MYS9_DROME
ID MYS9_DROME Reviewed; 1253 AA.
AC Q01989; A4V3C6; Q59DV3; Q59DV4; Q9VCA4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Myosin heavy chain 95F;
DE AltName: Full=95F MHC;
DE AltName: Full=Protein jaguar;
GN Name=jar; Synonyms=Mhc95F; ORFNames=CG5695;
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 B), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC STRAIN=Canton-S; TISSUE=Embryo, and Ovary;
RX PubMed=1429838; DOI=10.1083/jcb.119.4.823;
RA Kellerman K.A., Miller K.G.;
RT "An unconventional myosin heavy chain gene from Drosophila melanogaster.";
RL J. Cell Biol. 119:823-834(1992).
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 B).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9472041; DOI=10.1083/jcb.140.4.897;
RA Lantz V.A., Miller K.G.;
RT "A class VI unconventional myosin is associated with a homologue of a
RT microtubule-binding protein, cytoplasmic linker protein-170, in neurons and
RT at the posterior pole of Drosophila embryos.";
RL J. Cell Biol. 140:897-910(1998).
CC -!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
CC activity that is activated by actin. Together CLIP-190 and jar may
CC coordinate the interaction between the actin and microtubule
CC cytoskeleton. May link endocytic vesicles to microtubules and may be
CC involved in transport in the early embryo and in the dynamic process of
CC dorsal closure. It is believed that its function changes during the
CC life cycle. {ECO:0000269|PubMed:1429838, ECO:0000269|PubMed:9472041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9472041}. Note=Microtubule-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=B; Synonyms=G, J, K, Em-3;
CC IsoId=Q01989-1; Sequence=Displayed;
CC Name=H; Synonyms=C, Em-1;
CC IsoId=Q01989-2; Sequence=VSP_003343;
CC Name=I; Synonyms=D, Em-5;
CC IsoId=Q01989-3; Sequence=VSP_003344, VSP_003345;
CC Name=145 kDa;
CC IsoId=Q01989-4; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Isoform B is present at a higher level in the head
CC and gonads than in the thoraxes. Isoform 145 kDa is found only in the
CC head. CLIP-190 and jar are coexpressed at several times in development
CC and in a number of tissues, including embryonic axonal neuron processes
CC and posterior pole. {ECO:0000269|PubMed:1429838,
CC ECO:0000269|PubMed:9472041}.
CC -!- DEVELOPMENTAL STAGE: Isoform B is expressed both maternally and
CC zygotically throughout development with highest level during mid-
CC embryogenesis and adulthood. At these zygotic stages isoform D is also
CC expressed. {ECO:0000269|PubMed:1429838}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO45215.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X67077; CAA47462.1; -; mRNA.
DR EMBL; AE014297; AAF56269.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN13992.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52973.2; -; Genomic_DNA.
DR EMBL; AE014297; AAX52974.2; -; Genomic_DNA.
DR EMBL; AE014297; AAX52975.2; -; Genomic_DNA.
DR EMBL; AE014297; AAX52976.2; -; Genomic_DNA.
DR EMBL; BT004859; AAO45215.1; ALT_FRAME; mRNA.
DR PIR; A44400; A44400.
DR RefSeq; NP_001014647.2; NM_001014647.3. [Q01989-1]
DR RefSeq; NP_001014648.2; NM_001014648.3. [Q01989-1]
DR RefSeq; NP_001014649.2; NM_001014649.3. [Q01989-3]
DR RefSeq; NP_001014650.2; NM_001014650.3. [Q01989-2]
DR RefSeq; NP_001262905.1; NM_001275976.1. [Q01989-2]
DR RefSeq; NP_001262906.1; NM_001275977.2. [Q01989-1]
DR RefSeq; NP_524478.4; NM_079754.4. [Q01989-1]
DR RefSeq; NP_732976.1; NM_170138.3. [Q01989-1]
DR AlphaFoldDB; Q01989; -.
DR SMR; Q01989; -.
DR BioGRID; 67817; 33.
DR IntAct; Q01989; 4.
DR STRING; 7227.FBpp0290582; -.
DR PaxDb; Q01989; -.
DR PRIDE; Q01989; -.
DR DNASU; 42889; -.
DR EnsemblMetazoa; FBtr0084636; FBpp0084020; FBgn0011225. [Q01989-1]
DR EnsemblMetazoa; FBtr0301367; FBpp0290581; FBgn0011225. [Q01989-1]
DR EnsemblMetazoa; FBtr0301368; FBpp0290582; FBgn0011225. [Q01989-2]
DR EnsemblMetazoa; FBtr0301369; FBpp0290583; FBgn0011225. [Q01989-3]
DR EnsemblMetazoa; FBtr0301370; FBpp0290584; FBgn0011225. [Q01989-1]
DR EnsemblMetazoa; FBtr0301371; FBpp0290585; FBgn0011225. [Q01989-1]
DR EnsemblMetazoa; FBtr0334871; FBpp0306894; FBgn0011225. [Q01989-2]
DR EnsemblMetazoa; FBtr0334872; FBpp0306895; FBgn0011225. [Q01989-1]
DR GeneID; 42889; -.
DR KEGG; dme:Dmel_CG5695; -.
DR CTD; 42889; -.
DR FlyBase; FBgn0011225; jar.
DR VEuPathDB; VectorBase:FBgn0011225; -.
DR eggNOG; KOG0163; Eukaryota.
