ID   SYB_APLCA               Reviewed;         180 AA.
AC   P35589;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Synaptobrevin;
DE   AltName: Full=Vesicle-associated membrane protein;
DE            Short=VAMP;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-59, SUBCELLULAR
RP   LOCATION, PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP   NEUROTOXIN TYPES D AND F AND BY C.TETANI TETANUS TOXIN, AND TOPOLOGY.
RC   TISSUE=Ganglion;
RX   PubMed=8197120; DOI=10.1073/pnas.91.11.4688;
RA   Yamasaki S., Hu Y., Binz T., Kalkuhl A., Kurazono H., Tamura T., Jahn R.,
RA   Kandel E., Niemann H.;
RT   "Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia
RT   californica: structure and proteolysis by tetanus toxin and botulinal
RT   neurotoxins type D and F.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:4688-4692(1994).
CC   -!- FUNCTION: Intrinsic membrane protein of small synaptic vesicles.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000305|PubMed:8197120}; Single-pass type IV
CC       membrane protein {ECO:0000305|PubMed:8197120}. Synapse, synaptosome.
CC       Note=Neuronal synaptic vesicles. In vitro integrates into vesicles
CC       co- and post-translationally (PubMed:8197120).
CC       {ECO:0000269|PubMed:8197120}.
CC   -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC       neurotoxin type D (BoNT/D, botD) which hydrolyzes the 49-Lys-|-Ile-50
CC       bond and probably inhibits neurotransmitter release (PubMed:8197120).
CC       {ECO:0000269|PubMed:8197120}.
CC   -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC       neurotoxin type F (BoNT/F, botF) which hydrolyzes the 48-Gln-|-Lys-49
CC       bond and probably inhibits neurotransmitter release (PubMed:8197120).
CC       {ECO:0000269|PubMed:8197120}.
CC   -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani toxin
CC       (tetX) which hydrolyzes the 66-Gln-|-Phe-67 bond and probably inhibits
CC       neurotransmitter release (PubMed:8197120).
CC       {ECO:0000269|PubMed:8197120}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC   -!- CAUTION: It is not known if C.botulinum or C.tetani infect this
CC       organism. {ECO:0000305}.
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DR   EMBL; U00997; AAA19442.1; -; mRNA.
DR   RefSeq; NP_001191557.1; NM_001204628.1.
DR   AlphaFoldDB; P35589; -.
DR   SMR; P35589; -.
DR   GeneID; 100533331; -.
DR   OrthoDB; 1606985at2759; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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   Coiled coil; Cytoplasmic vesicle; Direct protein sequencing; Membrane;
KW   Synapse; Synaptosome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="Synaptobrevin"
FT                   /id="PRO_0000206740"
FT   TOPO_DOM        1..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8197120"
FT   TRANSMEM        85..104
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..180
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000305|PubMed:8197120"
FT   DOMAIN          21..81
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   REGION          110..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            48..49
FT                   /note="(Microbial infection) Cleavage; by C.botulinum
FT                   neurotoxin type F (BoNT/F, botF)"
FT                   /evidence="ECO:0000269|PubMed:8197120"
FT   SITE            49..50
FT                   /note="(Microbial infection) Cleavage; by C.botulinum
FT                   neurotoxin type D (BoNT/D, botD)"
FT                   /evidence="ECO:0000269|PubMed:8197120"
FT   SITE            66..67
FT                   /note="(Microbial infection) Cleavage; by C.tetani toxin
FT                   (tetX)"
FT                   /evidence="ECO:0000269|PubMed:8197120"
SQ   SEQUENCE   180 AA;  19746 MW;  ADC7780DA74CF347 CRC64;
     MSAGPGGPQG GMQPPREQSK RLQQTQAQVD EVVDIMRVNV EKVLDRDQKI SQLDDRAEAL
     QAGASQFEAS AGKLKRKYWW KNCKMMLILG AIIGVIVIII IVWVVTSQDS GGDDSGSKTP
     ATAGTSPKPV ESGVQGGGGR QQRPHSQLVE RRNVLRRTED HIGCRPHIHS FIHIFMICLV