ID PRIC1_DROME Reviewed; 1299 AA. AC A1Z6W3; A1Z6V4; A1Z6V8; Q9N9H6; Q9U5X0; Q9U5X1; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 24-JAN-2024, entry version 122. DE RecName: Full=Protein prickle; DE AltName: Full=Protein spiny legs; GN Name=pk {ECO:0000312|EMBL:AAF59281.2}; ORFNames=CG11084; 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] {ECO:0000305, ECO:0000312|EMBL:CAB57345.3} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=DP CN BW; TISSUE=Embryo {ECO:0000269|PubMed:10485852}; RX PubMed=10485852; DOI=10.1101/gad.13.17.2315; RA Gubb D., Green C., Huen D., Coulson D., Johnson G., Tree D.R.P., RA Collier S., Roote J.; RT "The balance between isoforms of the prickle LIM domain protein is critical RT for planar polarity in Drosophila imaginal discs."; RL Genes Dev. 13:2315-2327(1999). RN [2] {ECO:0000312|EMBL:AAF59281.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132}; 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] {ECO:0000305, ECO:0000312|EMBL:AAF59281.2} 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] {ECO:0000305} RP FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DISRUPTION PHENOTYPE. RX PubMed=12015986; DOI=10.1016/s0092-8674(02)00715-8; RA Tree D.R.P., Shulman J.M., Rousset R., Scott M.P., Gubb D., Axelrod J.D.; RT "Prickle mediates feedback amplification to generate asymmetric planar cell RT polarity signaling."; RL Cell 109:371-381(2002). RN [5] {ECO:0000305} RP INTERACTION WITH VANG, AND SUBCELLULAR LOCATION. RX PubMed=12941693; DOI=10.1093/emboj/cdg424; RA Jenny A., Darken R.S., Wilson P.A., Mlodzik M.; RT "Prickle and Strabismus form a functional complex to generate a correct RT axis during planar cell polarity signaling."; RL EMBO J. 22:4409-4420(2003). RN [6] {ECO:0000305} RP FUNCTION, INTERACTION WITH VANG, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DISRUPTION PHENOTYPE. RX PubMed=12642492; DOI=10.1242/dev.00411; RA Rawls A.S., Wolff T.; RT "Strabismus requires Flamingo and Prickle function to regulate tissue RT polarity in the Drosophila eye."; RL Development 130:1877-1887(2003). RN [7] {ECO:0000305} RP FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DISRUPTION PHENOTYPE. RX PubMed=15937478; DOI=10.1038/ncb1271; RA Jenny A., Reynolds-Kenneally J., Das G., Burnett M., Mlodzik M.; RT "Diego and Prickle regulate Frizzled planar cell polarity signalling by RT competing for Dishevelled binding."; RL Nat. Cell Biol. 7:691-697(2005). CC -!- FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization CC along the apical/basal axis of epithelial cells. Correct expression of CC the alternative isoforms is required for PCP signaling in imaginal CC disks. PCP signaling in the wing disk requires the receptor fz and the CC cytoplasmic proteins dsh and pk. These act in a feedback loop leading CC to activation of the jnk cascade and subsequent polarized arrangement CC of hairs and bristles. Dgo and pk compete with one another for dsh CC binding, thereby modulating fz dsh activity and ensuring tight control CC over fz PCP signaling. Vang, stan and pk function together to regulate CC the establishment of tissue polarity in the adult eye. CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, CC ECO:0000269|PubMed:15937478}. CC -!- SUBUNIT: Interacts with dsh; PET and LIM domains interact with dsh DEP CC domain, in wing cells. Interacts with Vang in photoreceptor cells. CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12015986, CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, CC ECO:0000269|PubMed:15937478}; Peripheral membrane protein CC {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Cytoplasmic CC side {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, CC ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}. CC Note=Localized to the proximal wing cell boundary where fz and dsh CC localization is antagonized by binding the dsh DEP domain and CC preventing dsh cortical localization. Localization to the anterior CC photoreceptor cell membrane. {ECO:0000269|PubMed:12015986, CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, CC ECO:0000269|PubMed:15937478}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=C {ECO:0000269|PubMed:10731132}; Synonyms=sple CC {ECO:0000269|PubMed:10485852}; CC IsoId=A1Z6W3-1; Sequence=Displayed; CC Name=A {ECO:0000269|PubMed:10731132}; Synonyms=pk CC {ECO:0000269|PubMed:10485852}; CC IsoId=A1Z6W3-2; Sequence=VSP_052413, VSP_052414; CC Name=B {ECO:0000269|PubMed:10731132}; Synonyms=pkM CC {ECO:0000269|PubMed:10485852}; CC IsoId=A1Z6W3-3; Sequence=VSP_052412, VSP_052415; CC -!- TISSUE SPECIFICITY: Expressed in the wing, leg and eye imaginal disks. CC Expressed within the photoreceptors of the eye. CC {ECO:0000269|PubMed:10485852, ECO:0000269|PubMed:12015986, CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:15937478}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Isoform CC B is expressed in embryos only. Isoform A and isoform C are expressed CC in embryos and pupae. {ECO:0000269|PubMed:10485852}. CC -!- DISRUPTION PHENOTYPE: Flies exhibit aberrant hair and bristle CC orientation on the wings and aberrant ommatidial arrangement in the CC compound eye. {ECO:0000269|PubMed:12015986, CC ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:15937478}. CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family. CC {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; AJ243708; CAB57344.3; -; mRNA. DR EMBL; AJ243710; CAB57345.3; -; mRNA. DR EMBL; AJ243709; CAB99211.2; -; mRNA. DR EMBL; AE013599; AAF59281.2; -; Genomic_DNA. DR EMBL; AE013599; AAF59284.2; -; Genomic_DNA. DR EMBL; AE013599; AAM68908.1; -; Genomic_DNA. DR RefSeq; NP_724534.1; NM_165508.2. [A1Z6W3-2] DR RefSeq; NP_724535.1; NM_165509.2. [A1Z6W3-3] DR RefSeq; NP_724538.1; NM_165512.2. [A1Z6W3-1] DR AlphaFoldDB; A1Z6W3; -. DR SMR; A1Z6W3; -. DR BioGRID; 69608; 31. DR DIP; DIP-59584N; -. DR IntAct; A1Z6W3; 4. DR STRING; 7227.FBpp0088115; -. DR PaxDb; 7227-FBpp0088115; -. DR EnsemblMetazoa; FBtr0089042; FBpp0088113; FBgn0003090. [A1Z6W3-2] DR EnsemblMetazoa; FBtr0089043; FBpp0088114; FBgn0003090. [A1Z6W3-3] DR EnsemblMetazoa; FBtr0089044; FBpp0088115; FBgn0003090. [A1Z6W3-1] DR GeneID; 45343; -. DR KEGG; dme:Dmel_CG11084; -. DR AGR; FB:FBgn0003090; -. DR CTD; 18745; -. DR FlyBase; FBgn0003090; pk. DR VEuPathDB; VectorBase:FBgn0003090; -. DR eggNOG; KOG1704; Eukaryota. DR GeneTree; ENSGT00940000153629; -. DR InParanoid; A1Z6W3; -. DR OMA; WPAKPTN; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; A1Z6W3; -. DR Reactome; R-DME-350368; Activation of RHO1 by FZ:DSH complex. DR Reactome; R-DME-350369; Negative feedback loop regulates asymmetric localisation. DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex. DR Reactome; R-DME-350411; Formation and asymmetric localisation of transmembrane complexes. DR Reactome; R-DME-350480; Activation of non-muscle Myosin II. DR Reactome; R-DME-450728; Inhibition of actin polymerization. DR Reactome; R-DME-4608870; Asymmetric localization of PCP proteins. DR BioGRID-ORCS; 45343; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 45343; -. DR PRO; PR:A1Z6W3; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0003090; Expressed in eye disc (Drosophila) and 20 other cell types or tissues. DR ExpressionAtlas; A1Z6W3; baseline and differential. DR GO; GO:0030424; C:axon; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB. DR GO; GO:0098930; P:axonal transport; IMP:FlyBase. DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase. DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase. DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; TAS:FlyBase. DR GO; GO:0007164; P:establishment of tissue polarity; IMP:UniProtKB. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase. DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:FlyBase. DR GO; GO:0045185; P:maintenance of protein location; TAS:FlyBase. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase. DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase. DR GO; GO:0045773; P:positive regulation of axon extension; IGI:FlyBase. DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase. DR CDD; cd09415; LIM1_Prickle; 1. DR CDD; cd09418; LIM2_Prickle; 1. DR CDD; cd09420; LIM3_Prickle; 1. DR CDD; cd09827; PET_Prickle; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3. DR InterPro; IPR033725; LIM1_prickle. DR InterPro; IPR033726; LIM2_prickle. DR InterPro; IPR033727; LIM3_prickle. DR InterPro; IPR010442; PET_domain. DR InterPro; IPR033723; PET_prickle. DR InterPro; IPR047120; Pk/Esn/Tes. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24211; LIM DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24211:SF20; PROTEIN ESPINAS-RELATED; 1. DR Pfam; PF00412; LIM; 2. DR Pfam; PF06297; PET; 1. DR SMART; SM00132; LIM; 3. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR PROSITE; PS00478; LIM_DOMAIN_1; 2. DR PROSITE; PS50023; LIM_DOMAIN_2; 3. DR PROSITE; PS51303; PET; 1. DR Genevisible; A1Z6W3; DM. