PLCE1_CAEEL
ID PLCE1_CAEEL Reviewed; 1898 AA.
AC G5EFI8; G5ED55; G5EEI0; G5EEJ6; G5EFI5;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 {ECO:0000250|UniProtKB:Q9P212};
DE EC=3.1.4.11 {ECO:0000255|RuleBase:RU361133, ECO:0000269|PubMed:9497345};
DE AltName: Full=Phosphoinositide phospholipase C-epsilon plc-1 {ECO:0000305};
DE AltName: Full=Phosphoinositide-specific phospholipase PLC210 {ECO:0000303|PubMed:9497345};
DE AltName: Full=Phospholipase C-epsilon plc-1 {ECO:0000305};
DE Short=PLC-epsilon plc-1 {ECO:0000305};
GN Name=plc-1 {ECO:0000312|WormBase:F31B12.1a};
GN ORFNames=F31B12.1 {ECO:0000312|WormBase:F31B12.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC38963.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, INTERACTION WITH LET-60, AND DOMAIN.
RX PubMed=9497345; DOI=10.1074/jbc.273.11.6218;
RA Shibatohge M., Kariya K., Liao Y., Hu C.-D., Watari Y., Goshima M.,
RA Shima F., Kataoka T.;
RT "Identification of PLC210, a Caenorhabditis elegans phospholipase C, as a
RT putative effector of Ras.";
RL J. Biol. Chem. 273:6218-6222(1998).
RN [2] {ECO:0000312|EMBL:CAQ51495.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), 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 [3] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15355798; DOI=10.1016/j.ydbio.2004.06.024;
RA Kariya K., Bui Y.K., Gao X., Sternberg P.W., Kataoka T.;
RT "Phospholipase Cepsilon regulates ovulation in Caenorhabditis elegans.";
RL Dev. Biol. 274:201-210(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15194811; DOI=10.1091/mbc.e04-03-0198;
RA Yin X., Gower N.J., Baylis H.A., Strange K.;
RT "Inositol 1,4,5-trisphosphate signaling regulates rhythmic contractile
RT activity of myoepithelial sheath cells in Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:3938-3949(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23887678; DOI=10.1038/ncomms3210;
RA Kunitomo H., Sato H., Iwata R., Satoh Y., Ohno H., Yamada K., Iino Y.;
RT "Concentration memory-dependent synaptic plasticity of a taste circuit
RT regulates salt concentration chemotaxis in Caenorhabditis elegans.";
RL Nat. Commun. 4:2210-2210(2013).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=23671426; DOI=10.1371/journal.pgen.1003510;
RA Kovacevic I., Orozco J.M., Cram E.J.;
RT "Filamin and phospholipase C-epsilon are required for calcium signaling in
RT the Caenorhabditis elegans spermatheca.";
RL PLoS Genet. 9:E1003510-E1003510(2013).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27184844; DOI=10.1016/j.celrep.2016.04.052;
RA Najibi M., Labed S.A., Visvikis O., Irazoqui J.E.;
RT "An evolutionarily conserved PLC-PKD-TFEB pathway for host defense.";
RL Cell Rep. 15:1728-1742(2016).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes
CC (PubMed:9497345). plc-1 is a bifunctional enzyme which also regulates
CC small GTPases of the Ras superfamily through its Ras guanine-exchange
CC factor (RasGEF) activity (By similarity). By activating IP3 receptor
CC itr-1-mediated intracellular Ca(2+) release via the production of IP3,
CC regulates ovulation by controlling contraction and/or dilation of the
CC distal spermatheca valve during oocyte entry and the timing of the
CC dilation of the spermatheca-uterine valve during oocyte exit
CC (PubMed:23671426, PubMed:15355798, PubMed:18369461, PubMed:15194811).
