PLCB_CAEEL
ID PLCB_CAEEL Reviewed; 1431 AA.
AC G5EBH0; Q6EZG7; Q95X30; Q9U6B9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8;
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q9QW07};
DE AltName: Full=Egg-laying defective protein 8;
DE AltName: Full=Phosphoinositide phospholipase C-beta egl-8;
DE AltName: Full=Phospholipase C-beta egl-8 {ECO:0000303|PubMed:10571228, ECO:0000312|EMBL:AAF05701.1};
DE Short=PLC-beta egl-8 {ECO:0000250|UniProtKB:Q9QW07, ECO:0000303|PubMed:10571228};
GN Name=egl-8 {ECO:0000312|EMBL:CCD61783.1, ECO:0000312|WormBase:B0348.4b};
GN ORFNames=B0348.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF05701.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAF05701.1};
RX PubMed=10571227; DOI=10.1016/s0896-6273(00)80847-8;
RA Miller K.G., Emerson M.D., Rand J.B.;
RT "Goalpha and diacylglycerol kinase negatively regulate the Gqalpha pathway
RT in C. elegans.";
RL Neuron 24:323-333(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF01458.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-45.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAF01458.1};
RX PubMed=10571228; DOI=10.1016/s0896-6273(00)80848-x;
RA Lackner M.R., Nurrish S.J., Kaplan J.M.;
RT "Facilitation of synaptic transmission by EGL-30 Gqalpha and EGL-8 PLCbeta:
RT DAG binding to UNC-13 is required to stimulate acetylcholine release.";
RL Neuron 24:335-346(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CCD61783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD61783.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15958491; DOI=10.1091/mbc.e05-02-0096;
RA Gower N.J., Walker D.S., Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signaling regulates mating behavior in
RT Caenorhabditis elegans males.";
RL Mol. Biol. Cell 16:3978-3986(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18369461; DOI=10.1371/journal.pgen.1000043;
RA Vazquez-Manrique R.P., Nagy A.I., Legg J.C., Bales O.A., Ly S.,
RA Baylis H.A.;
RT "Phospholipase C-epsilon regulates epidermal morphogenesis in
RT Caenorhabditis elegans.";
RL PLoS Genet. 4:E1000043-E1000043(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19380113; DOI=10.1016/j.chom.2009.03.006;
RA Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N.,
RA Ewbank J.J.;
RT "Antifungal innate immunity in C. elegans: PKCdelta links G protein
RT signaling and a conserved p38 MAPK cascade.";
RL Cell Host Microbe 5:341-352(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19730689; DOI=10.1371/journal.pgen.1000636;
RA Walker D.S., Vazquez-Manrique R.P., Gower N.J., Gregory E., Schafer W.R.,
RA Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signalling regulates the avoidance response
RT to nose touch in Caenorhabditis elegans.";
RL PLoS Genet. 5:E1000636-E1000636(2009).
RN [8]
RP FUNCTION.
RX PubMed=23072806; DOI=10.1038/ncomms2136;
RA Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
RA Hisamoto N.;
RT "Endocannabinoid-Goalpha signalling inhibits axon regeneration in
RT Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
RL Nat. Commun. 3:1136-1136(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:24212673};
RX PubMed=24212673; DOI=10.1038/nn.3575;
RA Peden A.S., Mac P., Fei Y.J., Castro C., Jiang G., Murfitt K.J.,
RA Miska E.A., Griffin J.L., Ganapathy V., Jorgensen E.M.;
RT "Betaine acts on a ligand-gated ion channel in the nervous system of the
RT nematode C. elegans.";
RL Nat. Neurosci. 16:1794-1801(2013).
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) which plays
CC an important role in the regulation of intracellular signaling cascades
CC (By similarity). Required in the nervous system to modulate neuronal
CC activity. Facilitates synaptic transmission at neuromuscular junctions
CC by regulating the release of acetylcholine from the motor neurons and
CC thus affecting locomotion (PubMed:10571228). Plays a role in efficient
CC egg laying and defecation (PubMed:10571227, PubMed:10571228,
CC PubMed:24212673). Involved in axon regeneration after injury
CC (PubMed:23072806). Plays a role in male mating behavior by regulating
CC spicule insertion and sperm transfer (PubMed:15958491). By triggering
CC Ca(2+) transient via IP3-mediated activation of IPR3 receptor itr-1 in
CC ASH sensory neurons, regulates avoidance behavior in response to nose
CC touch (PubMed:19730689). By activating tpa-1 via DAG production,
CC required for the expression of antimicrobial peptide nlp-29 in response
CC to fungal infection (PubMed:19380113). During embryogenesis, may play a
CC role in epidermal morphogenesis together with plc-1 (PubMed:18369461).
CC {ECO:0000250|UniProtKB:P10687, ECO:0000269|PubMed:10571227,
CC ECO:0000269|PubMed:10571228, ECO:0000269|PubMed:15958491,
CC ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:19380113,
CC ECO:0000269|PubMed:19730689, ECO:0000269|PubMed:23072806,
CC ECO:0000269|PubMed:24212673}.
