ID ACT1_DROME Reviewed; 376 AA. AC P10987; A4V404; Q24227; Q6YN46; Q9U5X7; Q9W460; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 4. DT 27-MAR-2024, entry version 213. DE RecName: Full=Actin-5C; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE Flags: Precursor; GN Name=Act5C; ORFNames=CG4027; 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 [GENOMIC DNA]. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. 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. 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]. RC STRAIN=Berkeley; TISSUE=Embryo; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84 AND 324-376. RX PubMed=3123314; DOI=10.1101/gad.1.10.1161; RA Vigoreaux J.O., Tobin S.L.; RT "Stage-specific selection of alternative transcriptional initiation sites RT from the 5C actin gene of Drosophila melanogaster."; RL Genes Dev. 1:1161-1171(1987). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75. RX PubMed=6263481; DOI=10.1016/0092-8674(81)90506-7; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly conserved RT but intron positions are not."; RL Cell 24:107-116(1981). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. RX PubMed=3097509; DOI=10.1128/mcb.6.6.2080-2088.1986; RA Bond B.J., Davidson N.; RT "The Drosophila melanogaster actin 5C gene uses two transcription RT initiation sites and three polyadenylation sites to express multiple mRNA RT species."; RL Mol. Cell. Biol. 6:2080-2088(1986). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376. RC STRAIN=Canton-S; RX PubMed=2896018; DOI=10.1016/0167-4781(88)90070-x; RA Rao J.P., Zafar R.S., Sodja A.; RT "Transcriptional activity at the 3' end of the actin gene at 5C on the X RT chromosome of Drosophila melanogaster."; RL Biochim. Biophys. Acta 950:30-44(1988). RN [9] RP OXIDATION AT MET-45 AND MET-48, AND MUTAGENESIS OF MET-45 AND MET-48. RX PubMed=22116028; DOI=10.1126/science.1211956; RA Hung R.J., Pak C.W., Terman J.R.; RT "Direct redox regulation of F-actin assembly and disassembly by Mical."; RL Science 334:1710-1713(2011). RN [10] RP INTERACTION WITH RAB6. RX PubMed=22928698; DOI=10.1021/pr300274k; RA Ye T., Tang W., Zhang X.; RT "Involvement of Rab6 in the regulation of phagocytosis against virus RT infection in invertebrates."; RL J. Proteome Res. 11:4834-4846(2012). CC -!- FUNCTION: Actins are highly conserved proteins that are involved in CC various types of cell motility and are ubiquitously expressed in all CC eukaryotic cells. CC -!- FUNCTION: Multiple isoforms are involved in various cellular functions CC such as cytoskeleton structure, cell mobility, chromosome movement and CC muscle contraction. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P68137}; CC -!- SUBUNIT: Interacts with Rab6. {ECO:0000269|PubMed:22928698}. CC -!- INTERACTION: CC P10987; Q9U1K1-1: spir; NbExp=6; IntAct=EBI-130188, EBI-3431623; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- PTM: N-terminal cleavage of acetylated cysteine of immature actin by CC ACTMAP. {ECO:0000250|UniProtKB:P68134}. CC -!- PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes CC actin filament depolymerization. Methionine sulfoxide is produced CC stereospecifically, but it is not known whether the (S)-S-oxide or the CC (R)-S-oxide is produced. {ECO:0000269|PubMed:22116028}. CC -!- MISCELLANEOUS: In Drosophila there are 6 closely related actin genes. CC -!- SIMILARITY: Belongs to the actin family. {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; K00667; AAA28316.1; -; Genomic_DNA. DR EMBL; AE014298; AAF46098.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09154.1; -; Genomic_DNA. DR EMBL; AE014298; AAX52479.1; -; Genomic_DNA. DR EMBL; AE014298; AAX52480.1; -; Genomic_DNA. DR EMBL; AY089562; AAL90300.1; -; mRNA. DR EMBL; X06383; CAA29681.1; -; Genomic_DNA. DR EMBL; X06384; CAB61444.1; -; Genomic_DNA. DR EMBL; M13587; AAA28315.1; -; Genomic_DNA. DR EMBL; X07627; CAA30474.1; -; Genomic_DNA. DR PIR; A28258; A28258. DR RefSeq; NP_001014725.1; NM_001014725.2. DR RefSeq; NP_001014726.1; NM_001014726.2. DR RefSeq; NP_001284915.1; NM_001297986.1. DR RefSeq; NP_511052.1; NM_078497.4. DR RefSeq; NP_727048.1; NM_167053.2. DR PDB; 2HF3; X-ray; 1.80 A; A=3-376. DR PDB; 2HF4; X-ray; 1.80 A; A=3-376. DR PDB; 3EKS; X-ray; 1.80 A; A=2-376. DR PDB; 3EKU; X-ray; 2.50 A; A=2-376. DR PDB; 3EL2; X-ray; 2.50 A; A=2-376. DR PDB; 3MMV; X-ray; 2.80 A; A=3-376. DR PDB; 3MN6; X-ray; 2.00 A; A/F/K=3-376. DR PDB; 3MN7; X-ray; 2.00 A; A=3-376. DR PDB; 3MN9; X-ray; 2.00 A; A=3-376. DR PDB; 4JHD; X-ray; 2.91 A; A/B/D/E=1-376. DR PDB; 4M63; X-ray; 2.75 A; C/D/E=1-376. DR PDB; 4RWT; X-ray; 2.98 A; A/B=1-376. DR PDB; 5WFN; X-ray; 3.00 A; A/B=1-376. DR PDB; 8OH4; EM; 16.50 A; A/B/C/D/E/F/G/H=7-376. DR PDBsum; 2HF3; -. DR PDBsum; 2HF4; -. DR PDBsum; 3EKS; -. DR PDBsum; 3EKU; -. DR PDBsum; 3EL2; -. DR PDBsum; 3MMV; -. DR PDBsum; 3MN6; -. DR PDBsum; 3MN7; -. DR PDBsum; 3MN9; -. DR PDBsum; 4JHD; -. DR PDBsum; 4M63; -. DR PDBsum; 4RWT; -. DR PDBsum; 5WFN; -. DR PDBsum; 8OH4; -. DR AlphaFoldDB; P10987; -. DR SMR; P10987; -. DR BioGRID; 58020; 93. DR ComplexPortal; CPX-2346; Non-canonical BRAHMA-associated SWI/SNF ATP-dependent chromatin remodeling complex. DR ComplexPortal; CPX-2383; Polybromo-containing BRAHMA associated proteins complex. DR ComplexPortal; CPX-2693; INO80 chromatin remodeling complex. DR ComplexPortal; CPX-2746; Brahma SWI/SNF ATP-dependent chromatin remodeling complex. DR DIP; DIP-18961N; -. DR ELM; P10987; -. DR IntAct; P10987; 11. DR MINT; P10987; -. DR STRING; 7227.FBpp0311818; -. DR MetOSite; P10987; -. DR PaxDb; 7227-FBpp0100124; -. DR EnsemblMetazoa; FBtr0070822; FBpp0070787; FBgn0000042. DR EnsemblMetazoa; FBtr0070823; FBpp0070788; FBgn0000042. DR EnsemblMetazoa; FBtr0100662; FBpp0100124; FBgn0000042. DR EnsemblMetazoa; FBtr0100663; FBpp0100125; FBgn0000042. DR EnsemblMetazoa; FBtr0345894; FBpp0311818; FBgn0000042. DR GeneID; 31521; -. DR KEGG; dme:Dmel_CG4027; -. DR AGR; FB:FBgn0000042; -. DR CTD; 31521; -. DR FlyBase; FBgn0000042; Act5C. DR VEuPathDB; VectorBase:FBgn0000042; -. DR eggNOG; KOG0676; Eukaryota. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; P10987; -. DR OMA; FHTTAER; -. DR OrthoDB; 10at2759; -. DR PhylomeDB; P10987; -. DR Reactome; R-DME-114608; Platelet degranulation. DR Reactome; R-DME-190873; Gap junction degradation. DR Reactome; R-DME-196025; Formation of annular gap junctions. DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-DME-3928662; EPHB-mediated forward signaling. DR Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-DME-437239; Recycling pathway of L1. DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-DME-445095; Interaction between L1 and Ankyrins. DR Reactome; R-DME-446353; Cell-extracellular matrix interactions. DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-DME-5674135; MAP2K and MAPK activation. DR Reactome; R-DME-5689603; UCH proteinases. DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER. DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis. DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-DME-9035034; RHOF GTPase cycle. DR SignaLink; P10987; -. DR