SV2C
entrez
22987
canonical
uniprot
Q496J9
canonical
ensembl
ENSG00000122012
resolver
ensp
ENSP00000316983
resolver
ensp
ENSP00000423541
resolver
enst
ENST00000322285
resolver
enst
ENST00000502798
resolver
genesymbol
SV2C
resolver
genesymbol_syn
KIAA1054
resolver
hgnc
HGNC:30670
resolver
uniprot
B3KT41
resolver
uniprot
J3KNI3
resolver
uniprot
Q496K1
resolver
uniprot
Q9UPU8
resolver
uniprot_entry
B3KT41_HUMAN
resolver
uniprot_entry
J3KNI3_HUMAN
resolver
uniprot_entry
SV2C_HUMAN
resolver
uniprot_sec
Q496K1
resolver
uniprot_sec
Q9UPU8
resolver
amino_acid_sequence
MEDSYKDRTSLMKGAKDIAREVKKQTVKKVNQAVDRAQDEYTQRSYSRFQDEEDDDDYYPAGETYNGEANDDEGSSEATEGHDEDDEIYEGEYQGIPSMNQAKDSIVSVGQPKGDEYKDRRELESERRADEEELAQQYELIIQECGHGRFQWALFFVLGMALMADGVEVFVVGFVLPSAETDLCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRKQSLLICMSVNGFFAFLSSFVQGYGFFLFCRLLSGFGIGGAIPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYASAMAWAIIPHYGWSFSMGSAYQFHSWRVFVIVCALPCVSSVVALTFMPESPRFLLEVGKHDEAWMILKLIHDTNMRARGQPEKVFTVNKIKTPKQIDELIEIESDTGTWYRRCFVRIRTELYGIWLTFMRCFNYPVRDNTIKLTIVWFTLSFGYYGLSVWFPDVIKPLQSDEYALLTRNVERDKYANFTINFTMENQIHTGMEYDNGRFIGVKFKSVTFKDSVFKSCTFEDVTSVNTYFKNCTFIDTVFDNTDFEPYKFIDSEFKNCSFFHNKTGCQITFDDDYSAYWIYFVNFLGTLAVLPGNIVSALLMDRIGRLTMLGGSMVLSGISCFFLWFGTSESMMIGMLCLYNGLTISAWNSLDVVTVELYPTDRRATGFGFLNALCKAAAVLGNLIFGSLVSITKSIPILLASTVLVCGGLVGLCLPDTRTQVLM
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. {ECO:0000250|UniProtKB:Q9Z2I6}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin probably binds via extracellular loop 4 (PubMed:27313224). Recognition by BoNT/A relies on both protein-protein and protein-N-glycosylation; glycosylation of Asn-559 increases its affinity for BoNT/A (PubMed:27313224). 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:24240280, ECO:0000269|PubMed:27294781, ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640, ECO:0000269|PubMed:29649119}.; FUNCTION: (Microbial infection) Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD); note that type D does not usually infect humans. {ECO:0000269|PubMed:21483489}.
uniprot
proteins
mass_dalton
82342
uniprot
proteins
mutagenesis
MUTAGEN 559; /note="N->A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/AHC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/AHC."; /evidence="ECO:0000269|PubMed:24240280, ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640"; MUTAGEN 559; /note="N->Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/AHC. Greater reduction in weight; when associated with Q-565."; /evidence="ECO:0000269|PubMed:27313224"; MUTAGEN 561; /note="S->A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/AHC."; /evidence="ECO:0000269|PubMed:27313224"; MUTAGEN 563; /note="F->A: No longer interacts with BoNT/AHC."; /evidence="ECO:0000269|PubMed:24240280, ECO:0000269|PubMed:28252640"; MUTAGEN 565; /note="N->Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559."; /evidence="ECO:0000269|PubMed:27313224
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Upon expression in a kidney cell line the most abundant glycan on Asn-534 is GlcNAc(3)Hex(5), while on Asn-559 and Asn-565 the most abundant glycan is GlcNAc2Fuc1Man3GlcNAc3Gal3. Both Asn-559 and Asn-565 have a high degree of glycan heterogeneity (PubMed:27313224). {ECO:0000269|PubMed:27294781, ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640}.
uniprot
proteins
protein_family
Major facilitator superfamily
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21483489
uniprot
proteins
pubmed
24240280
uniprot
proteins
pubmed
27294781
uniprot
proteins
pubmed
27313224
uniprot
proteins
pubmed
28252640
uniprot
proteins
pubmed
29649119
uniprot
proteins
sequence_length
727
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9Z2I6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z2I6}. Note=Enriched in small synaptic vesicles and adrenal microsomes, not present in chromaffin granules. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas. {ECO:0000250|UniProtKB:Q9Z2I6}.
uniprot
proteins
transmembrane_region
TRANSMEM 155..175; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 192..212; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 227..247; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 249..269; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 281..301; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 321..341; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 438..458; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 579..599; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 610..630; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 637..657; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 670..690; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 699..719; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins