SV2B_HUMAN
ID SV2B_HUMAN Reviewed; 683 AA.
AC Q7L1I2; B4DH30; C6G489; O94840; Q6IAR8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Synaptic vesicle glycoprotein 2B;
GN Name=SV2B; Synonyms=KIAA0735;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [9]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A2 RECEPTOR (MICROBIAL INFECTION),
RP AND SUBUNIT (MICROBIAL INFECTION).
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: Probably plays a role in the control of regulated secretion
CC in neural and endocrine cells. {ECO:0000250}.
CC -!- FUNCTION: (Microbial infection) Receptor for the C.botulinum neurotoxin
CC type A2 (BoNT/A, botA); glycosylation is not essential but enhances the
CC interaction (PubMed:29649119). Probably also serves as a receptor for
CC the closely related C.botulinum neurotoxin type A1.
CC {ECO:0000269|PubMed:29649119, ECO:0000305|PubMed:29649119}.
CC -!- SUBUNIT: Interacts with SYT1 in a calcium-independent manner. Forms a
CC complex with SYT1, syntaxin-1 and SNAP25 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is improved by
CC glycosylation of SV2 (PubMed:29649119). {ECO:0000305|PubMed:29649119}.
CC -!- INTERACTION:
CC Q7L1I2; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-10290607, EBI-3957665;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q63564}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q63564}. Note=Associated with synaptic-like
CC microvesicles but not with insulin-containing vesicles in insulin-
CC secreting cells of the pancreas (By similarity). Localizes to
CC microvesicles in the pinealocytes. Localizes to the acrosome in
CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q63564}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L1I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L1I2-2; Sequence=VSP_045194;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: The N-terminal cytoplasmic domain is phosphorylated by CK1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34455.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018278; BAA34455.2; ALT_INIT; mRNA.
DR EMBL; CR457086; CAG33367.1; -; mRNA.
DR EMBL; AK294902; BAG57991.1; -; mRNA.
DR EMBL; FJ515843; ACS13737.1; -; Genomic_DNA.
DR EMBL; AC123784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02143.1; -; Genomic_DNA.
DR EMBL; BC030011; AAH30011.1; -; mRNA.
DR CCDS; CCDS10370.1; -. [Q7L1I2-1]
DR CCDS; CCDS53972.1; -. [Q7L1I2-2]
DR RefSeq; NP_001161052.1; NM_001167580.2. [Q7L1I2-2]
DR RefSeq; NP_001309960.1; NM_001323031.2. [Q7L1I2-1]
DR RefSeq; NP_001309961.1; NM_001323032.2. [Q7L1I2-1]
DR RefSeq; NP_001309966.1; NM_001323037.2. [Q7L1I2-1]
DR RefSeq; NP_001309967.1; NM_001323038.2. [Q7L1I2-1]
DR RefSeq; NP_001309968.1; NM_001323039.2. [Q7L1I2-1]
DR RefSeq; NP_001309969.1; NM_001323040.2. [Q7L1I2-2]
DR RefSeq; NP_055663.1; NM_014848.6. [Q7L1I2-1]
DR RefSeq; XP_005255055.1; XM_005254998.3. [Q7L1I2-1]
DR RefSeq; XP_016878250.1; XM_017022761.1. [Q7L1I2-1]
DR RefSeq; XP_016878251.1; XM_017022762.1. [Q7L1I2-1]
DR AlphaFoldDB; Q7L1I2; -.
DR BioGRID; 115228; 7.
DR IntAct; Q7L1I2; 1.
DR STRING; 9606.ENSP00000377779; -.
DR ChEMBL; CHEMBL4665594; -.
DR TCDB; 2.A.1.22.7; the major facilitator superfamily (mfs).
DR GlyGen; Q7L1I2; 3 sites.
DR iPTMnet; Q7L1I2; -.
DR PhosphoSitePlus; Q7L1I2; -.
DR BioMuta; SV2B; -.
DR DMDM; 74738530; -.
DR MassIVE; Q7L1I2; -.
DR PaxDb; Q7L1I2; -.
DR PeptideAtlas; Q7L1I2; -.
DR PRIDE; Q7L1I2; -.
DR ProteomicsDB; 4186; -.
