DMDA_DROME
ID DMDA_DROME Reviewed; 3598 AA.
AC Q9VDW6; Q0KI51; Q0KI52; Q0KI53; Q9BK96; Q9BK98; Q9BKA0; Q9GT71; Q9VDW4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Dystrophin, isoforms A/C/F/G/H;
DE Short=DmDYS;
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:AAF55673.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND SUBUNIT.
RX PubMed=11018515; DOI=10.1016/s0014-5793(00)02018-4;
RA Greener M.J., Roberts R.G.;
RT "Conservation of components of the dystrophin complex in Drosophila.";
RL FEBS Lett. 482:13-18(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; F AND G), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
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 [3] {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 [4] {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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18093579; DOI=10.1016/j.ydbio.2007.09.044;
RA Christoforou C.P., Greer C.E., Challoner B.R., Charizanos D., Ray R.P.;
RT "The detached locus encodes Drosophila Dystrophin, which acts with other
RT components of the Dystrophin Associated Protein Complex to influence
RT intercellular signalling in developing wing veins.";
RL Dev. Biol. 313:519-532(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1832; SER-1838 AND SER-3207,
RP AND IDENTIFICATION BY 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. Both det and Dg are required for
CC maintenance of early dpp signaling in the presumptive crossvein.
CC Isoform A is not required to maintain muscle integrity, but plays a
CC role in neuromuscular homeostasis by regulating neurotransmitter
CC release. May play a role in anchoring the cytoskeleton to the plasma
CC membrane. {ECO:0000269|PubMed:16399704, ECO:0000269|PubMed:17543506,
CC ECO:0000269|PubMed:18093579}.
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:11018515, 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}. Note=Isoform A is localized to both the
CC postsynaptic region of the NMJ and to the extrasynaptic regions, where
CC it colocalizes with actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=H;
CC IsoId=Q9VDW6-5; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:11223239}; Synonyms=DLP2
CC {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-1; Sequence=VSP_036500;
CC Name=C {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VDW6-2; Sequence=VSP_050731, VSP_050732;
CC Name=F; Synonyms=DLP1 {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-3; Sequence=VSP_050729;
CC Name=G; Synonyms=DLP3 {ECO:0000269|PubMed:11223239};
CC IsoId=Q9VDW6-4; Sequence=VSP_050730;
CC Name=B {ECO:0000303|PubMed:10731132}; Synonyms=Dp186;
CC IsoId=Q9VDW3-1; 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 -!- TISSUE SPECIFICITY: Isoform A, isoform F and isoform G are expressed in
CC the midgut endoderm of stage 12 embryos. In stage 16 embryos,
CC expression is also seen in the pericardial cells, cells at the ectoderm
CC segmental border and cells along the midline of the CNS. During
CC embryogenesis, isoform A is also expressed in the visceral mesoderm,
CC muscle attachment sites, mesectodermal cells at the midline, the gut,
CC and throughout muscle fibers. In larvae, isoform A is found in all
CC muscle fibers, but not detectable in the brain or neuropil.
CC {ECO:0000269|PubMed:11223239, ECO:0000269|PubMed:16399704}.
CC -!- DEVELOPMENTAL STAGE: Isoform A is expressed in embryos and larvae and
CC levels increase further in adults. Isoform F has weak expression in
CC embryos, increases in larvae and falls again in adults. Isoform G is
CC weakly expressed in adult flies, and not detectable earlier in
CC development. {ECO:0000269|PubMed:11223239,
CC ECO:0000269|PubMed:16399704}.
CC -!- DISRUPTION PHENOTYPE: Wings exhibit a 'crossveinless' phenotype. Adult
CC flies are viable and the crossvein defect is the sole overt
CC morphological defect observed. Flies that have reduced expression of
CC all isoforms (due to transgenic RNA interference targeting the common
CC C-terminal region) exhibit severe muscle degeneration in larvae and
CC adult 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 ECO:0000269|PubMed:18093579}.
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DR EMBL; AF277386; AAG17395.1; -; mRNA.
DR EMBL; AF297644; AAK15256.1; -; mRNA.
DR EMBL; AF300456; AAK15258.1; -; mRNA.
DR EMBL; AF302236; AAK18176.1; -; mRNA.
DR EMBL; AE014297; AAF55673.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55675.2; -; Genomic_DNA.
DR EMBL; AE014297; ABI31176.1; -; Genomic_DNA.
DR EMBL; AE014297; ABI31178.1; -; Genomic_DNA.
DR EMBL; AE014297; ABI31180.1; -; Genomic_DNA.
DR RefSeq; NP_001036722.1; NM_001043257.2. [Q9VDW6-5]
DR RefSeq; NP_001036723.1; NM_001043258.2. [Q9VDW6-1]
DR RefSeq; NP_001036724.1; NM_001043259.2.
DR RefSeq; NP_001036726.1; NM_001043261.2.
DR RefSeq; NP_001036728.1; NM_001043263.2.
DR SMR; Q9VDW6; -.
DR BioGRID; 67322; 74.
DR IntAct; Q9VDW6; 39.
DR STRING; 7227.FBpp0110219; -.
DR iPTMnet; Q9VDW6; -.
DR PaxDb; Q9VDW6; -.
DR PRIDE; Q9VDW6; -.
DR DNASU; 42327; -.
DR EnsemblMetazoa; FBtr0083764; FBpp0083178; FBgn0260003. [Q9VDW6-1]
DR EnsemblMetazoa; FBtr0110919; FBpp0110219; FBgn0260003. [Q9VDW6-5]
DR GeneID; 42327; -.
DR UCSC; CG34157-RH; d. melanogaster.
DR CTD; 42327; -.
DR FlyBase; FBgn0260003; Dys.
DR VEuPathDB; VectorBase:FBgn0260003; -.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000166230; -.
DR InParanoid; Q9VDW6; -.
DR PhylomeDB; Q9VDW6; -.
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; Q9VDW6; baseline and differential.
DR Genevisible; Q9VDW6; 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:UniProtKB.
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: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; cd00014; CH; 1.
DR CDD; cd00176; SPEC; 4.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
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; PF00307; CH; 2.
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 PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 11.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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..3598
FT /note="Dystrophin, isoforms A/C/F/G/H"
FT /id="PRO_0000076080"
FT DOMAIN 12..116
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044,
FT ECO:0000305"
FT DOMAIN 127..230
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044,
FT ECO:0000305"
FT REPEAT 307..420
FT /note="Spectrin 1"
FT REPEAT 423..525
FT /note="Spectrin 2"
FT REPEAT 851..963
FT /note="Spectrin 3"
FT REPEAT 1056..1170
FT /note="Spectrin 4"
FT REPEAT 1173..1275
FT /note="Spectrin 5"
FT REPEAT 1381..1483
FT /note="Spectrin 6"
FT REPEAT 2237..2363
FT /note="Spectrin 7"
FT REPEAT 2366..2472
FT /note="Spectrin 8"
FT REPEAT 2475..2576
FT /note="Spectrin 9"
FT REPEAT 2579..2712
FT /note="Spectrin 10"
FT REPEAT 2715..2819
FT /note="Spectrin 11"
FT DOMAIN 2849..2882
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224,
FT ECO:0000305"
FT ZN_FING 3107..3163
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..230
FT /note="Actin-binding"
FT REGION 233..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2204..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2655..2679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2822..2852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3316..3344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3387..3449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3483..3545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3560..3598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2214..2233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2659..2679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2822..2845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3316..3342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3390..3443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3483..3513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3568..3598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1832
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1838
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..7
FT /note="MEPGILI -> MHDPSDYDSVYSEEDFVDTVRGAATPPLMDYEEFRVKTM
FT (in isoform F)"
FT /evidence="ECO:0000303|PubMed:11223239"
FT /id="VSP_050729"
FT VAR_SEQ 1..7
FT /note="MEPGILI -> MAYNLALKPADLAR (in isoform G)"
FT /evidence="ECO:0000303|PubMed:11223239"
FT /id="VSP_050730"
FT VAR_SEQ 1619..1965
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11018515"
FT /id="VSP_050731"
FT VAR_SEQ 2316..2338
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11018515"
FT /id="VSP_050732"
FT VAR_SEQ 3447..3547
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11223239"
FT /id="VSP_036500"
FT CONFLICT 2615
FT /note="V -> A (in Ref. 2; AAK15256)"
FT /evidence="ECO:0000305"
FT CONFLICT 2682
FT /note="T -> R (in Ref. 2; AAK15256)"
FT /evidence="ECO:0000305"
FT CONFLICT 2700
FT /note="I -> L (in Ref. 2; AAK15256)"
FT /evidence="ECO:0000305"
FT CONFLICT 2873
FT /note="E -> Q (in Ref. 2; AAK15256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3598 AA; 410414 MW; 97848038A8DD0C99 CRC64;
MEPGILIDER QHIQKKTFTK WINSHLIDTQ CTPVKDLFLD LRDGHRLLAL LSTLTQTNLK
PEKGRMRVHH INNLNKVITE IQQHGVKLVN ISSDDIVGGN AKLTLGLIWL IALEFNGQHL
VKSHSSNGVE KSLLAWARQY TEPHGLQLND FSSSWSDGRA FLMILDAHVE ELNLQAALQQ
HALKRLHLAF DLAHRHFKIE KLLDAEDVHT HKPDNKSIQM YVMCLYHAME SMRTRQQEQE
QDEGQDQDPG RVPCTSITDL DEVPLDNDQT SLGLYTSDSA GSMEQRSSGE LKTHSMRPLS
TATNASVEIS GYQSALEAVL TLLLEDEQLL SQNLPDPQDF QTAKLQFHEN ESFMLKLTEH
QEYVGEALEE GSNLINESQK AGAGLSQEDQ NEVRQQMVLL NERWETLRLR ALDVQAKILM
RLAEFQKQKL EQLRQFLTSV EDRISHMSDI GPTLEEAEKQ LLEAQKLKAD LSEQQELVDS
LSSMVVIVND TSGNFNDLED RLSALGERWS HVVKWSDLRK EKLQQYKCIS RWLDAREQDL
KLMESRDVTD VGGITQRINE LNYCAKDLLE LQRYLIDLRQ MVAATLQDGD DKGERVLIQL
ESYEDRLDAL KQIVEVQTVR IETKGFNFGR DRASYDDSRV VRPEGWVDYQ MIIRFGEDDS
QEDDDEHDLA SKKRKLRNAD NFNALENHIM EHFGYVQEVE QKLQQLQRQS LRQQCELLKE
LQAENSRRCG TLPELKKLYE VCELEDPSRN LLLEETHIKQ LEQRYANLSQ KLSSQQSESH
TLLAKEKYYN SLTGFKLVLA DSRDWYKQHA GSASGNELEQ RLSHMESLAS EISEAKTATE
ELDDNLIEWK QDFGLFYDSW HDMKQALQAL IQQRGGESLS RQLKQIQDFV TKVSNQKVRV
SNLEVMQEQQ HFLNQLLDEM ESLRLTYDNI PKHLIGEELQ TAWNRLPEQL NERVIKQTTA
IENLNHFAAE YNAIIAMLRS AADSKLNGSD GASSQDLRKL EIDVISARNF SEILIKEAEP
