Sv2a
entrez
117559
canonical
uniprot
Q02563
canonical
ensembl
ENSRNOG00000021182
resolver
ensembl
ENSRNOG00055032256
resolver
ensembl
ENSRNOG00060013977
resolver
ensembl
ENSRNOG00065031025
resolver
ensp
ENSRNOP00000028760
resolver
ensp
ENSRNOP00055045906
resolver
ensp
ENSRNOP00060019040
resolver
ensp
ENSRNOP00065043972
resolver
enst
ENSRNOT00000028760
resolver
enst
ENSRNOT00055055705
resolver
enst
ENSRNOT00060023914
resolver
enst
ENSRNOT00065053497
resolver
genesymbol
Sv2a
resolver
genesymbol_syn
Sv2
resolver
uniprot
Q58DZ8
resolver
uniprot_entry
SV2A_RAT
resolver
uniprot_sec
Q58DZ8
resolver
amino_acid_sequence
MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEEDDDDFPAPADGYYRGEGAQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKDREELAQQYETILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFSPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYAARTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLVNSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVLSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ
uniprot
proteins
function
FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin binds via extracellular loop 4 (PubMed:16543415). Restores uptake of BoNT/A in mouse cells that are deleted for SV2 receptor (PubMed:16543415, PubMed:18815274). Glycosylation of Asn-573 is not essential for receptor activity, but enhances uptake (PubMed:18815274, PubMed:19650874). Also serves as a receptor for the closely related C.botulinum neurotoxin type A2; glycosylation is not essential but enhances the interaction (PubMed:29649119). {ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:29649119}.; FUNCTION: Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD); BoNT/D does not bind to extracellular loop 4 as do BoNT/A and BoNT/E, nor to loop 1 or loop 3 (PubMed:21483489). Another group does not find a convincing interaction with SV2 (PubMed:21632541). {ECO:0000269|PubMed:21483489, ECO:0000269|PubMed:21632541}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type E (BoNT/E); the toxin probably binds via extracellular loop 4 and requires glycosylation of Asn-573 (PubMed:18815274, PubMed:19650874). Restores uptake of BoNT/E in mouse cells that are deleted for SV2 receptor (PubMed:18815274). {ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19650874}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type F (BoNT/F) (PubMed:19476346, PubMed:19650874). Binding requires glycosylation of Asn-573 (PubMed:19476346). {ECO:0000269|PubMed:19650874, ECO:0000305|PubMed:19476346}.
uniprot
proteins
mass_dalton
82661
uniprot
proteins
mutagenesis
MUTAGEN 196..200; /note="Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E)."; /evidence="ECO:0000269|PubMed:21483489"; MUTAGEN 321..331; /note="Missing: No change in uptake of BoNT/D or BoNT/E."; /evidence="ECO:0000269|PubMed:21483489"; MUTAGEN 498; /note="N->Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D."; /evidence="ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:21483489"; MUTAGEN 548; /note="N->Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D."; /evidence="ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:21483489"; MUTAGEN 570..573; /note="RLVN->TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E."; /evidence="ECO:0000269|PubMed:18815274"; MUTAGEN 573; /note="N->Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D."; /evidence="ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:21483489
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1. {ECO:0000269|PubMed:10747945}.; PTM: N-glycosylated, on at least 3 residues. {ECO:0000269|PubMed:1355409, ECO:0000305|PubMed:18815274, ECO:0000305|PubMed:19476346, ECO:0000305|PubMed:29649119}.
uniprot
proteins
protein_family
Major facilitator superfamily
uniprot
proteins
pubmed
10455054
uniprot
proteins
pubmed
10625067
uniprot
proteins
pubmed
10747945
uniprot
proteins
pubmed
1355409
uniprot
proteins
pubmed
1426240
uniprot
proteins
pubmed
1519064
uniprot
proteins
pubmed
15210974
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15866046
uniprot
proteins
pubmed
16306227
uniprot
proteins
pubmed
16543415
uniprot
proteins
pubmed
18815274
uniprot
proteins
pubmed
19476346
uniprot
proteins
pubmed
19650874
uniprot
proteins
pubmed
21483489
uniprot
proteins
pubmed
21632541
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24090084
uniprot
proteins
pubmed
29649119
uniprot
proteins
pubmed
8910372
uniprot
proteins
sequence_length
742
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240, ECO:0000269|PubMed:16306227}; Multi-pass membrane protein {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240, ECO:0000269|PubMed:16306227}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas. Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q9JIS5, ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:16306227}.
uniprot
proteins
transmembrane_region
TRANSMEM 170..190; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 206..226; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 234..254; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 263..283; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 295..315; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 335..355; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 448..468; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 599..619; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 627..647; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 652..672; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 686..708; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 713..731; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins