SV2A_RAT
ID SV2A_RAT Reviewed; 742 AA.
AC Q02563; Q58DZ8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Synaptic vesicle glycoprotein 2A;
DE Short=Synaptic vesicle protein 2;
DE Short=Synaptic vesicle protein 2A;
GN Name=Sv2a; Synonyms=Sv2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND GLYCOSYLATION.
RX PubMed=1355409; DOI=10.1016/0092-8674(92)90319-8;
RA Feany M.B., Lee S., Edwards R.H., Buckley K.M.;
RT "The synaptic vesicle protein SV2 is a novel type of transmembrane
RT transporter.";
RL Cell 70:861-867(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 177-194 AND 372-381, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=1426240; DOI=10.1016/0014-5793(92)80917-6;
RA Gingrich J.A., Andersen P.H., Tiberi M., el Mestikawy S., Jorgensen P.N.,
RA Fremeau R.T. Jr., Caron M.G.;
RT "Identification, characterization, and molecular cloning of a novel
RT transporter-like protein localized to the central nervous system.";
RL FEBS Lett. 312:115-122(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-40.
RC TISSUE=Brain;
RX PubMed=1519064; DOI=10.1126/science.1519064;
RA Bajjalieh S.M., Peterson K., Shingal R., Scheller R.H.;
RT "SV2, a brain synaptic vesicle protein homologous to bacterial
RT transporters.";
RL Science 257:1271-1273(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SYT1.
RX PubMed=8910372; DOI=10.1074/jbc.271.44.27770;
RA Schivell A.E., Batchelor R.H., Bajjalieh S.M.;
RT "Isoform-specific, calcium-regulated interaction of the synaptic vesicle
RT proteins SV2 and synaptotagmin.";
RL J. Biol. Chem. 271:27770-27775(1996).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10625067; DOI=10.1016/s0306-4522(99)00370-x;
RA Janz R., Suedhof T.C.;
RT "SV2C is a synaptic vesicle protein with an unusually restricted
RT localization: anatomy of a synaptic vesicle protein family.";
RL Neuroscience 94:1279-1290(1999).
RN [7]
RP INTERACTION WITH AP-2.
RX PubMed=10455054; DOI=10.1126/science.285.5431.1268;
RA Haucke V., De Camilli P.;
RT "AP-2 recruitment to synaptotagmin stimulated by tyrosine-based endocytic
RT motifs.";
RL Science 285:1268-1271(1999).
RN [8]
RP PHOSPHORYLATION BY CK1, AND INTERACTION WITH SYT1.
RX PubMed=10747945; DOI=10.1074/jbc.m000674200;
RA Pyle R.A., Schivell A.E., Hidaka H., Bajjalieh S.M.;
RT "Phosphorylation of synaptic vesicle protein 2 modulates binding to
RT synaptotagmin.";
RL J. Biol. Chem. 275:17195-17200(2000).
RN [9]
RP CHARACTERIZATION AS BINDING-SITE FOR ANTIEPILEPTIC DRUG LEVETIRACETAM.
RX PubMed=15210974; DOI=10.1073/pnas.0308208101;
RA Lynch B.A., Lambeng N., Nocka K., Kensel-Hammes P., Bajjalieh S.M.,
RA Matagne A., Fuks B.;
RT "The synaptic vesicle protein SV2A is the binding site for the
RT antiepileptic drug levetiracetam.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9861-9866(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16306227; DOI=10.1242/jcs.02658;
RA Iezzi M., Theander S., Janz R., Loze C., Wollheim C.B.;
RT "SV2A and SV2C are not vesicular Ca2+ transporters but control glucose-
RT evoked granule recruitment.";
RL J. Cell Sci. 118:5647-5660(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH SYT1.
RX PubMed=15866046; DOI=10.1016/j.mcn.2004.12.011;
RA Schivell A.E., Mochida S., Kensel-Hammes P., Custer K.L., Bajjalieh S.M.;
RT "SV2A and SV2C contain a unique synaptotagmin-binding site.";
RL Mol. Cell. Neurosci. 29:56-64(2005).
RN [12]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RX PubMed=16543415; DOI=10.1126/science.1123654;
RA Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R., Chapman E.R.;
RT "SV2 is the protein receptor for botulinum neurotoxin A.";
RL Science 312:592-596(2006).
RN [13]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPES A AND E RECEPTOR (MICROBIAL
RP INFECTION), SUBUNIT (MICROBIAL INFECTION), GLYCOSYLATION AT ASN-498;
RP ASN-548 AND ASN-573, AND MUTAGENESIS OF ASN-498; ASN-548; 570-ARG--ASN-573
RP AND ASN-573.
