DMDD_DROME
ID DMDD_DROME Reviewed; 1854 AA.
AC Q0KI50; Q2VQZ5; Q6IJP4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Dystrophin, isoform D {ECO:0000303|PubMed:10731132, ECO:0000303|PubMed:17543506};
DE AltName: Full=Protein detached {ECO:0000250|UniProtKB:Q9VDW6};
GN Name=Dys; Synonyms=det; ORFNames=CG34157;
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:AAX59985.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16198353; DOI=10.1016/j.febslet.2005.08.073;
RA Neuman S., Kovalio M., Yaffe D., Nudel U.;
RT "The Drosophila homologue of the dystrophin gene - introns containing
RT promoters are the major contributors to the large size of the gene.";
RL FEBS Lett. 579:5365-5371(2005).
RN [2] {ECO:0000312|EMBL:ABI31177.1}
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] {ECO:0000305, ECO:0000312|EMBL:ABI31177.1}
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] {ECO:0000305, ECO:0000312|EMBL:DAA04178.1}
RP IDENTIFICATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16399704; DOI=10.1523/jneurosci.4069-05.2006;
RA van der Plas M.C., Pilgram G.S.K., Plomp J.J., de Jong A., Fradkin L.G.,
RA Noordermeer J.N.;
RT "Dystrophin is required for appropriate retrograde control of
RT neurotransmitter release at the Drosophila neuromuscular junction.";
RL J. Neurosci. 26:333-344(2006).
RN [6] {ECO:0000305}
RP INTERACTION WITH DG.
RX PubMed=17355978; DOI=10.1074/jbc.m608800200;
RA Yatsenko A.S., Gray E.E., Shcherbata H.R., Patterson L.B., Sood V.D.,
RA Kucherenko M.M., Baker D., Ruohola-Baker H.;
RT "A putative Src homology 3 domain binding motif but not the C-terminal
RT dystrophin WW domain binding motif is required for dystroglycan function in
RT cellular polarity in Drosophila.";
RL J. Biol. Chem. 282:15159-15169(2007).
RN [7] {ECO:0000305}
RP FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17543506; DOI=10.1016/j.mod.2007.04.003;
RA van der Plas M.C., Pilgram G.S.K., de Jong A.W.M., Bansraj M.R.K.S.,
RA Fradkin L.G., Noordermeer J.N.;
RT "Drosophila Dystrophin is required for integrity of the musculature.";
RL Mech. Dev. 124:617-630(2007).
RN [8] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for the maintenance of appropriate synaptic
CC retrograde communication and the stabilization of muscle cell
CC architecture or physiology. May play a role in anchoring the
CC cytoskeleton to the plasma membrane. {ECO:0000269|PubMed:17543506}.
CC -!- SUBUNIT: Component of the dystrophin associated protein complex (DAPC).
CC Interacts with Dg, via the Dg WW domain binding sites.
CC {ECO:0000269|PubMed:17355978}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:16399704}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16399704}; Cytoplasmic side
CC {ECO:0000269|PubMed:16399704}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16399704}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=D {ECO:0000269|PubMed:10731132}; Synonyms=Dp205
CC {ECO:0000269|PubMed:17543506};
CC IsoId=Q0KI50-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132}; Synonyms=DLP2
CC {ECO:0000250|UniProtKB:Q9VDW6};
CC IsoId=Q9VDW6-1; Sequence=External;
CC Name=B {ECO:0000269|PubMed:10731132}; Synonyms=Dp186
CC {ECO:0000250|UniProtKB:Q9VDW3};
CC IsoId=Q9VDW3-1; Sequence=External;
CC Name=C {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VDW6-2; Sequence=External;
CC Name=E {ECO:0000269|PubMed:10731132}; Synonyms=Dp117
CC {ECO:0000269|PubMed:17543506};
CC IsoId=Q7YU29-1; Sequence=External;
CC Name=F {ECO:0000269|PubMed:10731132}; Synonyms=DLP1
CC {ECO:0000250|UniProtKB:Q9VDW6};
CC IsoId=Q9VDW6-3; Sequence=External;
CC Name=G {ECO:0000269|PubMed:10731132}; Synonyms=DLP3
CC {ECO:0000250|UniProtKB:Q9VDW6};
CC IsoId=Q9VDW6-4; Sequence=External;
CC Name=H {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VDW6-5; Sequence=External;
CC -!- TISSUE SPECIFICITY: During embryogenesis and in third instar larvae,
CC expression is seen in pericardial cells of the dorsal vessel and in the
CC ventral nerve cord. Expression is absent from both the embryonic and
CC larval musculature. {ECO:0000269|PubMed:17543506}.