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Developmental protein; LIM domain; KW Membrane; Metal-binding; Reference proteome; Repeat; Zinc. FT CHAIN 1..1299 FT /note="Protein prickle" FT /id="PRO_0000288834" FT DOMAIN 515..623 FT /note="PET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636" FT DOMAIN 622..686 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 687..747 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 748..810 FT /note="LIM zinc-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 115..181 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 241..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 425..527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 807..865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..940 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1026..1249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 249..273 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 274..288 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 808..827 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 843..865 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 919..936 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1028..1042 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1065..1102 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1135..1152 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1153..1180 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1182..1216 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 2..80 FT /note="SSLSTGGGAGGSSGGPGGADAAAAPAAGQATVTATGNMEPAMVPRTANLLAC FT KQWWRVCFLYGDQQKYYRQLYSKAAAQ -> NDSTDNLHADCDGRVSNNNNGNSNTNDG FT PNNDGDSDEEVIEGMALLEGNYQVLRQWVPPAPNYWDAPPKAIIKSAEVR (in FT isoform B)" FT /evidence="ECO:0000303|PubMed:10485852" FT /id="VSP_052412" FT VAR_SEQ 2..13 FT /note="SSLSTGGGAGGS -> DTPNQMPVELER (in isoform A)" FT /evidence="ECO:0000303|PubMed:10485852" FT /id="VSP_052413" FT VAR_SEQ 14..349 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000303|PubMed:10485852" FT /id="VSP_052414" FT VAR_SEQ 81..349 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:10485852" FT /id="VSP_052415" FT CONFLICT 175..177 FT /note="ESS -> VSN (in Ref. 1; CAB57345)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="V -> A (in Ref. 1; CAB57345)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="Q -> P (in Ref. 1; CAB57345)" FT /evidence="ECO:0000305" FT CONFLICT 715 FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 746 FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 755 FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 797 FT /note="A -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 830 FT /note="R -> G (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 970 FT /note="S -> P (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 1029 FT /note="L -> V (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 1134 FT /note="G -> S (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" FT CONFLICT 1231 FT /note="E -> K (in Ref. 1; CAB57344/CAB57345/CAB99211)" FT /evidence="ECO:0000305" SQ SEQUENCE 1299 AA; 140722 MW; 8BFAF1F75F352485 CRC64; MSSLSTGGGA GGSSGGPGGA DAAAAPAAGQ ATVTATGNME PAMVPRTANL LACKQWWRVC FLYGDQQKYY RQLYSKAAAQ RLADANQEPD NARDREYDTV DCDLIAGQLD AVEDADDGID LGDHSSTPKG GATTAGRPLF PHSSSPRRSK KLLRSLRAHV RGEKLPKNDT TTANESSEVT QRNARVTVLD DPFLFGIDAD HLGDLVVRGK RYSTLDATEN MARFYAEQEA TAQVLEIIEQ EEESPEQEAP KPALPPKQKQ QRPVPPLPPP PANRVTQDQG TQPAAPQVPL QPLTAGDLQF LNLSLRQRSL PRSMKPFKDA HDISFTFNEL DTSAEPEVAT GAAQQESNEP ISRTPLTQIS YLQKIPTLPR HFSPSGQGLA TPPALGSGGM GLPSSSSASA LYAAQAAAGI LPTSPLPLQR HQQYLPPHHQ QHPGAGMGPG PGSGAAAGPP LGPQYSPGCS ANPKYSNAQL PPPPHHHHQL SPALSTPSPP SLLHHPAGGT SSASAHAPFL GGPHMDMQRQ SHSDDDSGCA LEEYTWVPPG LRPDQVRLYF SQIPDDKVPY VNSPGEQYRV RQLLHQLPPH DNEVRYCHSL TDEERKELRL FSTQRKRDAL GRGNVRQLMS ARPCDGCDDL ISTGDIAVFA TRLGPNASWH PACFACSVCR ELLVDLIYFH RDGRMYCGRH HAETLKPRCS ACDEIILADE CTEAEGRAWH MNHFACHECD KQLGGQRYIM REGKPYCLHC FDAMFAEYCD YCGEAIGVDQ GQMSHDGQHW HATDECFSCN TCRCSLLGRA FLPRRGAIYC SIACSKGEPP TPSDSSGTGM YTTPTPPTQR VRPHPQAPLP ARIPSSHASS SPPMSPQQQQ QHQATFNQAM YQMQSQQMEA AGGLVDQSKS YAASDSDAGV VKDLEHGGHM GGGDLTDFSG GRASSTSQNL SPLNSPGDFQ PHFLPKPMEL QRDGVYNFNE MSSNLDAAWS AKPTNSYHLQ RQLLENPHTA SMPELAGKLV APPAHMQHLS QLHAVSSHQF QQHEYADILH PPPPPPGEIP ELPTPNLSVA STALPPELMG SPTHSAGDRS LNTPMSTQSA SHAPPHPVSI LSGASSSSPM SGEPAKKKGV RFEGIPDTLP RSRSYSGNGA GTSGGGERER DRDKDKEGGG RHGHGHSSRR RRRRKSSSSS SHHRSGSGHR SHSTTRADTY APAQPLSSSY QGPPSVLQAA NLVHESPSRQ QRERERERER EESEESDVCS TCSSSSSSSE DYMMMYQLPQ RRHYGGVRVS YVPNDALAYD RKRKPSELGG DKDKNCIIS //