DR GeneTree; ENSGT00940000156078; -.
DR InParanoid; Q01989; -.
DR OMA; KAYMPDK; -.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q01989; -.
DR BioGRID-ORCS; 42889; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42889; -.
DR PRO; PR:Q01989; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011225; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q01989; baseline and differential.
DR Genevisible; Q01989; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0070865; C:investment cone; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0031476; C:myosin VI complex; IPI:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0070864; C:sperm individualization complex; IDA:FlyBase.
DR GO; GO:0016461; C:unconventional myosin complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IPI:FlyBase.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; IPI:FlyBase.
DR GO; GO:0070856; F:myosin VI light chain binding; IPI:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030048; P:actin filament-based movement; IDA:FlyBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0045175; P:basal protein localization; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0045217; P:cell-cell junction maintenance; TAS:FlyBase.
DR GO; GO:0019749; P:cytoskeleton-dependent cytoplasmic transport, nurse cell to oocyte; IDA:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:FlyBase.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:FlyBase.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:FlyBase.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0055057; P:neuroblast division; IMP:FlyBase.
DR GO; GO:0051647; P:nucleus localization; IMP:FlyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; IMP:FlyBase.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0032970; P:regulation of actin filament-based process; IMP:FlyBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01382; MYSc_Myo6; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR032412; Myosin-VI_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR036114; MYSc_Myo6.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16521; Myosin-VI_CBD; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1253
FT /note="Myosin heavy chain 95F"
FT /id="PRO_0000123389"
FT DOMAIN 3..54
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 57..766
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 808..837
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 647..666
FT /note="Actin-binding"
FT REGION 1187..1193
FT /note="Hydrophobic region"
FT REGION 1233..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 900..1022
FT /evidence="ECO:0000255"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VAR_SEQ 1047
FT /note="R -> SFSQVVSNIASRYLNK (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_003343"
FT VAR_SEQ 1048..1073
FT /note="SENVRAQQQALGKQKYDLSKWKYSEL -> YSTLYELPMSTTLVNFVNLFLL
FT SQKH (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_003344"
FT VAR_SEQ 1074..1253
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_003345"
FT CONFLICT 220
FT /note="V -> M (in Ref. 1; CAA47462)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="V -> L (in Ref. 1; CAA47462)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121
FT /note="R -> P (in Ref. 1; CAA47462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 143299 MW; 7586E03ECE8DCC59 CRC64;
MLEDTQLVWV RDAAEGYIQG RITEIGAKEF EVTPTDRKYP KRTCHFDDIH SSCDGPQDHD
DNCELMLLNE ATFLDNLKTR YYKDKIYTYV ANILIAVNPY REIKELYAPD TIKKYNGRSL
GELPPHVFAI ADKAIRDMRV YKLSQSIIVS GESGAGKTES TKYLLKYLCY SHDSAGPIET
KILDANPVLE AFGNAKTTRN NNSSRFGKFI EVHYDAKCQV VGGYISHYLL EKSRICTQSA
EERNYHVFYM LLAGAPQQLR DKLSLGKPDD YRYLSGCTQY FANAKTEQLI PGSQKSKNHQ
QKGPLKDPII DDYQHFHNLD KALGRLGLSD TEKLGIYSLV AAVLHLGNIA FEEIPDDVRG
GCQVSEASEQ SLTITSGLLG VDQTELRTAL VSRVMQSKGG GFKGTVIMVP LKIYEASNAR
DALAKAIYSR LFDRIVGLIN QSIPFQASNF YIGVLDIAGF EYFTVNSFEQ FCINYCNEKL
QKFFNDNILK NEQELYKREG LNVPEITFTD NQDIIELIEA KSNGIFTLLD EESKLPKPSY
SHFTAEVHKS WANHYRLGLP RSSRLKAHRT LRDEEGFLVR HFAGAVCYNT EQFIEKNNDA
LHASLEGLVQ ECDNPLLQTL FPSGSSTSVR GKLNFISVGS KFKTQLGELM EKLEQNGTNF
IRCIKPNSKM IDRQFEGSLA LAQLKCSGTI SVLELMEHGY PSRVLFADLY SMYKSVLPPE
LVSLPARTFC EAMFQSLNLS AKDFKFGITK VFFRPGKFVE FDRIMRSDPE NMLAIVAKVK
KWLIRSRWVK SALGALCVIK LRNRIIYRNK CVLIAQRIAR GFLARKQHRP RYQGIGKINK
IRTNTLKTIE IASGLKMGRE EIISGVNDIY RQIDDAIKKI KMNPRITQRE MDSMYTVVMA
NMNKLTVDLN TKLKEQQQAE EQERLRKIQE ALEAERAAKE AEEQRQREEI ENKRLKAEME
TRRKAAEAQR LRQEEEDRRA ALALQEQLEK EAKDDAKYRQ QLEQERRDHE LALRLANESN
GQVEDSPPVI RNGVNDASPM GPNKLIRSEN VRAQQQALGK QKYDLSKWKY SELRDAINTS
CDIELLEACR QEFHRRLKVY HAWKAKNRKR TTMDENERAP RSVMEAAFKQ PPLVQPIQEI
VTAQHRYFRI PFMRANAPDN TKRGLWYAHF DGQWIARQME LHADKPPILL VAGTDDMQMC
ELSLEETGLT RKRGAEILEH EFNREWERNG GKAYKNLGAA KPNGPAAAMQ KQQ
