NSYB_DROME
ID NSYB_DROME Reviewed; 183 AA.
AC Q9W0C1; C6TP85; M9PDW0; M9PE71; Q86BQ0; Q9W0C2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Neuronal synaptobrevin {ECO:0000303|PubMed:8229205};
DE Short=n-syb {ECO:0000303|PubMed:8229205};
GN Name=nSyb {ECO:0000303|PubMed:8229205, ECO:0000312|FlyBase:FBgn0013342};
GN ORFNames=CG17248 {ECO:0000312|FlyBase:FBgn0013342};
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 [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 [2]
RP GENOME REANNOTATION.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND H).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39190.1}; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8229205; DOI=10.1523/jneurosci.13-11-04924.1993;
RA DiAntonio A., Burgess R.W., Chin A.C., Deitcher D.L., Scheller R.H.,
RA Schwarz T.L.;
RT "Identification and characterization of Drosophila genes for synaptic
RT vesicle proteins.";
RL J. Neurosci. 13:4924-4935(1993).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=9482790; DOI=10.1523/jneurosci.18-06-02028.1998;
RA Deitcher D.L., Ueda A., Stewart B.A., Burgess R.W., Kidokoro Y.,
RA Schwarz T.L.;
RT "Distinct requirements for evoked and spontaneous release of
RT neurotransmitter are revealed by mutations in the Drosophila gene neuronal-
RT synaptobrevin.";
RL J. Neurosci. 18:2028-2039(1998).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10460261; DOI=10.1523/jneurosci.19-17-07548.1999;
RA Hiesinger P.R., Reiter C., Schau H., Fischbach K.F.;
RT "Neuropil pattern formation and regulation of cell adhesion molecules in
RT Drosophila optic lobe development depend on synaptobrevin.";
RL J. Neurosci. 19:7548-7556(1999).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12364587; DOI=10.1073/pnas.202335999;
RA Bhattacharya S., Stewart B.A., Niemeyer B.A., Burgess R.W., McCabe B.D.,
RA Lin P., Boulianne G., O'Kane C.J., Schwarz T.L.;
RT "Members of the synaptobrevin/vesicle-associated membrane protein (VAMP)
RT family in Drosophila are functionally interchangeable in vivo for
RT neurotransmitter release and cell viability.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13867-13872(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22270918; DOI=10.1083/jcb.201108088;
RA Haberman A., Williamson W.R., Epstein D., Wang D., Rina S.,
RA Meinertzhagen I.A., Hiesinger P.R.;
RT "The synaptic vesicle SNARE neuronal Synaptobrevin promotes endolysosomal
RT degradation and prevents neurodegeneration.";
RL J. Cell Biol. 196:261-276(2012).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane (PubMed:12364587, PubMed:22270918). Major
CC SNARE protein of synaptic vesicles which mediates fusion of synaptic
CC vesicles to release neurotransmitters (PubMed:9482790,
CC PubMed:12364587). Essential for fast vesicular exocytosis and activity-
CC dependent neurotransmitter release as well as fast endocytosis that
CC mediates rapid reuse of synaptic vesicles (PubMed:12364587). Also
CC involved in a neuron-specific sort-and-degrade mechanism that promotes
CC endolysosomal degradation and is required for neuronal maintenance
CC (PubMed:22270918). {ECO:0000269|PubMed:12364587,
CC ECO:0000269|PubMed:22270918, ECO:0000269|PubMed:9482790}.
CC -!- SUBUNIT: Part of the SNARE core complex containing Snap25 and syntaxin.
CC {ECO:0000269|PubMed:12364587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:22270918,
CC ECO:0000305|PubMed:9482790}; Single-pass type IV membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:22270918};
CC Single-pass type IV membrane protein {ECO:0000255}. Note=Localizes to
CC synaptic vesicles and to a subset of early endosomal compartments,
CC predominantly at synapses. {ECO:0000269|PubMed:22270918}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A; Synonyms=F;
CC IsoId=Q9W0C1-1; Sequence=Displayed;
CC Name=J;
CC IsoId=Q9W0C1-2; Sequence=VSP_061566, VSP_061571;
CC Name=E; Synonyms=G;
CC IsoId=Q9W0C1-3; Sequence=VSP_061565;
CC Name=H; Synonyms=I;
CC IsoId=Q9W0C1-4; Sequence=VSP_061565, VSP_061567, VSP_061570;
CC Name=K;
CC IsoId=Q9W0C1-5; Sequence=VSP_061568, VSP_061569;
CC -!- TISSUE SPECIFICITY: Specifically expressed in neurons and synapses.
CC {ECO:0000269|PubMed:8229205}.
CC -!- DEVELOPMENTAL STAGE: Transcripts are first detectable at stage 13 or 14
CC (PubMed:8229205). The expression is restricted to the nervous system,
CC becoming quite robust in both the central and peripheral nervous system
CC (CNS and PNS, respectively) by late embryogenesis (PubMed:8229205).
CC {ECO:0000269|PubMed:8229205}.
CC -!- DISRUPTION PHENOTYPE: Embryos develop normally, but their nerve
CC terminals do not release transmitter in response to an action potential
CC (PubMed:9482790). Spontaneous neurotransmitter release is reduced, but
CC not abolished (PubMed:9482790, PubMed:10460261). Slow degeneration in
CC adult photoreceptor neurons is also observed: defects are caused by an
CC accumulation of endosomal vesicles, leading to transmembrane protein
CC degradation defects and a secondary increase in autophagy
CC (PubMed:22270918). {ECO:0000269|PubMed:10460261,
CC ECO:0000269|PubMed:22270918, ECO:0000269|PubMed:9482790}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AE014296; AAF47529.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11493.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB93964.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47530.1; -; Genomic_DNA.
DR EMBL; AE014296; AAS64932.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11494.2; -; Genomic_DNA.
DR EMBL; AE014296; AFH04218.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB93965.1; -; Genomic_DNA.
DR EMBL; AY069045; AAL39190.1; -; mRNA.
DR EMBL; BT099571; ACU43533.1; -; mRNA.
DR RefSeq; NP_001246547.1; NM_001259618.2.
DR RefSeq; NP_001261269.1; NM_001274340.1.
DR RefSeq; NP_001261270.1; NM_001274341.1.
DR RefSeq; NP_477058.1; NM_057710.6.
DR RefSeq; NP_728644.1; NM_167904.3.
DR RefSeq; NP_728645.1; NM_167905.4.
DR RefSeq; NP_728646.2; NM_167906.3.
DR RefSeq; NP_995956.1; NM_206234.4.
DR SMR; Q9W0C1; -.
DR PaxDb; M9PE71; -.
DR PRIDE; Q9W0C1; -.
DR DNASU; 38196; -.
DR EnsemblMetazoa; FBtr0072815; FBpp0072697; FBgn0013342.
DR EnsemblMetazoa; FBtr0300893; FBpp0290115; FBgn0013342.
DR GeneID; 38196; -.
DR KEGG; dme:Dmel_CG17248; -.
DR UCSC; CG17248-RA; d. melanogaster.
DR CTD; 38196; -.
DR FlyBase; FBgn0013342; nSyb.
DR VEuPathDB; VectorBase:FBgn0013342; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000164382; -.
DR HOGENOM; CLU_1333168_0_0_1; -.
DR OMA; SKFWLQN; -.
DR OrthoDB; 1534477at2759; -.
DR Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-DME-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-449836; Other interleukin signaling.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR Reactome; R-DME-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 38196; 0 hits in 3 CRISPR screens.
DR ChiTaRS; nSyb; fly.
DR GenomeRNAi; 38196; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0013342; Expressed in brain and 28 other tissues.
DR ExpressionAtlas; Q9W0C1; baseline and differential.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0031201; C:SNARE complex; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
DR GO; GO:0099536; P:synaptic signaling; IMP:UniProtKB.
DR GO; GO:0016081; P:synaptic vesicle docking; ISS:FlyBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45701; PTHR45701; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endosome; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..183
FT /note="Neuronal synaptobrevin"
FT /id="PRO_0000456041"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..183
FT /note="Vesicular"
FT /evidence="ECO:0000305"
FT DOMAIN 41..101
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT VAR_SEQ 1
FT /note="M -> MGKKDKNKEQ (in isoform E and isoform H)"
FT /id="VSP_061565"
FT VAR_SEQ 122..144
FT /note="NKLGLIGGEQPPQYQYPPQYMQP -> KPYMSDDNAAPQPPALQQQVAPASA
FT TAPDSA (in isoform J)"
FT /id="VSP_061566"
FT VAR_SEQ 122..126
FT /note="NKLGL -> KKDEE (in isoform H)"
FT /id="VSP_061567"
FT VAR_SEQ 122..125
FT /note="NKLG -> SNFM (in isoform K)"
FT /id="VSP_061568"
FT VAR_SEQ 126..183
FT /note="Missing (in isoform K)"
FT /id="VSP_061569"
FT VAR_SEQ 127..183
FT /note="Missing (in isoform H)"
FT /id="VSP_061570"
FT VAR_SEQ 151..183
FT /note="QPAGGQSSLVDAAGAGDGAGAGGSAGAGDHGGV -> LLQQQEQQLQPHHHT
FT QNLKSEPPTLEKPLAEKLTDHPQSPSNEVATGQ (in isoform J)"
FT /id="VSP_061571"
SQ SEQUENCE 183 AA; 18776 MW; 139A0C9B34E15D74 CRC64;
MADAAPAGDA PPNAGAPAGE GGDGEIVGGP HNPQQIAAQK RLQQTQAQVD EVVDIMRTNV
EKVLERDSKL SELDDRADAL QQGASQFEQQ AGKLKRKFWL QNLKMMIIMG VIGLVVVGII
ANKLGLIGGE QPPQYQYPPQ YMQPPPPPPQ QPAGGQSSLV DAAGAGDGAG AGGSAGAGDH
GGV