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:0000250|UniProtKB:P10687};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P10688};
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:10571227}. Cell
CC projection, axon {ECO:0000269|PubMed:10571227}. Synapse
CC {ECO:0000269|PubMed:10571227}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:10571227}. Note=Present in neuronal cell somas and
CC axon processes of the nerve ring in head ganglia. Present in the
CC adherens junction of intestinal cells. {ECO:0000269|PubMed:10571227}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000269|PubMed:10571227};
CC IsoId=G5EBH0-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:10571228};
CC IsoId=G5EBH0-2; Sequence=VSP_053885;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=G5EBH0-3; Sequence=VSP_053882, VSP_053883, VSP_053884;
CC -!- TISSUE SPECIFICITY: Expressed in most or all neurons with high
CC expression in the head and tail ganglia and low expression in the motor
CC neurons of the ventral cord. Expressed in the intestine (at protein
CC level) (PubMed:10571227, PubMed:10571228). In males, expressed in vas
CC deferens, spicule protractor muscles, diagonal muscles and a male-
CC specific neuron (PubMed:15958491). {ECO:0000269|PubMed:10571227,
CC ECO:0000269|PubMed:10571228, ECO:0000269|PubMed:15958491}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms are similar in size to the wild-type
CC but animals are bloated with eggs due to defective egg laying with
CC decreased body flexion and sluggish locomotion (PubMed:10571227,
CC PubMed:10571228). They have defects in the posterior body contraction
CC step of the defecation motor program and become sluggish in the
CC presence of exogenous betaine (PubMed:24212673). Animals are resistant
CC to aldicarb, a carbamate insecticide (PubMed:10571228). Simultaneous
CC knockout of egl-8 and snf-3 results in uncoordinated, hypercontracted
CC and paralyzed animals (PubMed:24212673). RNAi-mediated knockdown causes
CC a defect in sperm transfer and a slight defect in spicule protrusion
CC resulting in male infertility (PubMed:15958491). Ca(2+) transient
CC increase and avoidance behavior are defective in response to nose touch
CC but not to benzaldehyde (PubMed:19730689). nlp-29 expression is
CC abrogated following fungal infection by D.coniospora but not following
CC physical injury (PubMed:19380113). Causes a 1.6 fold increase in
CC embryonic arrest in a plc-1 (tm753) mutant background
CC (PubMed:18369461). {ECO:0000269|PubMed:10571227,
CC ECO:0000269|PubMed:10571228, ECO:0000269|PubMed:15958491,
CC ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:19380113,
CC ECO:0000269|PubMed:19730689, ECO:0000269|PubMed:24212673}.
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DR EMBL; AF179426; AAF05701.1; -; mRNA.
DR EMBL; AF188477; AAF01458.1; -; mRNA.
DR EMBL; FO080176; CCD61782.1; -; Genomic_DNA.
DR EMBL; FO080176; CCD61783.1; -; Genomic_DNA.
DR EMBL; FO080176; CCD61784.1; -; Genomic_DNA.
DR PIR; T37264; T37264.
DR RefSeq; NP_001021346.1; NM_001026175.3. [G5EBH0-2]
DR RefSeq; NP_001021347.1; NM_001026176.2. [G5EBH0-1]
DR RefSeq; NP_001021348.1; NM_001026177.3. [G5EBH0-3]
DR AlphaFoldDB; G5EBH0; -.
DR SMR; G5EBH0; -.
DR BioGRID; 43612; 1.
DR STRING; 6239.B0348.4b; -.
DR EPD; G5EBH0; -.
DR PaxDb; G5EBH0; -.
DR PeptideAtlas; G5EBH0; -.
DR EnsemblMetazoa; B0348.4a.1; B0348.4a.1; WBGene00001177. [G5EBH0-2]
DR EnsemblMetazoa; B0348.4b.1; B0348.4b.1; WBGene00001177. [G5EBH0-1]
DR EnsemblMetazoa; B0348.4c.1; B0348.4c.1; WBGene00001177. [G5EBH0-3]
DR GeneID; 178537; -.
DR UCSC; B0348.4a; c. elegans.
DR CTD; 178537; -.
DR WormBase; B0348.4a; CE30588; WBGene00001177; egl-8. [G5EBH0-2]
DR WormBase; B0348.4b; CE30589; WBGene00001177; egl-8. [G5EBH0-1]
DR WormBase; B0348.4c; CE36909; WBGene00001177; egl-8. [G5EBH0-3]
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000156426; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR InParanoid; G5EBH0; -.
DR PhylomeDB; G5EBH0; -.
DR Reactome; R-CEL-112043; PLC beta mediated events.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR PRO; PR:G5EBH0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001177; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; G5EBH0; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IGI:WormBase.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:WormBase.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0035418; P:protein localization to synapse; IGI:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IGI:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0043052; P:thermotaxis; IGI:WormBase.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
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; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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 Alternative splicing; Calcium; Cell junction; Cell projection; Coiled coil;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Synapse; Transducer.
