DYN_DROME
ID DYN_DROME Reviewed; 877 AA.
AC P27619; Q0KHS4; Q9VXM2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Dynamin;
DE EC=3.6.5.5;
DE AltName: Full=Protein shibire;
DE AltName: Full=dDyn;
GN Name=shi; ORFNames=CG18102;
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] (ISOFORMS 1 AND 2).
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=1828536; DOI=10.1038/351583a0;
RA Chen M.S., Obar R.A., Schroeder C.C., Austin T.W., Poodry C.A.,
RA Wadsworth S.C., Vallee R.B.;
RT "Multiple forms of dynamin are encoded by shibire, a Drosophila gene
RT involved in endocytosis.";
RL Nature 351:583-586(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF GLY-141
RP AND GLY-268.
RC STRAIN=Oregon-R;
RX PubMed=1674590; DOI=10.1038/351411a0;
RA van der Bliek A.M., Meyerowitz E.M.;
RT "Dynamin-like protein encoded by the Drosophila shibire gene associated
RT with vesicular traffic.";
RL Nature 351:411-414(1991).
RN [3]
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 [4]
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756; SER-764 AND SER-767, AND
RP 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: Microtubule-associated force-producing protein which is
CC involved in the production of microtubule bundles and which is able to
CC bind and hydrolyze GTP. Implicated in endocytic protein sorting.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Microtubule-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=4, D, F;
CC IsoId=P27619-1; Sequence=Displayed;
CC Name=2; Synonyms=3, A, B;
CC IsoId=P27619-2; Sequence=VSP_001330, VSP_001331;
CC -!- MISCELLANEOUS: Shibire mutation is the cause of temperature-sensitive
CC paralysis. This is believed to be due to a reversible block of
CC endocytosis, which prevents membrane cycling and thus depletes synaptic
CC vesicles.
CC -!- MISCELLANEOUS: 'Shibire' means 'paralyzed' in Japanese.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42061.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
CC Sequence=CAA42067.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
CC Sequence=CAA42068.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
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DR EMBL; X59448; CAA42067.1; ALT_SEQ; mRNA.
DR EMBL; X59449; CAA42068.1; ALT_SEQ; mRNA.
DR EMBL; X59435; CAA42061.1; ALT_SEQ; mRNA.
DR EMBL; X59436; CAA42062.1; -; mRNA.
DR EMBL; AE014298; AAF48536.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65368.1; -; Genomic_DNA.
DR EMBL; BT010049; AAQ22518.1; -; mRNA.
DR PIR; S15413; S15413.
DR PIR; S16130; S16130.
DR PIR; S17974; S17974.
DR PIR; S17975; S17975.
DR PIR; S34399; S34399.
DR RefSeq; NP_001036278.1; NM_001042813.2. [P27619-2]
DR RefSeq; NP_001036279.1; NM_001042814.2. [P27619-2]
DR RefSeq; NP_001162766.1; NM_001169295.1. [P27619-1]
DR RefSeq; NP_001162768.1; NM_001169297.2.
DR RefSeq; NP_524853.2; NM_080114.4. [P27619-2]
DR RefSeq; NP_727910.1; NM_167470.3. [P27619-1]
DR RefSeq; NP_727911.1; NM_167471.5. [P27619-2]
DR RefSeq; NP_996465.1; NM_206742.1. [P27619-1]
DR RefSeq; NP_996466.1; NM_206743.2. [P27619-1]
DR RefSeq; NP_996467.1; NM_206744.3. [P27619-2]
DR RefSeq; NP_996468.1; NM_206745.3. [P27619-2]
DR AlphaFoldDB; P27619; -.
DR SMR; P27619; -.
DR BioGRID; 69991; 59.
DR DIP; DIP-17621N; -.
DR IntAct; P27619; 4.
DR STRING; 7227.FBpp0305866; -.
DR iPTMnet; P27619; -.
DR PaxDb; P27619; -.
DR PRIDE; P27619; -.
DR EnsemblMetazoa; FBtr0074118; FBpp0073928; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0074119; FBpp0073929; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0074121; FBpp0089278; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0074122; FBpp0089279; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0074123; FBpp0089280; FBgn0003392. [P27619-1]
DR EnsemblMetazoa; FBtr0074124; FBpp0089277; FBgn0003392. [P27619-1]
DR EnsemblMetazoa; FBtr0111036; FBpp0110335; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0111037; FBpp0110336; FBgn0003392. [P27619-2]
DR EnsemblMetazoa; FBtr0301594; FBpp0290809; FBgn0003392. [P27619-1]
DR EnsemblMetazoa; FBtr0301595; FBpp0290810; FBgn0003392. [P27619-1]
DR GeneID; 45928; -.
