PIPA_DROME
ID PIPA_DROME Reviewed; 1095 AA.
AC P13217; A4V3Y2; Q59E70; Q86P93; Q9U4G4; Q9W4K9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 4.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q9P212};
DE AltName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta {ECO:0000303|PubMed:25639794, ECO:0000312|FlyBase:FBgn0262738};
DE AltName: Full=No receptor potential A protein {ECO:0000303|PubMed:2457447};
DE AltName: Full=Phosphoinositide phospholipase C {ECO:0000305};
DE AltName: Full=Phosphoinositide phospholipase C-beta {ECO:0000305};
GN Name=norpA {ECO:0000312|FlyBase:FBgn0262738};
GN Synonyms=PLC-beta {ECO:0000303|PubMed:25639794,
GN ECO:0000312|FlyBase:FBgn0262738};
GN ORFNames=CG3620 {ECO:0000312|FlyBase:FBgn0262738};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=2457447; DOI=10.1016/s0092-8674(88)80017-5;
RA Bloomquist B.T., Shortridge R.D., Schneuwly S., Perdew M.H., Montell C.,
RA Steller H., Rubin G., Pak W.L.;
RT "Isolation of a putative phospholipase C gene of Drosophila, norpA, and its
RT role in phototransduction.";
RL Cell 54:723-733(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1089-1095 IN A COMPLEX WITH INAD.
RX PubMed=11500369; DOI=10.1093/emboj/20.16.4414;
RA Kimple M.E., Siderovski D.P., Sondek J.;
RT "Functional relevance of the disulfide-linked complex of the N-terminal PDZ
RT domain of InaD with NorpA.";
RL EMBO J. 20:4414-4422(2001).
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 (By
CC similarity). Essential component of the phototransduction pathway
CC (PubMed:2457447). Essential downstream component of a hh-signaling
CC pathway which regulates the Duox-dependent gut immune response to
CC bacterial uracil; required for the activation of Cad99C and
CC consequently Cad99C-dependent endosome formation, which is essential
CC for the Duox-dependent production of reactive oxygen species (ROS) in
CC response to intestinal bacterial infection (PubMed:25639794).
CC {ECO:0000250|UniProtKB:Q9P212, ECO:0000269|PubMed:2457447,
CC ECO:0000269|PubMed:25639794}.
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:Q9P212};
CC -!- SUBUNIT: Interacts with inaD. {ECO:0000269|PubMed:11500369}.
CC -!- INTERACTION:
CC P13217; Q24008: inaD; NbExp=4; IntAct=EBI-101510, EBI-195326;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B;
CC IsoId=P13217-1; Sequence=Displayed;
CC Name=C; Synonyms=D;
CC IsoId=P13217-2; Sequence=VSP_034088;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the adult retina.
CC {ECO:0000269|PubMed:2457447}.
CC -!- DISRUPTION PHENOTYPE: Flies have no photoreceptor potential, their eyes
CC lack phospholipase C (PLC) activity and they are completely blind.
CC {ECO:0000269|PubMed:2457447}.
CC -!- CAUTION: 3D structural studies were performed with a synthetic
CC heptapeptide that contained Cys, corresponding to position 1094,
CC therefore the detected disulfide bridge is an artifact.
CC {ECO:0000305|PubMed:11500369}.
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DR EMBL; J03138; AAA28724.1; -; mRNA.
DR EMBL; AE014298; AAF45942.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09121.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52474.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52475.1; -; Genomic_DNA.
DR EMBL; AF181641; AAD55427.1; -; mRNA.
DR EMBL; BT003293; AAO25053.1; -; mRNA.
DR PIR; A31225; A31225.
DR RefSeq; NP_001014720.1; NM_001014720.2. [P13217-2]
DR RefSeq; NP_001014721.1; NM_001014721.3. [P13217-2]
DR RefSeq; NP_001162661.1; NM_001169190.2. [P13217-1]
DR RefSeq; NP_001284860.1; NM_001297931.1. [P13217-2]
DR RefSeq; NP_525069.2; NM_080330.4. [P13217-1]
DR RefSeq; NP_726925.1; NM_167008.2. [P13217-1]
DR PDB; 1IHJ; X-ray; 1.80 A; A/B=211-214.
DR PDB; 6IRB; X-ray; 2.66 A; A/B=863-1074.
DR PDB; 6IRC; X-ray; 3.54 A; A=863-1095.
DR PDB; 6IRE; X-ray; 3.25 A; A=863-1095.
DR PDBsum; 1IHJ; -.
DR PDBsum; 6IRB; -.
DR PDBsum; 6IRC; -.
DR PDBsum; 6IRE; -.
DR AlphaFoldDB; P13217; -.
DR SMR; P13217; -.
DR BioGRID; 57893; 34.
DR DIP; DIP-45N; -.
DR IntAct; P13217; 8.
DR MINT; P13217; -.
DR STRING; 7227.FBpp0070618; -.
DR PaxDb; P13217; -.
DR EnsemblMetazoa; FBtr0070650; FBpp0070618; FBgn0262738. [P13217-1]
DR EnsemblMetazoa; FBtr0070651; FBpp0070619; FBgn0262738. [P13217-1]
DR EnsemblMetazoa; FBtr0100670; FBpp0100136; FBgn0262738. [P13217-2]
DR EnsemblMetazoa; FBtr0100671; FBpp0100137; FBgn0262738. [P13217-2]
DR EnsemblMetazoa; FBtr0301475; FBpp0290690; FBgn0262738. [P13217-1]
DR EnsemblMetazoa; FBtr0343599; FBpp0310196; FBgn0262738. [P13217-2]
DR GeneID; 31376; -.