CC In a similar manner, plays an essential role in epidermal morphogenesis
CC by regulating migration of epidermal cells during ventral closure and
CC to a lesser extent by regulating epidermal cell dorsal intercalation
CC (PubMed:18369461). Involved in the immune response to S.aureus
CC bacterium by activating kinase dkf-1 via the production of DAG which in
CC turn activates transcription factor hlh-30 (PubMed:27184844). In ASER
CC neurons, required for adjusting the orientation behavior in salt
CC gradients based on the memory of previous salt concentration
CC encountered (PubMed:23887678). {ECO:0000250|UniProtKB:Q9P212,
CC ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:15355798,
CC ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:23671426,
CC ECO:0000269|PubMed:23887678, ECO:0000269|PubMed:27184844,
CC ECO:0000269|PubMed:9497345}.
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:0000255|RuleBase:RU361133, ECO:0000269|PubMed:9497345};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9497345};
CC -!- SUBUNIT: Interacts (via Ras-associating domain 1) with let-60 (in GTP-
CC bound form). {ECO:0000269|PubMed:9497345}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000312|WormBase:F31B12.1a};
CC IsoId=G5EFI8-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F31B12.1b};
CC IsoId=G5EFI8-2; Sequence=VSP_058533, VSP_058534, VSP_058536,
CC VSP_058537;
CC Name=c {ECO:0000312|WormBase:F31B12.1c};
CC IsoId=G5EFI8-3; Sequence=VSP_058534, VSP_058535;
CC Name=d {ECO:0000312|WormBase:F31B12.1d};
CC IsoId=G5EFI8-4; Sequence=VSP_058531, VSP_058533, VSP_058534,
CC VSP_058536, VSP_058537;
CC Name=e {ECO:0000312|WormBase:F31B12.1e};
CC IsoId=G5EFI8-5; Sequence=VSP_058532, VSP_058533, VSP_058534,
CC VSP_058536, VSP_058537;
CC -!- TISSUE SPECIFICITY: Expressed in the spermatheca, vulva, intestine and
CC excretory cells (PubMed:15355798). Expressed in sensory neurons AWC,
CC AFD, ASE, ASG and BAG, interneurons, ventral nerve cord neurons and
CC tail neurons (PubMed:15355798, PubMed:23887678). Expressed in body
CC muscles (PubMed:23887678). {ECO:0000269|PubMed:15355798,
CC ECO:0000269|PubMed:23887678}.
CC -!- DOMAIN: Only Ras-associating 1 domain is involved in the binding to
CC let-60. {ECO:0000269|PubMed:9497345}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in 52 percent of
CC animals arrested at the embryonic stage (PubMed:18369461). RNAi-
CC mediated knockdown in larvae causes a severe decrease in brood size
CC (PubMed:15194811). In 20 percent of animals, spermatheca dilatation is
CC impaired causing oocyte retention in the gonad and persistent
CC triggering of ovulatory contractions (PubMed:15194811). In L4 larvae,
CC results in a shortened lifespan (PubMed:27184844). Prevents
CC transcription factor hlh-30 nuclear translocation and increases
CC lifespan in response to S.aureus infection (PubMed:27184844).
CC {ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:18369461,
CC ECO:0000269|PubMed:27184844}.
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DR EMBL; AF044576; AAC38963.1; -; mRNA.
DR EMBL; AM992255; CAQ51495.1; -; mRNA.
DR EMBL; BX284606; CAB60281.3; -; Genomic_DNA.
DR EMBL; BX284606; CAB60282.4; -; Genomic_DNA.
DR EMBL; BX284606; CAD44124.1; -; Genomic_DNA.
DR EMBL; BX284606; CAQ35039.1; -; Genomic_DNA.
DR EMBL; BX284606; CAQ58108.1; -; Genomic_DNA.
DR PIR; T42440; T42440.
DR RefSeq; NP_001024617.1; NM_001029446.2. [G5EFI8-1]
DR RefSeq; NP_001024619.1; NM_001029448.3. [G5EFI8-3]
DR RefSeq; NP_001123141.1; NM_001129669.2.
DR RefSeq; NP_001129926.1; NM_001136454.1. [G5EFI8-5]
DR RefSeq; NP_509805.3; NM_077404.5. [G5EFI8-2]
DR AlphaFoldDB; G5EFI8; -.
DR SMR; G5EFI8; -.