FT CHAIN 1..1431
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta egl-8"
FT /id="PRO_0000425864"
FT DOMAIN 340..491
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 758..874
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 877..1002
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 510..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1135..1166
FT /evidence="ECO:0000255"
FT COILED 1288..1318
FT /evidence="ECO:0000255"
FT COILED 1368..1402
FT /evidence="ECO:0000255"
FT COMPBIAS 556..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 403
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 787
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT BINDING 814
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10688"
FT VAR_SEQ 533..698
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053882"
FT VAR_SEQ 731..758
FT /note="PVLTKEEEERIFAEYHYTGATTNIHPLL -> ETNKISNFNIVFKGFLFLLI
FT LILLSQIP (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053883"
FT VAR_SEQ 759..1431
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053884"
FT VAR_SEQ 1167..1178
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10571228"
FT /id="VSP_053885"
FT MUTAGEN 45
FT /note="G->D: In n2659; egg laying and defecation defects,
FT and sluggish locomotion. Grows in the presence of aldicarb
FT unlike the wild-type."
FT /evidence="ECO:0000269|PubMed:10571228"
FT CONFLICT 147..149
FT /note="MKY -> I (in Ref. 2; AAF01458)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="A -> AA (in Ref. 2; AAF01458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1431 AA; 160904 MW; 02C827299787FF02 CRC64;
MAKEFQFNWK PTIIPELLHG SVFDRYDDES TCLELNAQVR IDENGFFLRW LIEGKDAVVL
DMGQIWEART GGLPKDGRIM FELEQRGASE TIAERTIWIT HGQDLVNVQS FFLVAESVEL
AKTCRAGIND ILKSSRIRHV CPTTQLMKYH TWLTMNVNER RKIPIKLIIK TFSSGKPEKM
VQKCLNDLGL GGDKYTPARV INRSMGKKFR NFYKCSRGRK RKEREELDVD ILTFEKFQRL
YNKICPRTEV QELFVKLSGQ KEYLTKERLI NFLNEEQRDP RLNEILFPFF DSQRIVALLK
KHENDIKYQE DGKMSGDGFL RFLMSDENPP VFLDRIEMFM DMDQPLCHYY INSSHNTYLT
GRQYGGKSSS EIYRQVLLSG CRCIELDCWD GTGENKGEPI ITHGKAMCTD VFFKDVLVQI
RDTAFARSDF PVVLSFENHC SKSNQLKMAK YCMDIFGDML LSKPFEDAPL DPGVSLPSPN
RLRKKILIKN KRLKTDIERH QLDQFLREGK LDEEDELNET PEVVGEDSVS PRSGGSGGTG
APEEVDDDTS DDDDDPSVQT SLNVMRTIPT VNTTSNNGSN RSARSSLDTP SPSGGSLMVP
DRATSTATSI KNAVLARSPN FSSLRQKLSF KRRQSPLAGD QRAHPEVEQP VSSSSPATPS
ISGPPPCATS SGSTSSITIT TTGCSTSSSG PSKHILGGEM PAKENDEAHP ELKQNFIAKN
LKGFGFSKKQ PVLTKEEEER IFAEYHYTGA TTNIHPLLSS LVNYTHPVKF SGFDVAEANN
LHFHMSSFSE STGLGYLKQS APEFVNYNKR QSSRIYPKGA RVDSSNFLPQ IFWNAGCQMV
SLNFQTPDVY MQLNMGKFEY NGGSGYLLKP DFLRRPDRTF DPFSESPVDG VIAAHCSVRV
ISGQFLSDRK IGTYVEVEMY GLPTDTIRKE HKTKVIPGNG LNPVYNEDPF VFRKVVLPEL
AVLRFAVYDE NGKQLGQRIL PLDGLQAGYR HISLRSDTNQ SFILSPVLFV QIVIKTYVPD
ELSGLVDALA DPRAFLSEQK KRQEALAHMG VDDSDIPDVP NTRNMALRHV KQPPRQNGSS
ADLLANNGQT GSARGDQTSS MASSTIRSPN EQPQPVAVDK FKVDPIEVDD LRRDKAFAKL
LKRFQKELDD LRKKHQKQRD SIQKQQPARR RNSSIAWIQT NVDKLITNNR RSTKKEKGSR
RSLTASVSSG CGSASGTVTV SVCSPSGASC SGYSTGGPST PVACNSDGTG SPATIGSPVP
QDLVNNDRVR SLVNTQTGEW SAMVRRHDEE EFELKKVQLK EQFDLLRKLM SEAQKNQMLA
LKLRLEAEGK DLKQTQTKKS MEDAKVIQLD KGIKTKAERD RRVKELNEKN LKMFVEERKR
LAMKAQKHEE QLTKRHLDQL EQLDKDFHKA LDAEVGNYKE EQLAAQPTSV V