CC -!- DISRUPTION PHENOTYPE: Flies that have reduced expression of all
CC isoforms (due to transgenic RNA interference targeting the common C-
CC terminal region) exhibit severe muscle degeneration in larvae and adult
CC flies. Muscles were either ruptured, absent, or the fibers were
CC detached from their attachment sites at tendon cells. These are
CC necrotic, not apoptotic processes. {ECO:0000269|PubMed:17543506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA04178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY875639; AAX59985.1; -; mRNA.
DR EMBL; AE014297; ABI31177.1; -; Genomic_DNA.
DR EMBL; BK002672; DAA04178.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001036725.1; NM_001043260.2. [Q0KI50-1]
DR AlphaFoldDB; Q0KI50; -.
DR SMR; Q0KI50; -.
DR BioGRID; 67322; 74.
DR IntAct; Q0KI50; 5.
DR iPTMnet; Q0KI50; -.
DR PRIDE; Q0KI50; -.
DR DNASU; 42327; -.
DR EnsemblMetazoa; FBtr0110915; FBpp0110215; FBgn0260003. [Q0KI50-1]
DR GeneID; 42327; -.
DR UCSC; CG34157-RD; d. melanogaster. [Q0KI50-1]
DR CTD; 42327; -.
DR FlyBase; FBgn0260003; Dys.
DR VEuPathDB; VectorBase:FBgn0260003; -.
DR GeneTree; ENSGT00940000166230; -.
DR HOGENOM; CLU_236807_0_0_1; -.
DR BioGRID-ORCS; 42327; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42327; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0260003; Expressed in spermathecum and 62 other tissues.
DR ExpressionAtlas; Q0KI50; baseline and differential.
DR Genevisible; Q0KI50; DM.
DR GO; GO:0005938; C:cell cortex; HDA:FlyBase.
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:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IPI:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IMP:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:FlyBase.
DR GO; GO:0050699; F:WW domain binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IDA:FlyBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:FlyBase.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:FlyBase.
DR CDD; cd00176; SPEC; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 3.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1854
FT /note="Dystrophin, isoform D"
FT /id="PRO_0000365454"
FT REPEAT 936..1069
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 1072..1176
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1206..1239
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 1464..1520
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1564
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 972
FT /note="V -> A (in Ref. 1; AAX59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="T -> R (in Ref. 1; AAX59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="I -> L (in Ref. 1; AAX59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="E -> Q (in Ref. 1; AAX59985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1854 AA; 205723 MW; 1264435B6A5ECF2E CRC64;
MTTTITAKIA QRQQQHQQHQ QQQLQHQQQQ QQQQQHQPTS SMNGFRITGY PAAATPPARS
NPIYAKPNAH ELDLHISESL LYPGSTTQQQ QALQSSPGPP PQLTSMLPSS GLPGAAQPIA
LKGNNPFLNS PSPTEAAPGV PTGLSSAQPA TSASSGNYEM PEYAEPSRLR GLKQRPHSIA
VGGSPAQSSF VDYNAQQQQR LLQLSRQQQQ LRNAVTAAAS TANGGDKETL YAALFQQYRQ
SPTNGQPAPP VPLHRKPAAA PVVPRRSQST PRPPLQQQQQ QQQAGINGQI NGNGNQRPRS
LDRFNGGLQS EAPPIPLRRF PNGNGNNNNG TLSRQKSPKK SSSADNMLMS PAGSQVNTMR
HSISFHGGQE TENGSKAEQT RPMSYAAPAP DQAYLEHQLR AYSEQLRTIT ESVRKYSEQA
KLLSELKRQQ QLAKQSQTNL NLLTPTTCNN STGSNGNNNF QPNMISPEIV SKSLASLSTS
QANEAQTPSN QLRLFLDNIR SSMRQEYQQH MPDDVLKPTS TLKRNGTDSL VTSNTAAKPE
VEATPTPSDQ LRQFLDAIRA NKIPESVDKP KMTSSQTLDS FISKPLQMPD VTSGTPGGGV
VGGQAASGGV AVNGQTNGIP TRRRPKSSII PSSSNGKLEQ REHSLVTSES FHQISDNLRL
MSEDLQALSP SKAIPSSASS NSLKSLAANG GSSLTTELRV ITSSPYSTSP KLQQMVMSKS
NSSLGSVTTP SSATTTPSTA PMITDFNEIL DSFQAMADKY KSKGSYDYLR KCSEALRQHS
LQLKLQQQHQ AHQQQQLPAH QQQQHQQQQQ QQIQNGFASD DNSSSCSTTP GSIREAVQNL
LLQPRNGFQI LDDRMRLFID IIDSQDRLSQ DLQSEIETHR VVYDRLDGTG RKLLGSLTSQ
EDAVMLQRRL DEMNQRWNNL KSKSIAIRNR LESNSEHWNA LLLSLRELTE WVIRKDTELS
TLGLGPVRGD AVSLQKQLDD HKAFRRQLED KRPIVESNLT SGRQYIANEA AVSDTSDTEA
NHDSDSRYMS AEEQSRELTR SIRREVGKLS EQWNNLIDRS DNWKHRLDEY MTKMRQFQKI
LEDLSSRVAL AEQTKTSWLP PSSVGEANEQ MQQLQRLRDK MTTASALLDD CNEQQSFFTA
NQVLVPTPCL SKLEDLNTRM KLLQIAMDER QKVLCQAGAQ QTHENGDDGR TTSNSGTIGP
LPNLGQSVKP PWERATTAAN VPYYIDHERE TTHWDHPEMI ELMKGLADLN EIRFSAYRTA
MKLRSVQKRL ALDRISMSTA CESFDRHGLR AQNDKLIDIP DMTTVLHSLY VTIDKIDLTL
MLDLAINWIL NVYDSQRTGQ IRVLSFKVGL VLLCKGHLEE KYRYLFRLVA DTDRRADQRR
LGLLLHDCIQ VPRQLGEVAA FGGSNIEPSV RSCLEQAGIS QEAIDGNQDI SIELQHFLGW
LQHEPQSLVW LPVLHRLAAA EAAKHQAKCN ICKEYPIVGF RYRCLKCFNF DMCQKCFFFG
RNAKNHKLTH PMHEYCTTTT STEDVRDFTR ALKNKFKSRK YFKKHPRVGY LPVQSVLEGD
ALESPAPSPQ HTTHQLQNDM HSRLEMYASR LAQVEYGGTG SNSTPDSDDE HQLIAQYCQA
LPGTSNGSAP KSPVQVMAAM DAEQREELEA IIRDLEEENA NLQAEYQQLC SKEQSGMPED
SNGMQHSSSS MTGLSGQGEQ GQDMMAEAKL LRQHKGRLEA RMQILEDHNR QLEAQLQRLR
QLLDEPNGGG SSATSSGLPS APGSALNSKP NTLQTRSVTA SQLNTDSPAK MNQQNGHYEH
NSKNSSGLVT VITEQELESI NDDLEDSSSS NTTNTTTTTT TTATTEKTCV ELQK