BioGRID-ORCS; 31521; 0 hits in 3 CRISPR screens. DR ChiTaRS; Act5C; fly. DR EvolutionaryTrace; P10987; -. DR GenomeRNAi; 31521; -. DR PRO; PR:P10987; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0000042; Expressed in cleaving embryo and 38 other cell types or tissues. DR ExpressionAtlas; P10987; baseline and differential. DR GO; GO:0035060; C:brahma complex; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006338; P:chromatin remodeling; IC:FlyBase. DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:FlyBase. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase. DR GO; GO:0007291; P:sperm individualization; IEP:FlyBase. DR GO; GO:0035148; P:tube formation; IGI:FlyBase. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF46; ACTIN-42A-RELATED; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. DR Genevisible; P10987; DM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; KW Methylation; Nucleotide-binding; Oxidation; Reference proteome. FT PROPEP 1..2 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000000656" FT CHAIN 3..376 FT /note="Actin-5C" FT /id="PRO_0000000657" FT MOD_RES 3 FT /note="N-acetylaspartate" FT /evidence="ECO:0000250" FT MOD_RES 45 FT /note="Methionine sulfoxide" FT /evidence="ECO:0000269|PubMed:22116028" FT MOD_RES 48 FT /note="Methionine sulfoxide" FT /evidence="ECO:0000269|PubMed:22116028" FT MOD_RES 74 FT /note="Tele-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:P02572" FT MUTAGEN 45 FT /note="M->L: Abolishes formation of methionine-sulfoxide FT and subsequent depolymerization." FT /evidence="ECO:0000269|PubMed:22116028" FT MUTAGEN 48 FT /note="M->L: Depolymerizes in the presence of Mical." FT /evidence="ECO:0000269|PubMed:22116028" FT CONFLICT 264 FT /note="Q -> H (in Ref. 1; AAA28316)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="A -> S (in Ref. 1; AAA28316)" FT /evidence="ECO:0000305" FT CONFLICT 350 FT /note="L -> S (in Ref. 1; AAA28316)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="I -> T (in Ref. 1; AAA28316)" FT /evidence="ECO:0000305" FT CONFLICT 366..367 FT /note="SG -> AW (in Ref. 8; CAA30474)" FT /evidence="ECO:0000305" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 15..22 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:3MN6" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:3EKS" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:3MMV" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:2HF3" FT TURN 71..74 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:4M63" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:2HF3" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 131..137 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 138..145 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 183..197 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 204..217 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 254..260 FT /evidence="ECO:0007829|PDB:2HF3" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 275..284 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 291..295 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 310..321 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 339..348 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 351..356 FT /evidence="ECO:0007829|PDB:2HF3" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 360..366 FT /evidence="ECO:0007829|PDB:2HF3" FT HELIX 370..374 FT /evidence="ECO:0007829|PDB:2HF3" SQ SEQUENCE 376 AA; 41822 MW; BDAF13C191BB1BBC CRC64; MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPSI VHRKCF //