DR STRING; 6239.F31B12.1a; -.
DR PaxDb; G5EFI8; -.
DR EnsemblMetazoa; F31B12.1a.1; F31B12.1a.1; WBGene00004036. [G5EFI8-1]
DR EnsemblMetazoa; F31B12.1b.1; F31B12.1b.1; WBGene00004036. [G5EFI8-2]
DR EnsemblMetazoa; F31B12.1c.1; F31B12.1c.1; WBGene00004036. [G5EFI8-3]
DR EnsemblMetazoa; F31B12.1d.1; F31B12.1d.1; WBGene00004036.
DR EnsemblMetazoa; F31B12.1e.1; F31B12.1e.1; WBGene00004036. [G5EFI8-5]
DR GeneID; 181274; -.
DR KEGG; cel:CELE_F31B12.1; -.
DR CTD; 181274; -.
DR WormBase; F31B12.1a; CE28227; WBGene00004036; plc-1. [G5EFI8-1]
DR WormBase; F31B12.1b; CE31494; WBGene00004036; plc-1. [G5EFI8-2]
DR WormBase; F31B12.1c; CE31495; WBGene00004036; plc-1. [G5EFI8-3]
DR WormBase; F31B12.1d; CE42555; WBGene00004036; plc-1. [G5EFI8-4]
DR WormBase; F31B12.1e; CE42678; WBGene00004036; plc-1. [G5EFI8-5]
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000157356; -.
DR InParanoid; G5EFI8; -.
DR OMA; RCIRAGY; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; G5EFI8; -.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:G5EFI8; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004036; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; G5EFI8; baseline and differential.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:WormBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:1902634; P:1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate catabolic process; IDA:WormBase.
DR GO; GO:0002253; P:activation of immune response; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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; IPR028398; PLC-epsilon1.
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 InterPro; IPR000159; RA_dom.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF6; PTHR10336:SF6; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 2.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 2.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Guanine-nucleotide releasing factor;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..1898
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase epsilon-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437464"
FT DOMAIN 66..328
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 910..1058
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 1279..1385
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 1391..1517
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1570..1665
FT /note="Ras-associating 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 1738..1857
FT /note="Ras-associating 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 419..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1680..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 970
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT VAR_SEQ 1..26
FT /note="MNWDTLKGVLKTRRLTKRTIPAYIHP -> MTLWEIMQNSASNSIQRSLNQS
FT MHRSHTEATVS (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058531"
FT VAR_SEQ 565
FT /note="G -> GGRVERWKGFG (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058532"
FT VAR_SEQ 1727..1728
FT /note="Missing (in isoform b, isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058533"
FT VAR_SEQ 1802..1817
FT /note="SMLQALSLARKRSNDL -> M (in isoform b, isoform c,
FT isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058534"
FT VAR_SEQ 1866..1898
FT /note="EFHEMAKIIREGIPKKDETYYMIYYSGLPGEDI -> GRRVESTTSSSTTTR
FT KISLSSVRSIGLPRKFSKFGKSLTMDAGPK (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058535"
FT VAR_SEQ 1866..1885
FT /note="EFHEMAKIIREGIPKKDETY -> VRSFISKLEAAKASMDPRHE (in
FT isoform b, isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058536"
FT VAR_SEQ 1886..1898
FT /note="Missing (in isoform b, isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058537"
SQ SEQUENCE 1898 AA; 212879 MW; C10F8EBBF1D647DD CRC64;
MNWDTLKGVL KTRRLTKRTI PAYIHPTSRS DSTSSTQSAT AGFILNEEPI TLFRLELERL
QYILHFPEEV AFQLSSTEYQ LFYSIQPMDY VRYVSCDLTS VPVSENPSPV RNLVKRLSEV
SSWITHVIVS QPTHDDRKVA LTAILRIVET CWNIGNFNAA VEVLMGLKSE KLRPFWLSLR
QEEKSQFDSL CETLLPANQA LPSQAYINAV QRALRMPQSR VIPFFGIFLR DLYAIVNDLP
NIVVIGQEGE TQKLEFMSDP NGEDHFSSRI GVGGLLNADK INLVAIVLDN LELFHRHSRT
MIKLLEEQAV PPIQIPQNER EQKEKEAKTY EPVQVVRGSS HGVALIPLDT LTFDLDVIQR
LQHGTTVIHY EPDSGRSNLC LLRLDPSCGQ INWHKISYSV NKDPKEKDVL AKVSVSNLQP
LDSGRGAPSP MPSGRTPGTG GVGVEEGELK LSVVKGVELV DSYDIDIEAI YRRHSMEEMS
VPVSCWKVSH GQLLSDNEFI YFLAPQQIAQ FWTNGLQSVV KSLQGQQRYP DRRMLWIKNV
YLSLYEITGE SNCGPRPFEA LQAFGLSQTN TNATRPNDSS LSSEPGGAKS RLKNLKNAMQ
KKLRGASREG SRSQSPQPHS PLVRPPSIKS QISSQSGPPG PNSPGYLLKP RGEPANSDAG
DIDSIYTPRS RTPTSSSYGG RSVGGRSCKS WRSRGGETPN SGSISSSGQM SIQVSGLSGP
SGKEFQEKPL TLVEFAELFR LFNTRMRKDL RDVFNDVLST ATTPQHCPKR ERDRHSPRMQ
SRLASVSNSY NADFLSNDFL TRNTAVTSHH ISEKQNKIYN ALALASVNSM GGLMDTSRSS
MLTPQMLRAF VNTHQMEQID EQTAIKLIQD HEPDGICRQK NQMSFEGFTR FLCDPVNFAF
VPETIEPDEE DLRYPLSHYY INSSHNTYLT GHQLKGPSSS EMYRQVLLTG CRCVELDCWD
GDDGLPLIYH GHTLVSKIGF RQVVEIIKKS AFITSDLPVI LSIENHCSLQ QQAKMAQMFK
TVLGDLLVSN FLFEADFSDS PRLPCPLQMK NKILIKNKKM IVDPPTPLPM IERGAVQRGE
TQLNLHRKQS KNSYESSTVD EVEDDDLDEF LDDEENEEDD QEEVQVRSEK EDSPKTSKRA
EKSARNIKQQ DSLCSDHSVE QAKPSTSKTT SKTNDRKTED EVLYAQLAQN AIRNQQPRKN
NTGVQIAPEL SDIVIYMQAT KFKGFPPVDG IQSPRIMEEG PASASLSFSS RARTPSNLLN
TPAPPRRQRS STQLSQELAA EFLGSVRANA TATCYQVTSL NENAAKKLMK RHPAKCVSYT
RDHLIRTYPS AKHYDSSNFN PINCWAHGMQ MVALNFQTPD VIMAVNQAMF EQSGNCGYQL
KPRCLWDESH LLYNKFLPLS KDIAGHSALL LNLTIISGQH VYPNTHYASL YVEIEVIGIH
NDCVREKSKV VQRNSVNPIW NHTTQLRIAC VDLAFLRIAV CDSGQNGRVV AHRVVPVKCI
RPGFRHLPLR TPTNLPIDNA MIFLRTRFEQ EEHIYLHDDD SNTYCNLEHT LAYRTDLTPN
LSPTPILKKQ IFVLRITGAF ADETAITVHS ESGSTVKTVM QQALLNAGKN ADQVEEYVLI
EESLPAPSGE DPIEQRVLPL NEPIMDAVAC WNGSMRRFVL RKKGSDPSSR AWITSIIKSG
TSGSSTSVSP SPLTKDGHVK SASSNQLHGR SLDTDAFGEH LEVTEGKWLN PRARSMGDTF
LVCVHNVSED QPYAILRAGI HSTAADIIRQ VFVKARRSNV DDSEFVLVEE TCDDPKLNQG
QSMLQALSLA RKRSNDLTPK YPNNRTTSRV LGQNENVWKA QSRWKSMGRF VLENRKDTVH
ATLEKEFHEM AKIIREGIPK KDETYYMIYY SGLPGEDI