RX PubMed=18815274; DOI=10.1091/mbc.e08-07-0765;
RA Dong M., Liu H., Tepp W.H., Johnson E.A., Janz R., Chapman E.R.;
RT "Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E
RT into neurons.";
RL Mol. Biol. Cell 19:5226-5237(2008).
RN [14]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE F RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), AND GLYCOSYLATION.
RX PubMed=19476346; DOI=10.1021/bi9002138;
RA Fu Z., Chen C., Barbieri J.T., Kim J.J., Baldwin M.R.;
RT "Glycosylated SV2 and gangliosides as dual receptors for botulinum
RT neurotoxin serotype F.";
RL Biochemistry 48:5631-5641(2009).
RN [15]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPES A; E AND F RECEPTOR (MICROBIAL
RP INFECTION), AND SUBUNIT (MICROBIAL INFECTION).
RX PubMed=19650874; DOI=10.1111/j.1471-4159.2009.06298.x;
RA Rummel A., Haefner K., Mahrhold S., Darashchonak N., Holt M., Jahn R.,
RA Beermann S., Karnath T., Bigalke H., Binz T.;
RT "Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding
RT site prior to stimulation-dependent uptake with botulinum neurotoxin F
RT utilising the three isoforms of SV2 as second receptor.";
RL J. Neurochem. 110:1942-1954(2009).
RN [16]
RP POSSIBLE FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE D RECEPTOR (MICROBIAL
RP INFECTION), AND MUTAGENESIS OF 196-ASP--SER-200; 321-SER--HIS-331; ASN-498;
RP ASN-548 AND ASN-573.
RX PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT as receptors.";
RL PLoS Pathog. 7:E1002008-E1002008(2011).
RN [17]
RP NOT RECEPTOR FOR C.BOTULINUM NEUROTOXIN TYPE D (MICROBIAL INFECTION), AND
RP SUBUNIT (MICROBIAL INFECTION).
RX PubMed=21632541; DOI=10.1074/jbc.m111.254086;
RA Kroken A.R., Karalewitz A.P., Fu Z., Kim J.J., Barbieri J.T.;
RT "Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into
RT neurons.";
RL J. Biol. Chem. 286:26828-26837(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-573, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [20]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A2 RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), AND GLYCOSYLATION.
RX PubMed=29649119; DOI=10.3390/toxins10040153;
RA Gustafsson R., Zhang S., Masuyer G., Dong M., Stenmark P.;
RT "Crystal structure of botulinum neurotoxin A2 in complex with the human
RT protein receptor SV2C reveals plasticity in receptor binding.";
RL Toxins 10:0-0(2018).
CC -!- FUNCTION: Plays a role in the control of regulated secretion in neural
CC and endocrine cells, enhancing selectively low-frequency
CC neurotransmission. Positively regulates vesicle fusion by maintaining
CC the readily releasable pool of secretory vesicles.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type A (BoNT/A, botA); the toxin binds via extracellular loop 4
CC (PubMed:16543415). Restores uptake of BoNT/A in mouse cells that are
CC deleted for SV2 receptor (PubMed:16543415, PubMed:18815274).
CC Glycosylation of Asn-573 is not essential for receptor activity, but
CC enhances uptake (PubMed:18815274, PubMed:19650874). Also serves as a
CC receptor for the closely related C.botulinum neurotoxin type A2;
CC glycosylation is not essential but enhances the interaction
CC (PubMed:29649119). {ECO:0000269|PubMed:16543415,
CC ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19650874,
CC ECO:0000269|PubMed:29649119}.
CC -!- FUNCTION: Possible receptor for C.botulinum neurotoxin type D (BoNT/D,
CC botD); BoNT/D does not bind to extracellular loop 4 as do BoNT/A and
CC BoNT/E, nor to loop 1 or loop 3 (PubMed:21483489). Another group does
CC not find a convincing interaction with SV2 (PubMed:21632541).
CC {ECO:0000269|PubMed:21483489, ECO:0000269|PubMed:21632541}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type E (BoNT/E); the toxin probably binds via extracellular loop 4 and
CC requires glycosylation of Asn-573 (PubMed:18815274, PubMed:19650874).
CC Restores uptake of BoNT/E in mouse cells that are deleted for SV2
CC receptor (PubMed:18815274). {ECO:0000269|PubMed:18815274,
CC ECO:0000269|PubMed:19650874}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type F (BoNT/F) (PubMed:19476346, PubMed:19650874). Binding requires
CC glycosylation of Asn-573 (PubMed:19476346).
CC {ECO:0000269|PubMed:19650874, ECO:0000305|PubMed:19476346}.
CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent
CC manner. Binds the adapter protein complex AP-2.
CC {ECO:0000269|PubMed:10455054, ECO:0000269|PubMed:10747945,
CC ECO:0000269|PubMed:15866046, ECO:0000269|PubMed:8910372}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A1 and type A2 (BoNT/A, botA) (PubMed:16543415, PubMed:19650874,
CC PubMed:21632541, PubMed:21483489, PubMed:29649119). Interaction is
CC improved by glycosylation of SV2 (PubMed:29649119).
CC {ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:19650874,
CC ECO:0000269|PubMed:21483489, ECO:0000269|PubMed:21632541,
CC ECO:0000269|PubMed:29649119}.
CC -!- SUBUNIT: (Microbial infection) Copurifies with C.botulinum neurotoxin
CC type B (BoNT/B, botB) and synaptotagmin 1 (SYT1) (PubMed:19476346).
CC Interaction does not require glycosylation of SV2 or SYT1 proteins
CC (PubMed:19476346). Another group finds only copurification with SYT1
CC and SYT2 (PubMed:19650874). {ECO:0000269|PubMed:19476346,
CC ECO:0000269|PubMed:19650874}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type E (BoNT/E) (PubMed:18815274, PubMed:19476346, PubMed:19650874).
CC Interaction requires glycosylation of SV2 proteins (PubMed:18815274,
CC PubMed:19476346, PubMed:19650874). {ECO:0000269|PubMed:18815274,
CC ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874}.
CC -!- SUBUNIT: (Microbial infection) Copurifies with C.botulinum neurotoxin
CC type F (BoNT/F) and synaptotagmin 1 (SYT2) (PubMed:19476346). Another
CC group finds only copurification with BoNT/F (PubMed:19650874).
CC Interaction requires SV2 glycosylation (PubMed:19476346).
CC {ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874}.
CC -!- INTERACTION:
CC Q02563; P21707: Syt1; NbExp=2; IntAct=EBI-466194, EBI-458098;
CC Q02563; O00213: APBB1; Xeno; NbExp=3; IntAct=EBI-466194, EBI-81694;
CC Q02563; P0DPI0: botA; Xeno; NbExp=2; IntAct=EBI-466194, EBI-8178893;
CC -!- SUBCELLULAR LOCATION: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240,
CC ECO:0000269|PubMed:16306227}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240,
CC ECO:0000269|PubMed:16306227}. Note=Enriched in chromaffin granules, not
CC present in adrenal microsomes. Associated with both insulin granules
CC and synaptic-like microvesicles in insulin-secreting cells of the
CC pancreas. Colocalizes with ATP2B1 at photoreceptor synaptic terminals.
CC {ECO:0000250|UniProtKB:Q9JIS5, ECO:0000269|PubMed:10625067,
CC ECO:0000269|PubMed:16306227}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout the brain (at protein
CC level). Expressed by neural and endocrine cells of brain and spinal
CC cord. {ECO:0000269|PubMed:1426240}.
CC -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
CC regulates interaction with SYT1. {ECO:0000269|PubMed:10747945}.
CC -!- PTM: N-glycosylated, on at least 3 residues.
CC {ECO:0000269|PubMed:1355409, ECO:0000305|PubMed:18815274,
CC ECO:0000305|PubMed:19476346, ECO:0000305|PubMed:29649119}.
CC -!- DISRUPTION PHENOTYPE: Short hairpin-mediated RNA knockdown of the
CC protein in PC12 cells leads to increased resistance to C.botulinum
CC neurotoxin type A (BoNT/A, botA) as assayed by reduced SNAP25 cleavage;
CC uptake and degradation are restored by expression of SV2B or SV2C
CC (PubMed:16543415). {ECO:0000269|PubMed:16543415}.
CC -!- MISCELLANEOUS: Identified as the brain binding-site for the
CC antiepileptic drug levetiracetam/lev.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The use of this protein as a coreceptor for C.botulinum type D
CC (BoNT/D, botD) is controversial. In double SV2A/SV2B knockout mice
CC BoNT/D does not degrade its synaptobrevin target; introducing SV2A,
CC SV2B or SV2C restores target cleavage (PubMed:21483489). However
CC another group does not find a convincing interaction with SV2
CC (PubMed:21632541). {ECO:0000269|PubMed:21483489,
CC ECO:0000269|PubMed:21632541}.
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DR EMBL; L01788; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; L05435; AAA42188.1; -; mRNA.
DR EMBL; BC092132; AAH92132.1; -; mRNA.
DR PIR; A43344; A43344.
