoptosis; KW ATP-binding; Calcium; Chromatin regulator; Cytoplasm; Immunity; Kinase; KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; KW Transcription regulation; Transferase; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P05771" FT CHAIN 2..671 FT /note="Protein kinase C beta type" FT /id="PRO_0000055683" FT DOMAIN 158..275 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 342..600 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 601..671 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT ZN_FING 36..86 FT /note="Phorbol-ester/DAG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ZN_FING 101..151 FT /note="Phorbol-ester/DAG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT REGION 309..330 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 614..635 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 614..633 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 466 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 247 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P68403" FT BINDING 348..356 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 371 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 16 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P68403, ECO:0000255" FT MOD_RES 17 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P68403, ECO:0000255" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 250 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 324 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P68403, ECO:0000255" FT MOD_RES 500 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 504 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 635 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P68403" FT MOD_RES 642 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P68403" FT MOD_RES 661 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P05771" FT MOD_RES 662 FT /note="Phosphotyrosine; by SYK" FT /evidence="ECO:0000250|UniProtKB:P68404" FT VAR_SEQ 622..671 FT /note="RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV FT -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS (in FT isoform Beta-II)" FT /evidence="ECO:0000303|PubMed:3755548" FT /id="VSP_039222" FT CONFLICT 576 FT /note="M -> I (in Ref. 2; AAA30703)" FT /evidence="ECO:0000305" SQ SEQUENCE 671 AA; 76790 MW; 1F31D6A9D3C4C61F CRC64; MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIER EVLIVVVRDA KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE LRQKFERAKI GPGPKTPEEK TTNTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF SYTNPEFVIN V //