ACTN_DROME
ID ACTN_DROME Reviewed; 924 AA.
AC P18091; O46044; O46045; Q24370; Q8T024; Q9W536; Q9W537;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Alpha-actinin, sarcomeric;
DE AltName: Full=F-actin cross-linking protein;
GN Name=Actn; Synonyms=fliA, l(1)2Cb; ORFNames=CG4376;
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 ADULT MUSCLE), AND FUNCTION.
RC STRAIN=Canton-S;
RX PubMed=2112549; DOI=10.1083/jcb.110.6.1999;
RA Fyrberg E.A., Kelly M., Ball E., Fyrberg C., Reedy M.C.;
RT "Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z
RT disc integrity and muscle insertions.";
RL J. Cell Biol. 110:1999-2011(1990).
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 GENOMIC DNA] (ISOFORMS LONG AND ADULT
RP MUSCLE).
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 229-286 (ISOFORM NON-MUSCLE), ALTERNATIVE
RP SPLICING, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1734023; DOI=10.1083/jcb.116.4.911;
RA Roulier E.M., Fyrberg C., Fyrberg E.;
RT "Perturbations of Drosophila alpha-actinin cause muscle paralysis,
RT weakness, and atrophy but do not confer obvious nonmuscle phenotypes.";
RL J. Cell Biol. 116:911-922(1992).
RN [7]
RP INTERACTION WITH SMN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17353360; DOI=10.1083/jcb.200610053;
RA Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K.,
RA Matera A.G.;
RT "A Drosophila melanogaster model of spinal muscular atrophy reveals a
RT function for SMN in striated muscle.";
RL J. Cell Biol. 176:831-841(2007).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein. {ECO:0000269|PubMed:1734023, ECO:0000269|PubMed:2112549}.
CC -!- SUBUNIT: Homodimer; antiparallel. Interacts with Smn; the interaction
CC occurs in adult thoracic tissues. {ECO:0000269|PubMed:17353360}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:17353360}. Note=Colocalizes with Smn at the Z-line
CC of indirect flight muscles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=Long;
CC IsoId=P18091-1; Sequence=Displayed;
CC Name=Non-muscle;
CC IsoId=P18091-2; Sequence=VSP_000712, VSP_000714;
CC Name=Larval muscle; Synonyms=C;
CC IsoId=P18091-3; Sequence=VSP_000716;
CC Name=Adult muscle; Synonyms=B;
CC IsoId=P18091-4; Sequence=VSP_000715;
CC Name=A;
CC IsoId=P18091-5; Sequence=VSP_000713;
CC -!- TISSUE SPECIFICITY: Larval muscle isoform is expressed in the larval
CC body wall, adult muscles of the head and abdomen and supercontractile
CC muscles of the larva and adult. Adult muscle isoform accumulates within
CC adult fibrillar and tubular muscles. {ECO:0000269|PubMed:1734023,
CC ECO:0000269|PubMed:17353360}.
CC -!- DEVELOPMENTAL STAGE: Larval muscle isoform is found in the larvae and
CC adults, the adult muscle isoform in adults only.
CC {ECO:0000269|PubMed:1734023}.
CC -!- SIMILARITY: Belongs to the alpha-actinin 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; X51753; CAA36042.1; -; mRNA.
DR EMBL; AE014298; AAF45705.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45706.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09068.1; -; Genomic_DNA.
DR EMBL; AL009192; CAA15688.1; -; Genomic_DNA.
DR EMBL; AL031765; CAA15688.1; JOINED; Genomic_DNA.
DR EMBL; AL009192; CAA15689.1; -; Genomic_DNA.
DR EMBL; AL031765; CAA15689.1; JOINED; Genomic_DNA.
DR EMBL; AL031765; CAA21120.1; -; Genomic_DNA.
DR EMBL; AL009192; CAA21120.1; JOINED; Genomic_DNA.
DR EMBL; AL031765; CAA21121.1; -; Genomic_DNA.
DR EMBL; AL009192; CAA21121.1; JOINED; Genomic_DNA.
DR EMBL; AY069615; AAL39760.1; -; mRNA.
DR EMBL; X64419; CAA45764.1; -; mRNA.
DR PIR; A35598; FAFFAA.
DR PIR; T13413; T13413.
DR PIR; T13414; T13414.
DR RefSeq; NP_001188532.1; NM_001201603.2. [P18091-4]
DR RefSeq; NP_001188533.1; NM_001201604.2. [P18091-4]
DR RefSeq; NP_001259165.1; NM_001272236.1. [P18091-3]
DR RefSeq; NP_001259166.1; NM_001272237.1. [P18091-3]
DR RefSeq; NP_001259167.1; NM_001272238.1. [P18091-3]
DR RefSeq; NP_477484.2; NM_058136.4. [P18091-5]
DR RefSeq; NP_477485.1; NM_058137.6. [P18091-3]
DR RefSeq; NP_726784.1; NM_166920.2. [P18091-4]
DR AlphaFoldDB; P18091; -.
DR SMR; P18091; -.
DR BioGRID; 57710; 45.
DR DIP; DIP-22313N; -.
DR IntAct; P18091; 12.
DR STRING; 7227.FBpp0070331; -.
DR PaxDb; P18091; -.
DR PRIDE; P18091; -.