DR RefSeq; NP_476558.2; NM_057210.2.
DR RefSeq; XP_006233014.1; XM_006232952.3.
DR AlphaFoldDB; Q02563; -.
DR BioGRID; 250772; 2.
DR IntAct; Q02563; 8.
DR MINT; Q02563; -.
DR STRING; 10116.ENSRNOP00000028760; -.
DR BindingDB; Q02563; -.
DR ChEMBL; CHEMBL4381; -.
DR DrugCentral; Q02563; -.
DR GuidetoPHARMACOLOGY; 2634; -.
DR TCDB; 2.A.1.22.1; the major facilitator superfamily (mfs).
DR GlyGen; Q02563; 3 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q02563; -.
DR PhosphoSitePlus; Q02563; -.
DR SwissPalm; Q02563; -.
DR jPOST; Q02563; -.
DR PaxDb; Q02563; -.
DR PRIDE; Q02563; -.
DR Ensembl; ENSRNOT00000028760; ENSRNOP00000028760; ENSRNOG00000021182.
DR GeneID; 117559; -.
DR KEGG; rno:117559; -.
DR UCSC; RGD:619715; rat.
DR CTD; 9900; -.
DR RGD; 619715; Sv2a.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q02563; -.
DR OMA; FNDKSMV; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q02563; -.
DR TreeFam; TF324824; -.
DR PRO; PR:Q02563; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021182; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; Q02563; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:RGD.
DR GO; GO:0014052; P:regulation of gamma-aminobutyric acid secretion; IMP:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR022308; SV2.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Direct protein sequencing;
KW Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Receptor; Reference proteome; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..742
FT /note="Synaptic vesicle glycoprotein 2A"
FT /id="PRO_0000084882"
FT TOPO_DOM 1..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..205
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21483489"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..334
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21483489"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..598
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16543415,
FT ECO:0000305|PubMed:18815274"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with SYT1"
FT REGION 40..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 480
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18815274"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18815274"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine; alternate"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18815274"
FT CARBOHYD 573
FT /note="N-linked (HexNAc...) asparagine; alternate"
FT /evidence="ECO:0007744|PubMed:24090084"
FT MUTAGEN 196..200
FT /note="Missing: No change in uptake of C.botulinum
FT neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin
FT type E (BoNT/E)."
FT /evidence="ECO:0000269|PubMed:21483489"
FT MUTAGEN 321..331
FT /note="Missing: No change in uptake of BoNT/D or BoNT/E."
FT /evidence="ECO:0000269|PubMed:21483489"
FT MUTAGEN 498
FT /note="N->Q: No change in uptake of BoNT/E or C.botulinum
FT neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B
FT knockout neurons; SV2A apparent molecular weight decreases.
FT No change in uptake of BoNT/E; when associated with Q-548.
FT No change in uptake of BoNT/D."
FT /evidence="ECO:0000269|PubMed:18815274,
FT ECO:0000269|PubMed:21483489"
FT MUTAGEN 548
FT /note="N->Q: No change in uptake of BoNT/E or BoNT/A by
FT mouse SV2A/SV2B knockout neurons; SV2A apparent molecular
FT weight decreases. No change in uptake of BoNT/E; when
FT associated with Q-498. No change in uptake of BoNT/D."
FT /evidence="ECO:0000269|PubMed:18815274,
FT ECO:0000269|PubMed:21483489"
FT MUTAGEN 570..573
FT /note="RLVN->TLVQ: Restores apparent molecular weight to
FT wild-type, does not restore uptake of BoNT/E."
FT /evidence="ECO:0000269|PubMed:18815274"
FT MUTAGEN 573
FT /note="N->Q: BoNT/E not taken up by mouse SV2A/SV2B
FT knockout neurons, decreased uptake of BoNT/A; SV2A apparent
FT molecular weight decreases. No change in uptake of BoNT/D."
FT /evidence="ECO:0000269|PubMed:18815274,
FT ECO:0000269|PubMed:21483489"
FT CONFLICT 340
FT /note="C -> F (in Ref. 1; AAA42188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 82661 MW; E10FC62BEEFE316A CRC64;
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEEDDDDFPA
PADGYYRGEG AQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA
GVRGGLSDGE GPPGGRGEAQ RRKDREELAQ QYETILRECG HGRFQWTLYF VLGLALMADG
VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS
VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF
FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW
GVRALSLGGQ VWGNFLSCFS PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY
AARTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT
SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LVNSTFLHNK EGCPLDVTGT GEGAYMVYFV
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVLSCVSCF FLSFGNSESA MIALLCLFGG
VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS
AALALGSSLA LKLPETRGQV LQ