DR KEGG; dme:Dmel_CG18102; -.
DR UCSC; CG18102-RA; d. melanogaster. [P27619-1]
DR CTD; 45928; -.
DR FlyBase; FBgn0003392; shi.
DR VEuPathDB; VectorBase:FBgn0003392; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000166903; -.
DR InParanoid; P27619; -.
DR OMA; MQMVQTF; -.
DR PhylomeDB; P27619; -.
DR BRENDA; 3.6.5.5; 1994.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-196025; Formation of annular gap junctions.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-437239; Recycling pathway of L1.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P27619; -.
DR BioGRID-ORCS; 45928; 3 hits in 3 CRISPR screens.
DR ChiTaRS; shi; fly.
DR GenomeRNAi; 45928; -.
DR PRO; PR:P27619; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003392; Expressed in brain and 38 other tissues.
DR ExpressionAtlas; P27619; baseline and differential.
DR Genevisible; P27619; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0070864; C:sperm individualization complex; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IMP:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0150008; P:bulk synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:0061883; P:clathrin-dependent endocytosis involved in vitellogenesis; IMP:FlyBase.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IDA:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0090148; P:membrane fission; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:FlyBase.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; IDA:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR GO; GO:0007637; P:proboscis extension reflex; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:FlyBase.
DR GO; GO:0032970; P:regulation of actin filament-based process; IGI:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:FlyBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
DR GO; GO:0035152; P:regulation of tube architecture, open tracheal system; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IMP:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:FlyBase.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:FlyBase.
DR GO; GO:0036465; P:synaptic vesicle recycling; IMP:FlyBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IDA:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027188; DNM2.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF23; PTHR11566:SF23; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Endocytosis; GTP-binding;
KW Hydrolase; Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..877
FT /note="Dynamin"
FT /id="PRO_0000206576"
FT DOMAIN 23..289
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 513..621
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 650..741
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 33..40
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 59..61
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 131..134
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 200..203
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 230..233
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 623..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 200..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 231..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 830
FT /note="V -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1674590,
FT ECO:0000303|PubMed:1828536"
FT /id="VSP_001330"
FT VAR_SEQ 831..877
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1674590,
FT ECO:0000303|PubMed:1828536"
FT /id="VSP_001331"
FT MUTAGEN 141
FT /note="G->S: In allele shi-TS2; temperature sensitive
FT larval and adult paralysis."
FT /evidence="ECO:0000269|PubMed:1674590"
FT MUTAGEN 268
FT /note="G->D: In allele shi-TS1; temperature sensitive
FT larval and adult paralysis."
FT /evidence="ECO:0000269|PubMed:1674590"
FT CONFLICT 594
FT /note="K -> R (in Ref. 1; CAA42067/CAA42068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 877 AA; 97809 MW; 5B85F96491490B14 CRC64;
MDSLITIVNK LQDAFTSLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT
RRPLILQLIN GVTEYGEFLH IKGKKFSSFD EIRKEIEDET DRVTGSNKGI SNIPINLRVY
SPHVLNLTLI DLPGLTKVAI GDQPVDIEQQ IKQMIFQFIR KETCLILAVT PANTDLANSD
ALKLAKEVDP QGVRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIEGR
KDIHQALAAE RKFFLSHPSY RHMADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML
TLEKEVEEFK HFQPGDASIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR
IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIALLKEPV
IKCVDLVVQE LSVVVRMCTA KMSRYPRLRE ETERIITTHV RQREHSCKEQ ILLLIDFELA
YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GSRPYWFVLT
SESISWYKDE DEKEKKFMLP LDGLKLRDIE QGFMSMSRRV TFALFSPDGR NVYKDYKQLE
LSCETVEDVE SWKASFLRAG VYPEKQETQE NGDESASEES SSDPQLERQV ETIRNLVDSY
MKIVTKTTRD MVPKAIMMLI INNAKDFING ELLAHLYASG DQAQMMEESA ESATRREEML
RMYRACKDAL QIIGDVSMAT VSSPLPPPVK NDWLPSGLDN PRLSPPSPGG VRGKPGPPAQ
SSLGGRNPPL PPSTGRPAPA IPNRPGGGAP PLPGGRPGGS LPPPMLPSRV SGAVGGAIVQ
QSGANRYVPE SMRGQVNQAV GQAAINELSN AFSSRFK
