ID   PLCB1_RAT               Reviewed;        1216 AA.
AC   P10687;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 209.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000269|PubMed:8454637};
DE   AltName: Full=PLC-154;
DE   AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE   AltName: Full=Phospholipase C-I;
DE            Short=PLC-I;
DE   AltName: Full=Phospholipase C-beta-1;
DE            Short=PLC-beta-1;
GN   Name=Plcb1 {ECO:0000312|RGD:3344};
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].
RX   PubMed=3390863; DOI=10.1016/0092-8674(88)90548-x;
RA   Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
RT   "Cloning and sequence of multiple forms of phospholipase C.";
RL   Cell 54:161-169(1988).
RN   [2]
RP   CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=8454637; DOI=10.1016/s0021-9258(18)53300-7;
RA   Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J., Rhee S.G.;
RT   "Cloning, sequencing, purification, and Gq-dependent activation of
RT   phospholipase C-beta 3.";
RL   J. Biol. Chem. 268:6654-6661(1993).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-1197; SER-1199 AND
RP   SER-1200, AND IDENTIFICATION BY 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).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-
CC       bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate
CC       (IP3) and mediates intracellular signaling downstream of G protein-
CC       coupled receptors. Regulates the function of the endothelial barrier.
CC       {ECO:0000250|UniProtKB:Q9Z1B3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000269|PubMed:8454637};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000305|PubMed:8454637};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC         1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC         Evidence={ECO:0000269|PubMed:8454637};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000305|PubMed:8454637};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- SUBUNIT: Interacts with DGKQ. {ECO:0000250|UniProtKB:Q9NQ66}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm
CC       {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic
CC       receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac
CC       myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
CC   -!- TISSUE SPECIFICITY: Highest expression in brain. Also expressed in
CC       parotid gland, liver, uterus, lung, heart, adrenal gland and ovary. Not
CC       detected in spleen, pancreas, intestine, thymus or kidney.
CC       {ECO:0000269|PubMed:8454637}.
CC   -!- PTM: Palmitoylated. Palmitoylation at Cys-17 by ZDHHC21 regulates the
CC       signaling activity of PLCB1 and the function of the endothelial
CC       barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation.
CC       {ECO:0000250|UniProtKB:Q9Z1B3}.
CC   -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC       mediated by two G protein alpha subunits, alpha-Q and alpha-11.
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DR   EMBL; M20636; AAA41885.1; -; mRNA.
DR   PIR; A28821; A28821.
DR   RefSeq; NP_001071109.1; NM_001077641.2.
DR   AlphaFoldDB; P10687; -.
DR   SMR; P10687; -.
DR   BioGRID; 246789; 163.
DR   CORUM; P10687; -.
DR   FunCoup; P10687; 3316.
DR   IntAct; P10687; 4.
DR   MINT; P10687; -.
DR   STRING; 10116.ENSRNOP00000006389; -.
DR   BindingDB; P10687; -.
DR   SwissLipids; SLP:000000946; -.
DR   GlyGen; P10687; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P10687; -.
DR   PhosphoSitePlus; P10687; -.
DR   SwissPalm; P10687; -.
DR   PaxDb; 10116-ENSRNOP00000006389; -.
DR   Ensembl; ENSRNOT00000006389.8; ENSRNOP00000006389.7; ENSRNOG00000004810.10.
DR   Ensembl; ENSRNOT00055039612; ENSRNOP00055032162; ENSRNOG00055022915.
DR   Ensembl; ENSRNOT00060003760; ENSRNOP00060002619; ENSRNOG00060002294.
DR   Ensembl; ENSRNOT00065021680; ENSRNOP00065016793; ENSRNOG00065013076.
DR   GeneID; 24654; -.
DR   KEGG; rno:24654; -.
DR   UCSC; RGD:3344; rat.
DR   AGR; RGD:3344; -.
DR   CTD; 23236; -.
DR   RGD; 3344; Plcb1.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000155428; -.
DR   InParanoid; P10687; -.
DR   OMA; PIVFKKX; -.
DR   OrthoDB; 269822at2759; -.
DR   PhylomeDB; P10687; -.
DR   BRENDA; 3.1.4.11; 5301.
DR   BRENDA; 3.1.4.3; 5301.
DR   Reactome; R-RNO-112043; PLC beta mediated events.
DR   Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   SABIO-RK; P10687; -.
DR   PRO; PR:P10687; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   ExpressionAtlas; P10687; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR   GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR   GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR   GO; GO:0005521; F:lamin binding; ISO:RGD.
DR   GO; GO:0120548; F:phosphatidylinositol phospholipase C activity; EXP:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR   GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; IDA:RGD.
DR   GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
DR   GO; GO:1902618; P:cellular response to fluoride; IDA:RGD.
DR   GO; GO:1905631; P:cellular response to glyceraldehyde; IDA:RGD.
DR   GO; GO:1904637; P:cellular response to ionomycin; IDA:RGD.
DR   GO; GO:1904117; P:cellular response to vasopressin; IDA:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
DR   GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR   GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0007612; P:learning; IEP:RGD.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0007613; P:memory; IEP:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:BHF-UCL.
DR   GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
DR   GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEP:RGD.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR   GO; GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:BHF-UCL.
DR   GO; GO:0040019; P:positive regulation of embryonic development; ISO:RGD.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
DR   GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISS:BHF-UCL.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR   GO; GO:0080154; P:regulation of fertilization; ISO:RGD.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISO:RGD.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0034284; P:response to monosaccharide; IDA:BHF-UCL.
DR   GO; GO:0043434; P:response to peptide hormone; IDA:BHF-UCL.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16208; EFh_PI-PLCbeta1; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08591; PI-PLCc_beta; 1.
DR   FunFam; 1.10.238.10:FF:000048; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 1.20.1230.10:FF:000001; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.30.29.240:FF:000004; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.60.40.150:FF:000008; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 3.20.20.190:FF:000039; Phosphoinositide phospholipase C; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR028400; PLC-beta1_EF.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR053945; PLCB1-4-like_EFh.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF12; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-1; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF17787; PH_14; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   Pfam; PF22631; PLCB1-4-like_EFh; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
KW   Reference proteome; Transducer.
FT   CHAIN           1..1216
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-1"
FT                   /id="PRO_0000088488"
FT   DOMAIN          316..467
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          540..656
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          656..784
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          469..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1072..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..501
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..979
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         582
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         887
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P10894"
FT   MOD_RES         978
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         1197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   LIPID           17
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
SQ   SEQUENCE   1216 AA;  138344 MW;  92F23691781F788E CRC64;
     MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
     TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV
     AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
     DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
     TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
     GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
     ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
     QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
     KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
     SNLVNYIQPV KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
     GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
     HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
     NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
     NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
     EADPGETSSE APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
     VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL
     RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
     QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
     TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
     KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS
     EEVQGENAGR EFDTPL
//