RUMI_DROME
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 03-AUG-2022, entry version 133.
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}.
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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; Q8T045; -.
DR PRIDE; Q8T045; -.
DR DNASU; 326122; -.
DR EnsemblMetazoa; FBtr0084320; FBpp0083713; FBgn0086253.
DR GeneID; 326122; -.
DR KEGG; dme:Dmel_CG31152; -.
DR UCSC; CG31152-RA; d. melanogaster.
DR CTD; 326122; -.
DR FlyBase; FBgn0086253; rumi.
DR VEuPathDB; VectorBase:FBgn0086253; -.
DR eggNOG; KOG2458; Eukaryota.
DR GeneTree; ENSGT00940000158283; -.
DR InParanoid; Q8T045; -.
DR OMA; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
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 tissues.
DR ExpressionAtlas; Q8T045; baseline and differential.
DR Genevisible; Q8T045; DM.
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 Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
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
