SYB1_CAEEL
ID SYB1_CAEEL Reviewed; 109 AA.
AC O02495;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Synaptobrevin-1;
DE AltName: Full=Synaptobrevin-related protein 1;
GN Name=snb-1 {ECO:0000312|WormBase:T10H9.4}; ORFNames=T10H9.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB61234.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF LEU-62 AND ALA-66, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB61235.1};
RX PubMed=9412487; DOI=10.1523/jneurosci.18-01-00070.1998;
RA Nonet M.L., Saifee O., Zhao H., Rand J.B., Wei L.;
RT "Synaptic transmission deficits in Caenorhabditis elegans synaptobrevin
RT mutants.";
RL J. Neurosci. 18:70-80(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=10476681; DOI=10.1016/s0165-0270(99)00031-x;
RA Nonet M.L.;
RT "Visualization of synaptic specializations in live C. elegans with synaptic
RT vesicle protein-GFP fusions.";
RL J. Neurosci. Methods 89:33-40(1999).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=15254012; DOI=10.1093/hmg/ddh209;
RA Williams S.N., Locke C.J., Braden A.L., Caldwell K.A., Caldwell G.A.;
RT "Epileptic-like convulsions associated with LIS-1 in the cytoskeletal
RT control of neurotransmitter signaling in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 13:2043-2059(2004).
RN [5] {ECO:0000305}
RP MUTAGENESIS OF ILE-97.
RX PubMed=16604067; DOI=10.1038/nn1685;
RA Sandoval G.M., Duerr J.S., Hodgkin J., Rand J.B., Ruvkun G.;
RT "A genetic interaction between the vesicular acetylcholine transporter
RT VAChT/UNC-17 and synaptobrevin/SNB-1 in C. elegans.";
RL Nat. Neurosci. 9:599-601(2006).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16844789; DOI=10.1073/pnas.0600784103;
RA Dittman J.S., Kaplan J.M.;
RT "Factors regulating the abundance and localization of synaptobrevin in the
RT plasma membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11399-11404(2006).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane. Acts in neuronal exocytosis of synaptic
CC transmission. Likely to have a role in cholinergic transmisson.
CC Required for viability, coordinated movement and M3 pharynx motor
CC neuron function. {ECO:0000269|PubMed:9412487}.
CC -!- SUBUNIT: Part of the SNARE core complex containing ric-4/SNAP25, snb-
CC 1/VAMP2 and unc-64/STX1A. This complex binds to cpx-1/CPLX1 (By
CC similarity). {ECO:0000250|UniProtKB:P63045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:10476681,
CC ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:10476681,
CC ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}. Cell
CC membrane {ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012,
CC ECO:0000269|PubMed:16844789}. Synapse, synaptosome. Note=Observed in
CC discrete synaptic vesicle puncta along the ventral cord. Functional
CC unc-104, a kinesin-like protein, is required for localization. The two
CC pools of synaptobrevin are recycled by clatherin- and
CC dynamin- dependent endocytosis. AP180-like adapter protein, unc-11, is
CC thought to act as a molecular chaperone. {ECO:0000250|UniProtKB:P63045,
CC ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012,
CC ECO:0000269|PubMed:16844789}.
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system notably the nerve
CC ring, ventral cord and dorsal cord. {ECO:0000269|PubMed:9412487}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit arrested development after
CC embryogenesis. Viable mutants appear lethargic with sporadic jerky
CC movements and absent M3 pharynx motorneuron activity. All mutants are
CC resistant to the acetylcholinesterase inhibitor aldicarb indicating
CC impaired cholinergic transmission. {ECO:0000269|PubMed:9412487}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000255}.
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DR EMBL; AF003281; AAB61234.1; -; mRNA.
DR EMBL; AF003282; AAB61235.1; -; Genomic_DNA.
DR EMBL; FO081382; CCD71211.1; -; Genomic_DNA.
DR PIR; T33239; T33239.
DR RefSeq; NP_504688.1; NM_072287.4.
DR AlphaFoldDB; O02495; -.
DR SMR; O02495; -.
DR BioGRID; 57298; 2.
DR DIP; DIP-27164N; -.
DR IntAct; O02495; 1.
DR STRING; 6239.T10H9.4; -.
DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR EPD; O02495; -.
DR PaxDb; O02495; -.
DR PeptideAtlas; O02495; -.
DR EnsemblMetazoa; T10H9.4.1; T10H9.4.1; WBGene00004897.
DR UCSC; T10H9.4; c. elegans.
DR WormBase; T10H9.4; CE18252; WBGene00004897; snb-1.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000158370; -.
DR HOGENOM; CLU_064620_4_1_1; -.
DR InParanoid; O02495; -.
DR OMA; CQDTFAT; -.
DR OrthoDB; 1589977at2759; -.
DR PhylomeDB; O02495; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-449836; Other interleukin signaling.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR Reactome; R-CEL-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:O02495; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004897; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0060473; C:cortical granule; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0048786; C:presynaptic active zone; IDA:WormBase.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043134; P:regulation of hindgut contraction; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IDA:WormBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:WormBase.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
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 PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Membrane;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..109
FT /note="Synaptobrevin-1"
FT /id="PRO_0000307354"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 23..83
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 62
FT /note="L->F: In js17; resist to aldicarb."
FT /evidence="ECO:0000269|PubMed:9412487"
FT MUTAGEN 66
FT /note="A->G: In js44; resist to aldicarb."
FT /evidence="ECO:0000269|PubMed:9412487"
FT MUTAGEN 97
FT /note="I->D: In e1563; viable showing only slightly
FT increased rate of thrashing behavior."
FT /evidence="ECO:0000269|PubMed:16604067"
SQ SEQUENCE 109 AA; 12025 MW; 3BBC0F085CE070EB CRC64;
MDAQGDAGAQ GGSQGGPRPS NKRLQQTQAQ VDEVVGIMKV NVEKVLERDQ KLSQLDDRAD
ALQEGASQFE KSAATLKRKY WWKNIKMMII MCAIVVILII IIVLWAGGK
