DMDB_DROME
ID DMDB_DROME Reviewed; 1669 AA.
AC Q9VDW3; O62529; Q9BK99;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dystrophin, isoform B;
DE AltName: Full=Protein detached;
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 {ECO:0000312|EMBL:AAF55676.3};
RN [1] {ECO:0000312|EMBL:AAK15257.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11223239; DOI=10.1016/s0378-1119(00)00584-9;
RA Neuman S., Kaban A., Volk T., Yaffe D., Nudel U.;
RT "The dystrophin / utrophin homologues in Drosophila and in sea urchin.";
RL Gene 263:17-29(2001).
RN [2] {ECO:0000305}
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 [3] {ECO:0000305}
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}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 643-1598.
RX PubMed=9499411; DOI=10.1093/hmg/7.4.589;
RA Roberts R.G., Bobrow M.;
RT "Dystrophins in vertebrates and invertebrates.";
RL Hum. Mol. Genet. 7:589-595(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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]
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]
RP FUNCTION, AND DISRUPTION 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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
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:16399704,
CC 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=B {ECO:0000303|PubMed:10731132}; Synonyms=Dp186;
CC IsoId=Q9VDW3-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:11223239}; Synonyms=DLP2
CC {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-1; Sequence=External;
CC Name=C {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VDW6-2; Sequence=External;
CC Name=D; Synonyms=Dp205;
CC IsoId=Q0KI50-1; Sequence=External;
CC Name=E; Synonyms=Dp117;
CC IsoId=Q7YU29-1; Sequence=External;
CC Name=F; Synonyms=DLP1 {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-3; Sequence=External;
CC Name=G; Synonyms=DLP3 {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-4; Sequence=External;
CC Name=H;
CC IsoId=Q9VDW6-5; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in neuronally derived tissues, mainly the
CC CNS and the brain of stage 16 embryos. Lower level expression is seen
CC in the sensory organs. Expression is absent from the musculature. In
CC larvae, expression is predominant throughout the neuropil and brain and
CC in the eye antennal disks. {ECO:0000269|PubMed:11223239,
CC ECO:0000269|PubMed:16399704}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:11223239,
CC ECO:0000269|PubMed:16399704}.
CC -!- DISRUPTION PHENOTYPE: Flies that have reduced expression of all
CC isoforms (transgenic RNA interference targeting the common C-terminal
CC region) exhibit severe muscle degeneration in larvae and adult flies.
CC Muscles were either ruptured, absent or the fibers were detached from
CC their attachment sites at tendon cells. These are necrotic, not
CC apoptotic processes. {ECO:0000269|PubMed:17543506}.
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; AF300294; AAK15257.1; -; mRNA.
DR EMBL; AE014297; AAF55676.3; -; Genomic_DNA.
DR EMBL; X99757; CAA68088.1; -; mRNA.
DR RefSeq; NP_001036721.1; NM_001043256.2. [Q9VDW3-1]
DR AlphaFoldDB; Q9VDW3; -.
DR SMR; Q9VDW3; -.
DR BioGRID; 67322; 74.
DR IntAct; Q9VDW3; 2.
DR iPTMnet; Q9VDW3; -.
DR PRIDE; Q9VDW3; -.
DR DNASU; 42327; -.
DR EnsemblMetazoa; FBtr0083766; FBpp0083180; FBgn0260003. [Q9VDW3-1]
DR GeneID; 42327; -.
DR KEGG; dme:Dmel_CG34157; -.
DR CTD; 42327; -.
DR FlyBase; FBgn0260003; Dys.
DR VEuPathDB; VectorBase:FBgn0260003; -.
DR GeneTree; ENSGT00940000166230; -.
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; Q9VDW3; baseline and differential.
DR Genevisible; Q9VDW3; 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; 2.
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; IPR002017; Spectrin_repeat.
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; PF00435; Spectrin; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 4.