DR EnsemblMetazoa; FBtr0070343; FBpp0070329; FBgn0000667. [P18091-4]
DR EnsemblMetazoa; FBtr0070344; FBpp0070330; FBgn0000667. [P18091-5]
DR EnsemblMetazoa; FBtr0070345; FBpp0070331; FBgn0000667. [P18091-3]
DR EnsemblMetazoa; FBtr0303048; FBpp0292167; FBgn0000667. [P18091-4]
DR EnsemblMetazoa; FBtr0310658; FBpp0302778; FBgn0000667. [P18091-3]
DR EnsemblMetazoa; FBtr0310659; FBpp0302779; FBgn0000667. [P18091-3]
DR EnsemblMetazoa; FBtr0333801; FBpp0305935; FBgn0000667. [P18091-4]
DR EnsemblMetazoa; FBtr0333802; FBpp0305936; FBgn0000667. [P18091-3]
DR GeneID; 31166; -.
DR KEGG; dme:Dmel_CG4376; -.
DR CTD; 31166; -.
DR FlyBase; FBgn0000667; Actn.
DR VEuPathDB; VectorBase:FBgn0000667; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000155548; -.
DR InParanoid; P18091; -.
DR OMA; QRFENVN; -.
DR PhylomeDB; P18091; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; P18091; -.
DR BioGRID-ORCS; 31166; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Actn; fly.
DR GenomeRNAi; 31166; -.
DR PRO; PR:P18091; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000667; Expressed in crop (Drosophila) and 36 other tissues.
DR ExpressionAtlas; P18091; baseline and differential.
DR Genevisible; P18091; DM.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IDA:FlyBase.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cytoplasm; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..924
FT /note="Alpha-actinin, sarcomeric"
FT /id="PRO_0000073447"
FT DOMAIN 34..138
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 147..253
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 251..395
FT /note="Spectrin 1"
FT REPEAT 396..510
FT /note="Spectrin 2"
FT REPEAT 511..631
FT /note="Spectrin 3"
FT REPEAT 632..744
FT /note="Spectrin 4"
FT DOMAIN 778..813
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 819..854
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..250
FT /note="Actin-binding"
FT BINDING 791
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 797
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 802
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 229..260
FT /note="Missing (in isoform Non-muscle)"
FT /evidence="ECO:0000303|PubMed:1734023"
FT /id="VSP_000712"
FT VAR_SEQ 231..260
FT /note="INTPKPDERAIMTYVSCYYHAFQGAQQVGN -> Q (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_000713"
FT VAR_SEQ 258..286
FT /note="Missing (in isoform Adult muscle)"
FT /evidence="ECO:0000303|PubMed:2112549"
FT /id="VSP_000715"
FT VAR_SEQ 261..286
FT /note="NTALPDERAVMTYVSSYYHCFSGAQK -> VTHVPEPTRQYTYVPNNYN
FT (in isoform Larval muscle)"
FT /evidence="ECO:0000305"
FT /id="VSP_000716"
FT VAR_SEQ 261
FT /note="N -> Q (in isoform Non-muscle)"
FT /evidence="ECO:0000303|PubMed:1734023"
FT /id="VSP_000714"
FT CONFLICT 409
FT /note="A -> G (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="C -> Y (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> C (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> C (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="E -> V (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="L -> R (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 684..691
FT /note="AVTAIGMG -> VVTPLVWD (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="Y -> H (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="D -> E (in Ref. 1; CAA36042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 924 AA; 107019 MW; 08F8961520328ACE CRC64;
MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK AGTAIDNIEE
DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL DFIASKGVHL VSIGAEEIVD
GNLKMTLGMI WTIILRFAIQ DISVEEMTAK EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL
AFCALIHRHR PDLIDYAKLS KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA
IMTYVSCYYH AFQGAQQVGN NTALPDERAV MTYVSSYYHC FSGAQKAETA ANRICKVLKV
NQENERLMEE YERLASDLLE WIRRTMPWLN SRQADNSLAG VQKKLEEYRT YRRKHKPPRV
EQKAKLETNF NTLQTKLRLS NRPAYLPTEG KTVSDISNSW KGLELAEKAF EEWLLAETMR
LERLEHLAQK FKHKADAHED WTRGKEEMLQ SQDFRQCKLN ELKALKKKHE AFESDLAAHQ
DRVEQIAAIA QELNTLEYHD CVSVNARCQR ICDQWDRLGA LTQRRRTALD EAERILEKID
ILHLEFAKRA APFNNWLDGT REDLVDMFIV HTMEEIQGLI QAHDQFKATL GEADKEFNLI
VNLVREVESI VKQHQIPGGL ENPYTTLTAN DMTRKWSDVR QLVPQRDQTL ANELRKQQNN
EMLRRQFAEK ANIVGPWIER QMDAVTAIGM GLQGSLEDQL HRLKEYEQAV YAYKPNIEEL
EKIHQAVQES MIFENRYTNY TMETLRVGWE QLLTSINRNI NEVENQILTR DSKGISQEQL
NEFRSSFNHF DKNRTGRLSP EEFKSCLVSL GYSIGKDRQG DLDFQRILAV VDPNNTGYVH
FDAFLDFMTR ESTDTDTAEQ VIDSFRILAA DKPYILPDEL RRELPPDQAE YCIQRMPPYK
GPNGVPGALD YMSFSTALYG ETDL