AQKESLQSQI RALNTLYDQV EQVHREKKEQ QTVLQSHIDL IQLRLKETDQ WLTDLESNTP
KSGISDIVNS NELFQSKSRF QTLKETCERE TTQFRDLNER GGELLLQMDE LQDQDRESRY
GSLAKQFTRI NARWTEVTEL VYAKTALLEH ISTQLGEFKK FMVSETGYLD KLENKIRNTP
ENAADAEEIM EELDDLENVL RSHSEEWLDK IQEIGNELID NEFMADSIRR DIDETVQRWT
QLQQQAKKRT ELLEQKVSEA EQSEKCIVQF EKWLTRVDDI LSDHLDNDVT IVDQPEEFQR
LAHEFVANEK NFKEISELID EHTRNGKVGA ANRLQEQLNL MEVRFKYCQA KLSKCTAIQH
SYESRLNRAY TDLRNVERST EVVDVASAGP NTVQTQYQKC LQIYRTLSEI KSEIESTIKT
GRRVCEDRYT KSPKQLSQRI DALKHLYNTL GENVTQSKAT LERLLTLARQ LEECFDSADN
LIRRFESPQE VHDRNSILLE FEDVLRRCED HYNEYNKSCD QSCMVETRQR IDGLKATYHK
LTSADIIKRL TEMKTTLQNL DNISLETLRA MEHDLKEINV PSNPEIEKLQ QQVIAIVVDV
LKTRFNEATT LAARNTSSPD NDDTEIVVVS DTVRQRRART PQSGESPSSA HTSSSESPTK
GVENSPGAVG DQVMPDLLPP QTFRLAESST LFSQISLNPQ KVTNTPPPKP AKTKRKAPSS
PAQVVEIRVK NIQNDKMSVQ NIDLEPQQGE IVDTVNILES VEPFVPEYVE TVQIVDLSED
SDSSVRVDSQ GKEMRRSKSK HSLNETPLPK VSDNDEDSAE QEEDLLRPSA ENTSTPFLRV
EKRRISFDEK RKRVANERDI LRDSEEEEPK TPDTPRAAQV SKPKRWRQLQ PEMDALEPES
PGRDSFYSPD KESGFDAEPL VFSDDEDIPR FSLEMTSTID SDSDTSRIMT PSTKNPNPFL
SKVLESLSSP VDDSNVTLKS PISEEQPQNL DDRVREFDKQ AKQMIYKLKL TKAKIEQCHE
SEAEDLRLLI APDAATLISQ GDSLVLETHG RQGSISRLVM RTQIILREQF REVQQARSKT
SGSGAPAPPL DSVNIEELVT KGLRRINVLI EKTVDLKSST DLEKRMEDIN ERHDDLQVIV
SAIGKNAQMP KVTPLMMNEI EKTKNNLIAH ADSIELSLTE LRNGPRISNG KERPDASSAA
TMSCRSEYNN EPSGTGALAG SFDKSVLQIS DWLTWEQNMI KIQSVLVDDG DAVRLAIEKQ
EKVLRELKMK KPQLNELVHT AEVLKGDVKR QQLQEKELKQ FSLAPHCSAD LDYMRCCLKV
TRLREHWDET SQCVLQRAAQ LKNMLSDSQR FEAKRLELEK WLARMEQRAE RMGTIATTAD
ILEAQQKEQK SFHAELHQNK QHFDIFNELT QKLIAVYPND DTTRIKKMTE VINQRYANLN
SGVINRGKQL HAAVHSLQSF DRAMDQFLAF LSETETLCEN AESDIERNPL MFKDLQSEIE
THRVVYDRLD GTGRKLLGSL TSQEDAVMLQ RRLDEMNQRW NNLKSKSIAI RNRLESNSEH
WNALLLSLRE LTEWVIRKDT ELSTLGLGPV RGDAVSLQKQ LDDHKAFRRQ LEDKRPIVES
NLTSGRQYIA NEAAVSDTSD TEANHDSDSR YMSAEEQSRE LTRSIRREVG KLSEQWNNLI
DRSDNWKHRL DEYMTKMRQF QKILEDLSSR VALAEQTKTS WLPPSSVGEA NEQMQQLQRL
RDKMTTASAL LDDCNEQQSF FTANQVLVPT PCLSKLEDLN TRMKLLQIAM DERQKVLCQA
GAQQTHENGD DGRTTSNSGT IGPLPNLGQS VKPPWERATT AANVPYYIDH ERETTHWDHP
EMIELMKGLA DLNEIRFSAY RTAMKLRSVQ KRLALDRISM STACESFDRH GLRAQNDKLI
DIPDMTTVLH SLYVTIDKID LTLMLDLAIN WILNVYDSQR TGQIRVLSFK VGLVLLCKGH
LEEKYRYLFR LVADTDRRAD QRRLGLLLHD CIQVPRQLGE VAAFGGSNIE PSVRSCLEQA
GISQEAIDGN QDISIELQHF LGWLQHEPQS LVWLPVLHRL AAAEAAKHQA KCNICKEYPI
VGFRYRCLKC FNFDMCQKCF FFGRNAKNHK LTHPMHEYCT TTTSTEDVRD FTRALKNKFK
SRKYFKKHPR VGYLPVQSVL EGDALESPAP SPQHTTHQLQ NDMHSRLEMY ASRLAQVEYG
GTGSNSTPDS DDEHQLIAQY CQALPGTSNG SAPKSPVQVM AAMDAEQREE LEAIIRDLEE
ENANLQAEYQ QLCSKEQSGM PEDSNGMQHS SSSMTGLSGQ GEQGQDMMAE AKLLRQHKGR
LEARMQILED HNRQLEAQLQ RLRQLLDEPN GGGSSATSSG LPSAPGSALN SKPNTLQTRS
VTASQLNTDS PAKMNQQNGH YEHNSKGIML PGMNSEIQQQ HAQLASLAAK HHQHQLSGAL
NALHQQQQQQ LQQQPPQQQR SMMTGNGGMD ISGGMQTSGG YLGDDGRPPP PPHSSLMQQQ
HQQHLNENSS GLVTVITEQE LESINDDLED SSSSNTTNTT TTTTTTATTE KTCVELQK