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..1669
FT /note="Dystrophin, isoform B"
FT /id="PRO_0000076081"
FT REPEAT 541..643
FT /note="Spectrin 1"
FT REPEAT 650..747
FT /note="Spectrin 2"
FT REPEAT 754..883
FT /note="Spectrin 3"
FT REPEAT 890..990
FT /note="Spectrin 4"
FT DOMAIN 1021..1054
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224,
FT ECO:0000305"
FT ZN_FING 1279..1335
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1379
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 643..644
FT /note="HA -> PR (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="D -> N (in Ref. 1; AAK15257)"
FT /evidence="ECO:0000305"
FT CONFLICT 734..736
FT /note="NLK -> DLR (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="I -> M (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="T -> S (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 783..784
FT /note="RG -> LT (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="V -> A (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="T -> R (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="I -> L (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="M -> L (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="K -> E (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 923..930
FT /note="NEQMQQLQ -> ISRCNSCS (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="Q -> E (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 990..1000
FT /note="CQAGAQQTHEN -> RQVEPSRRTRG (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="E -> Q (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102..1106
FT /note="HGLRA -> TWPAC (in Ref. 1; AAK15257 and 4;
FT CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="K -> E (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="K -> E (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="G -> L (in Ref. 1; AAK15257 and 4; CAA68088)"
FT /evidence="ECO:0000305"
FT CONFLICT 1596..1598
FT /note="SQL -> LRN (in Ref. 4; CAA68088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1669 AA; 185311 MW; B264332783162291 CRC64;
MTAKPPPPIP PTLGGDDSGT HGPKLAPEIP RINSELAAQA ALRGQQLLRK QGSQEQHATN
TLPAHKTGAP PPLPPTQSRP VPAIPARGAS DRAAPPEIPP KRHSLKSMPD GQPMMVPGLP
PTMRQPPPLP RKPASTQSSA QNSAQSSPLA GMKFKDKPPP PPEKHSTLSA EGMAARRCSN
PFEMPPPPPP LVLQSAVAAL SEQSSKNGLN PVPSPAPTRA SEAKKINQRS IASPTEEFGS
EDALRGIESG LRNMERAMQE QMNLRNMEAA VQNNFDLSFK ASLAAGARHL GGGSVNLRTA
NYERNLSLDE GRAGDSRQSL EELKQLRAQA QQQSLLNNSS SSSSNSQVEQ SMRSTIEHHM
RSLDRNLPLE LQYSRHRFQN NLNAVAAAGG GGGNSSTGNA VANSGTSGSQ QPPMPLSSEF
REQIRQQLLG NIPPQVVHNM GQSPGSAAAA ALLQHQAQSR AAAAAAAAAA AAAAAQVAAG
SGALSREELR MRRRSSHDET QLTQNSSGGI QVTRLREHWD ETSQCVLQRA AQLKNMLSDS
QRFEAKRLEL EKWLARMEQR AERMGTIATT ADILEAQQKE QKSFHAELHQ NKQHFDIFNE
LTQKLIAVYP NDDTTRIKKM TEVINQRYAN LNSGVINRGK QLHAAVHSLQ SFDRAMDQFL
AFLSETETLC ENAESDIERN PLMFKDLQSE IETHRVVYDR LDGTGRKLLG SLTSQEDAVM
LQRRLDEMNQ RWNNLKSKSI AIRNRLESNS EHWNALLLSL RELTEWVIRK DTELSTLGLG
PVRGDAVSLQ KQLDDHKAFR RQLEDKRPIV ESNLTSGRQY IANEAAVSDT SDTEANHDSD
SRYMSAEEQS RELTRSIRRE VGKLSEQWNN LIDRSDNWKH RLDEYMTKMR QFQKILEDLS
SRVALAEQTK TSWLPPSSVG EANEQMQQLQ RLRDKMTTAS ALLDDCNEQQ SFFTANQVLV
PTPCLSKLED LNTRMKLLQI AMDERQKVLC QAGAQQTHEN GDDGRTTSNS GTIGPLPNLG
QSVKPPWERA TTAANVPYYI DHERETTHWD HPEMIELMKG LADLNEIRFS AYRTAMKLRS
VQKRLALDRI SMSTACESFD RHGLRAQNDK LIDIPDMTTV LHSLYVTIDK IDLTLMLDLA
INWILNVYDS QRTGQIRVLS FKVGLVLLCK GHLEEKYRYL FRLVADTDRR ADQRRLGLLL
HDCIQVPRQL GEVAAFGGSN IEPSVRSCLE QAGISQEAID GNQDISIELQ HFLGWLQHEP
QSLVWLPVLH RLAAAEAAKH QAKCNICKEY PIVGFRYRCL KCFNFDMCQK CFFFGRNAKN
HKLTHPMHEY CTTTTSTEDV RDFTRALKNK FKSRKYFKKH PRVGYLPVQS VLEGDALESP
APSPQHTTHQ LQNDMHSRLE MYASRLAQVE YGGTGSNSTP DSDDEHQLIA QYCQALPGTS
NGSAPKSPVQ VMAAMDAEQR EELEAIIRDL EEENANLQAE YQQLCSKEQS GMPEDSNGMQ
HSSSSMTGLS GQGEQGQDMM AEAKLLRQHK GRLEARMQIL EDHNRQLEAQ LQRLRQLLDE
PNGGGSSATS SGLPSAPGSA LNSKPNTLQT RSVTASQLNT DSPAKMNQQN GHYEHNSKNS
SGLVTVITEQ ELESINDDLE DSSSSNTTNT TTTTTTTATT EKTCVELQK
