ID RUMI_DROME Reviewed; 411 AA. AC Q8T045; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=O-glucosyltransferase rumi; DE EC=2.4.1.- {ECO:0000269|PubMed:18243100, ECO:0000269|PubMed:27428513}; DE Flags: Precursor; GN Name=rumi {ECO:0000312|FlyBase:FBgn0086253}; ORFNames=CG31152; 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:0000312|EMBL:AAN13920.1} 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 [2] {ECO:0000305, ECO:0000312|EMBL:AAN13920.1} RP GENOME REANNOTATION. 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 [3] {ECO:0000312|EMBL:AAL39709.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39709.1}; RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF RP GLY-189, AND DISRUPTION PHENOTYPE. RX PubMed=18243100; DOI=10.1016/j.cell.2007.12.016; RA Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A., RA Pan H., Haltiwanger R.S., Bellen H.J.; RT "Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is RT required for Notch signaling."; RL Cell 132:247-258(2008). RN [5] RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-189. RX PubMed=27807076; DOI=10.15252/emmm.201505815; RA Servian-Morilla E., Takeuchi H., Lee T.V., Clarimon J., Mavillard F., RA Area-Gomez E., Rivas E., Nieto-Gonzalez J.L., Rivero M.C., RA Cabrera-Serrano M., Gomez-Sanchez L., Martinez-Lopez J.A., Estrada B., RA Marquez C., Morgado Y., Suarez-Calvet X., Pita G., Bigot A., Gallardo E., RA Fernandez-Chacon R., Hirano M., Haltiwanger R.S., Jafar-Nejad H., RA Paradas C.; RT "A POGLUT1 mutation causes a muscular dystrophy with reduced Notch RT signaling and satellite cell loss."; RL EMBO Mol. Med. 8:1289-1309(2016). RN [6] {ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, ECO:0007744|PDB:5F86, ECO:0007744|PDB:5F87} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 21-407 IN COMPLEXES WITH UDP; RP UDP-GLUCOSE AND SUBSTRATE PEPTIDES, CATALYTIC ACTIVITY, FUNCTION, ACTIVE RP SITE, PATHWAY, MUTAGENESIS OF PHE-122; ALA-124; ARG-125; ASP-151; ALA-192; RP PRO-197; GLY-199; SER-231; THR-233; ARG-237; ARG-245; GLN-259; THR-267; RP SER-296 AND ARG-298, AND DISULFIDE BONDS. RX PubMed=27428513; DOI=10.1038/nchembio.2135; RA Yu H., Takeuchi H., Takeuchi M., Liu Q., Kantharia J., Haltiwanger R.S., RA Li H.; RT "Structural analysis of Notch-regulating Rumi reveals basis for pathogenic RT mutations."; RL Nat. Chem. Biol. 12:735-740(2016). CC -!- FUNCTION: Protein O-glucosyltransferase. Catalyzes the reaction that CC attaches glucose through an O-glycosidic linkage to a conserved serine CC residue found in the consensus sequence C-X-S-X-[PA]-C in epidermal CC growth factor-like repeats (PubMed:27428513). Regulates Notch signaling CC by glucosylating Notch in the ER, glucosylation is required for the CC correct folding and cleavage of Notch. {ECO:0000269|PubMed:18243100, CC ECO:0000269|PubMed:27428513}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:27428513}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138, ECO:0000269|PubMed:18243100}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC {ECO:0000269|PubMed:18243100}. CC -!- DISRUPTION PHENOTYPE: Flies exhibit a temperature-dependent loss of CC Notch signaling, resulting in bristle loss (PubMed:18243100). Defects CC in muscle development (PubMed:27807076). {ECO:0000269|PubMed:18243100, CC ECO:0000269|PubMed:27807076}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 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; AE014297; AAN13920.1; -; Genomic_DNA. DR EMBL; AY069564; AAL39709.1; -; mRNA. DR RefSeq; NP_651095.1; NM_142838.4. DR PDB; 5F84; X-ray; 2.50 A; A=21-407. DR PDB; 5F85; X-ray; 2.15 A; A=21-407. DR PDB; 5F86; X-ray; 1.90 A; A=21-407. DR PDB; 5F87; X-ray; 3.20 A; A/B/C/D/E/F=21-407. DR PDBsum; 5F84; -. DR PDBsum; 5F85; -. DR PDBsum; 5F86; -. DR PDBsum; 5F87; -. DR AlphaFoldDB; Q8T045; -. DR SMR; Q8T045; -. DR BioGRID; 77376; 6. DR DIP; DIP-62084N; -. DR STRING; 7227.FBpp0083713; -. DR CAZy; GT90; Glycosyltransferase Family 90. DR PaxDb; 7227-FBpp0083713; -. DR DNASU; 326122; -. DR EnsemblMetazoa; FBtr0084320; FBpp0083713; FBgn0086253. DR GeneID; 326122; -. DR KEGG; dme:Dmel_CG31152; -. DR UCSC; CG31152-RA; d. melanogaster. DR AGR; FB:FBgn0086253; -. DR CTD; 326122; -. DR FlyBase; FBgn0086253; rumi. DR VEuPathDB; VectorBase:FBgn0086253; -. DR eggNOG; KOG2458; Eukaryota. DR GeneTree; ENSGT00940000158283; -. DR InParanoid; Q8T045; -. DR OMA; LEDHCQY; -. DR OrthoDB; 1826823at2759; -. DR PhylomeDB; Q8T045; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 326122; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 326122; -. DR PRO; PR:Q8T045; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0086253; Expressed in eye disc (Drosophila) and 20 other cell types or tissues. DR ExpressionAtlas; Q8T045; baseline and differential. DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0140561; F:EGF-domain serine glucosyltransferase activity; IDA:FlyBase. DR GO; GO:0140562; F:EGF-domain serine xylosyltransferase activity; IDA:FlyBase. DR GO; GO:0046527; F:glucosyltransferase activity; IDA:GO_Central. DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB. DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IBA:GO_Central. DR GO; GO:0045165; P:cell fate commitment; IMP:FlyBase. DR GO; GO:0060537; P:muscle tissue development; IMP:UniProtKB. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:FlyBase. DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB. DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase. DR InterPro; IPR006598; CAP10. DR PANTHER; PTHR12203; KDEL LYS-ASP-GLU-LEU CONTAINING - RELATED; 1. DR PANTHER; PTHR12203:SF35; PROTEIN O-GLUCOSYLTRANSFERASE 1; 1. DR Pfam; PF05686; Glyco_transf_90; 1. DR SMART; SM00672; CAP10; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR Genevisible; Q8T045; DM. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Glycosyltransferase; KW Notch signaling pathway; Reference proteome; Signal; Transferase. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..411 FT /note="O-glucosyltransferase rumi" FT /evidence="ECO:0000255" FT /id="PRO_0000342687" FT REGION 192..197 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:27428513" FT MOTIF 408..411 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138, FT ECO:0000269|PubMed:18243100" FT ACT_SITE 151 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000269|PubMed:27428513" FT BINDING 229..233 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F87" FT BINDING 237 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F87" FT BINDING 276..278 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F87" FT BINDING 294..298 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F87" FT SITE 122 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:27428513" FT SITE 232 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:27428513" FT SITE 259 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:27428513" FT DISULFID 64..75 FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F86, ECO:0007744|PDB:5F87" FT DISULFID 73..378 FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F86, ECO:0007744|PDB:5F87" FT DISULFID 120..126 FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F86, ECO:0007744|PDB:5F87" FT DISULFID 282..305 FT /evidence="ECO:0000269|PubMed:27428513, FT ECO:0007744|PDB:5F84, ECO:0007744|PDB:5F85, FT ECO:0007744|PDB:5F86, ECO:0007744|PDB:5F87" FT MUTAGEN 122 FT /note="F->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 124 FT /note="A->F: Slightly decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 125 FT /note="R->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 151 FT /note="D->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 189 FT /note="G->E: In rumi-79; complete loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:18243100, FT ECO:0000269|PubMed:27807076" FT MUTAGEN 192 FT /note="A->F: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 197 FT /note="P->A: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 199 FT /note="G->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 231 FT /note="S->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 233 FT /note="T->A: Nearly complete loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 237 FT /note="R->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 245 FT /note="R->L: Nearly complete loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 259 FT /note="Q->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 267 FT /note="T->I: Nearly complete loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 296 FT /note="S->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 298 FT /note="R->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT MUTAGEN 298 FT /note="R->W: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:27428513" FT HELIX 43..60 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 77..84 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:5F86" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 123..133 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 134..139 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 203..216 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 222..231 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 238..246 FT /evidence="ECO:0007829|PDB:5F86" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 264..267 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 278..281 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 284..290 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 298..303 FT /evidence="ECO:0007829|PDB:5F86" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:5F86" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:5F87" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 353..370 FT /evidence="ECO:0007829|PDB:5F86" FT HELIX 373..388 FT /evidence="ECO:0007829|PDB:5F86" FT STRAND 401..405 FT /evidence="ECO:0007829|PDB:5F86" SQ SEQUENCE 411 AA; 47735 MW; 785EA3A15977B69D CRC64; MLINHLIVVL LISLVGTGGA EDDGLCSADQ KSCAQSEPDQ INEDEFSFKI RRQIEKANAD YKPCSSDPQD SDCSCHANVL KRDLAPYKST GVTRQMIESS ARYGTKYKIY GHRLYRDANC MFPARCEGIE HFLLPLVATL PDMDLIINTR DYPQLNAAWG NAAGGPVFSF SKTKEYRDIM YPAWTFWAGG PATKLHPRGI GRWDQMREKL EKRAAAIPWS QKRSLGFFRG SRTSDERDSL ILLSRRNPEL VEAQYTKNQG WKSPKDTLDA PAADEVSFED HCKYKYLFNF RGVAASFRLK HLFLCKSLVF HVGDEWQEFF YDQLKPWVHY VPLKSYPSQQ EYEHILSFFK KNDALAQEIA QRGYDFIWEH LRMKDIKCYW RKLLKRYVKL LQYEVKPEDQ LIYIGPKKDE L //