DR KEGG; dme:Dmel_CG3620; -.
DR CTD; 31376; -.
DR FlyBase; FBgn0262738; norpA.
DR VEuPathDB; VectorBase:FBgn0262738; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000156426; -.
DR InParanoid; P13217; -.
DR OMA; FKICPRN; -.
DR PhylomeDB; P13217; -.
DR Reactome; R-DME-112043; PLC beta mediated events.
DR Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 31376; 0 hits in 3 CRISPR screens.
DR ChiTaRS; norpA; fly.
DR EvolutionaryTrace; P13217; -.
DR GenomeRNAi; 31376; -.
DR PRO; PR:P13217; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0262738; Expressed in oviduct (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P13217; baseline and differential.
DR Genevisible; P13217; DM.
DR GO; GO:0016027; C:inaD signaling complex; IPI:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IMP:FlyBase.
DR GO; GO:0004629; F:phospholipase C activity; TAS:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:FlyBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IGI:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IDA:FlyBase.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IMP:FlyBase.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:FlyBase.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IGI:FlyBase.
DR GO; GO:0008377; P:light-induced release of internally sequestered calcium ion; TAS:FlyBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:FlyBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; TAS:FlyBase.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; TAS:FlyBase.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; -; 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; 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; PF00168; C2; 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 3D-structure; Alternative splicing; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Sensory transduction; Transducer;
KW Vision.
FT CHAIN 1..1095
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase"
FT /id="PRO_0000088510"
FT DOMAIN 319..469
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 550..666
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 666..794
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 487..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 130..154
FT /note="SWQKNLRLITHNNRATNVCPRVNLM -> IWLDGIRKITHNVKANNICPMMC
FT LR (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_034088"
FT CONFLICT 446
FT /note="H -> R (in Ref. 1; AAA28724)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="D -> G (in Ref. 5; AAO25053)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094
FT /note="Y -> C (in Ref. 1; AAA28724)"
FT /evidence="ECO:0000305"
FT HELIX 873..877
FT /evidence="ECO:0007829|PDB:6IRB"
FT HELIX 880..1012
FT /evidence="ECO:0007829|PDB:6IRB"
FT HELIX 1020..1073
FT /evidence="ECO:0007829|PDB:6IRB"
FT TURN 1086..1088
FT /evidence="ECO:0007829|PDB:6IRE"
FT HELIX 1089..1091
FT /evidence="ECO:0007829|PDB:6IRE"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:6IRE"
SQ SEQUENCE 1095 AA; 124863 MW; CC712ABF9B065BB6 CRC64;
MTKKYEFDWI IPVPPELTTG CVFDRWFENE KETKENDFER DALFKVDEYG FFLYWKSEGR
DGDVIELCQV SDIRAGGTPK DPKILDKVTK KNGTNIPELD KRSLTICSNT DYINITYHHV
ICPDAATAKS WQKNLRLITH NNRATNVCPR VNLMKHWMRL SYCVEKSGKI PVKTLAKTFA
SGKTEKLVYT CIKDAGLPDD KNATMTKEQF TFDKFYALYH KVCPRNDIEE LFTSITKGKQ
DFISLEQFIQ FMNDKQRDPR MNEILYPLYE EKRCTEIIND YELDEEKKKN VQMSLDGFKR
YLMSDENAPV FLDRLDFYME MDQPLAHYYI NSSHNTYLSG RQIGGKSSVE MYRQTLLAGC
RCVELDCWNG KGEDEEPIVT HGHAYCTEIL FKDCIQAIAD CAFVSSEYPV ILSFENHCNR
AQQYKLAKYC DDFFGDLLLK EPLPDHPLDP GLPLPPPCKL KRKILIKNKR MKPEVEKVEL
ELWLKGELKT DDDPEEDASA GKPPEAAAAP APAPEAAAAA EGAAEGGGGA EAEAAAANYS
GSTTNVHPWL SSMVNYAQPI KFQGFDKAIE KNIAHNMSSF AESAGMNYLK QSSIDFVNYN
KRQMSRIYPK GTRADSSNYM PQVFWNAGCQ MVSLNFQSSD LPMQLNQGKF EYNGGCGYLL
KPDFMRRADK DFDPFADAPV DGVIAAQCSV KVIAGQFLSD KKVGTYVEVD MFGLPSDTVK
KEFRTRLVAN NGLNPVYNED PFVFRKVVLP DLAVLRFGVY EESGKILGQR ILPLDGLQAG
YRHVSLRTEA NFPMSLPMLF VNIELKIYVP DGFEDFMAML SDPRGFAGAA KQQNEQMKAL
GIEEQSGGAA RDAGKAKEEE KKEPPLVFEP VTLESLRQEK GFQKVGKKQI KELDTLRKKH
AKERTSVQKT QNAAIDKLIK GKSKDDIRND ANIKNSINDQ TKQWTDMIAR HRKEEWDMLR
QHVQDSQDAM KALMLTVQAA QIKQLEDRHA RDIKDLNAKQ AKMSADTAKE VQNDKTLKTK
NEKDRRLREK RQNNVKRFME EKKQIGVKQG RAMEKLKLAH SKQIEEFSTD VQKLMDMYKI
EEEAYKTQGK TEFYA
