DMDE_DROME
ID DMDE_DROME Reviewed; 1051 AA.
AC Q7YU29;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dystrophin, isoform E {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:ABI31179.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABI31179.1};
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 [2] {ECO:0000305, ECO:0000312|EMBL:ABI31179.1}
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 [3] {ECO:0000312|EMBL:AAQ22489.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22489.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {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 [5] {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 [6] {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 [7] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761, 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: Specifically required for survival and integrity of the
CC larval musculature: the maintenance of appropriate synaptic retrograde
CC communication and the stabilization of muscle cell architecture or
CC physiology. May play a role in anchoring the cytoskeleton to the plasma
CC 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=E {ECO:0000269|PubMed:10731132}; Synonyms=Dp117
CC {ECO:0000269|PubMed:17543506};
CC IsoId=Q7YU29-1; 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=D {ECO:0000269|PubMed:10731132}; Synonyms=Dp205
CC {ECO:0000269|PubMed:17543506};
CC IsoId=Q0KI50-1; 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: Expressed predominantly in all body wall muscle
CC fibers during embryogenesis and in third instar larvae. Expression is
CC also seen in the embryonic and larval ventral midline and larval brain.
CC {ECO:0000269|PubMed:17543506}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit muscle degeneration and lethality.
CC Flies that have reduced expression of all isoforms (due to transgenic
CC RNA interference targeting the common C-terminal region) exhibit severe
CC muscle degeneration in larvae and adult flies. Muscles were either
CC ruptured, absent or the fibers were detached from their attachment
CC sites at tendon cells. These are necrotic, not apoptotic processes.
CC {ECO:0000269|PubMed:17543506}.
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DR EMBL; AE014297; ABI31179.1; -; Genomic_DNA.
DR EMBL; BT010020; AAQ22489.1; -; mRNA.
DR RefSeq; NP_001036727.1; NM_001043262.2. [Q7YU29-1]
DR AlphaFoldDB; Q7YU29; -.
DR SMR; Q7YU29; -.
DR BioGRID; 67322; 74.
DR iPTMnet; Q7YU29; -.
DR DNASU; 42327; -.
DR EnsemblMetazoa; FBtr0110916; FBpp0110216; FBgn0260003. [Q7YU29-1]
DR GeneID; 42327; -.
DR UCSC; CG34157-RE; d. melanogaster. [Q7YU29-1]
DR CTD; 42327; -.
DR FlyBase; FBgn0260003; Dys.
DR VEuPathDB; VectorBase:FBgn0260003; -.
DR GeneTree; ENSGT00940000166230; -.
DR HOGENOM; CLU_001187_1_1_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; Q7YU29; baseline and differential.
DR Genevisible; Q7YU29; 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; 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; 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; 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 Zinc; Zinc-finger.
FT CHAIN 1..1051
FT /note="Dystrophin, isoform E"
FT /id="PRO_0000365455"
FT DOMAIN 403..436
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 661..717
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1051 AA; 116741 MW; E78A8A1C2232E778 CRC64;
MRLFASSGQA ATSPALAHSS SDEAGEVIEN SHTKRAGCSV LQSSGGKSRS LERYSGAPKI
HQQTLEMLPP YATPTCSTRR RLLAPFRSLK RRSRSSSSSN ESHHFGNHLN NLVVVNVGAA
AANGGVAKAK AKASSQSGDS GTGGTELEHE MEQDDDEEDE EEGEEMDELS LSYSQLSSSG
CEEAEAPPED VPDDRQAAVE ATVSACVQHV ANERRRNILS LYSSSSEEQL HCRLGDITLV
DDTYSNYDPQ NDAERMFLQV VGILRDENEK MRQFQKILED LSSRVALAEQ TKTSWLPPSS
VGEANEQMQQ LQRLRDKMTT ASALLDDCNE QQSFFTANQV LVPTPCLSKL EDLNTRMKLL
QIAMDERQKV LCQAGAQQTH ENGDDGRTTS NSGTIGPLPN LGQSVKPPWE RATTAANVPY
YIDHERETTH WDHPEMIELM KGLADLNEIR FSAYRTAMKL RSVQKRLALD RISMSTACES
FDRHGLRAQN DKLIDIPDMT TVLHSLYVTI DKIDLTLMLD LAINWILNVY DSQRTGQIRV
LSFKVGLVLL CKGHLEEKYR YLFRLVADTD RRADQRRLGL LLHDCIQVPR QLGEVAAFGG
SNIEPSVRSC LEQAGISQEA IDGNQDISIE LQHFLGWLQH EPQSLVWLPV LHRLAAAEAA
KHQAKCNICK EYPIVGFRYR CLKCFNFDMC QKCFFFGRNA KNHKLTHPMH EYCTTTTSTE
DVRDFTRALK NKFKSRKYFK KHPRVGYLPV QSVLEGDALE SPAPSPQHTT HQLQNDMHSR
LEMYASRLAQ VEYGGTGSNS TPDSDDEHQL IAQYCQALPG TSNGSAPKSP VQVMAAMDAE
QREELEAIIR DLEEENANLQ AEYQQLCSKE QSGMPEDSNG MQHSSSSMTG LSGQGEQGQD
MMAEAKLLRQ HKGRLEARMQ ILEDHNRQLE AQLQRLRQLL DEPNGGGSSA TSSGLPSAPG
SALNSKPNTL QTRSVTASQL NTDSPAKMNQ QNGHYEHNSK NSSGLVTVIT EQELESINDD
LEDSSSSNTT NTTTTTTTTA TTEKTCVELQ K