DR ProteomicsDB; 68743; -. [Q7L1I2-1]
DR Antibodypedia; 29003; 149 antibodies from 26 providers.
DR DNASU; 9899; -.
DR Ensembl; ENST00000330276.4; ENSP00000332818.4; ENSG00000185518.12. [Q7L1I2-1]
DR Ensembl; ENST00000394232.6; ENSP00000377779.1; ENSG00000185518.12. [Q7L1I2-1]
DR Ensembl; ENST00000545111.6; ENSP00000443243.2; ENSG00000185518.12. [Q7L1I2-2]
DR Ensembl; ENST00000557410.5; ENSP00000450992.1; ENSG00000185518.12. [Q7L1I2-1]
DR GeneID; 9899; -.
DR KEGG; hsa:9899; -.
DR MANE-Select; ENST00000394232.6; ENSP00000377779.1; NM_001323032.3; NP_001309961.1.
DR UCSC; uc010uqv.3; human. [Q7L1I2-1]
DR CTD; 9899; -.
DR DisGeNET; 9899; -.
DR GeneCards; SV2B; -.
DR HGNC; HGNC:16874; SV2B.
DR HPA; ENSG00000185518; Group enriched (brain, retina).
DR MIM; 185861; gene.
DR neXtProt; NX_Q7L1I2; -.
DR OpenTargets; ENSG00000185518; -.
DR PharmGKB; PA134930999; -.
DR VEuPathDB; HostDB:ENSG00000185518; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q7L1I2; -.
DR OMA; TNQVSDD; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q7L1I2; -.
DR TreeFam; TF324824; -.
DR PathwayCommons; Q7L1I2; -.
DR Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (botD).
DR Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (botA).
DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (botF).
DR Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (botE).
DR SignaLink; Q7L1I2; -.
DR BioGRID-ORCS; 9899; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; SV2B; human.
DR GeneWiki; SV2B; -.
DR GenomeRNAi; 9899; -.
DR Pharos; Q7L1I2; Tbio.
DR PRO; PR:Q7L1I2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7L1I2; protein.
DR Bgee; ENSG00000185518; Expressed in middle temporal gyrus and 139 other tissues.
DR Genevisible; Q7L1I2; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR001646; 5peptide_repeat.
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; PF13599; Pentapeptide_4; 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 Alternative splicing; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..683
FT /note="Synaptic vesicle glycoprotein 2B"
FT /id="PRO_0000239768"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG39"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG39"
FT MOD_RES 423
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG39"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045194"
FT CONFLICT 683
FT /note="M -> I (in Ref. 3; CAG33367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 77444 MW; B9818120898F09E2 CRC64;
MDDYKYQDNY GGYAPSDGYY RGNESNPEED AQSDVTEGHD EEDEIYEGEY QGIPHPDDVK
AKQAKMAPSR MDSLRGQTDL MAERLEDEEQ LAHQYETIMD ECGHGRFQWI LFFVLGLALM
ADGVEVFVVS FALPSAEKDM CLSSSKKGML GMIVYLGMMA GAFILGGLAD KLGRKRVLSM
SLAVNASFAS LSSFVQGYGA FLFCRLISGI GIGGALPIVF AYFSEFLSRE KRGEHLSWLG
IFWMTGGLYA SAMAWSIIPH YGWGFSMGTN YHFHSWRVFV IVCALPCTVS MVALKFMPES
PRFLLEMGKH DEAWMILKQV HDTNMRAKGT PEKVFTVSNI KTPKQMDEFI EIQSSTGTWY
QRWLVRFKTI FKQVWDNALY CVMGPYRMNT LILAVVWFAM AFSYYGLTVW FPDMIRYFQD
EEYKSKMKVF FGEHVYGATI NFTMENQIHQ HGKLVNDKFT RMYFKHVLFE DTFFDECYFE
DVTSTDTYFK NCTIESTIFY NTDLYEHKFI NCRFINSTFL EQKEGCHMDL EQDNDFLIYL
VSFLGSLSVL PGNIISALLM DRIGRLKMIG GSMLISAVCC FFLFFGNSES AMIGWQCLFC
GTSIAAWNAL DVITVELYPT NQRATAFGIL NGLCKFGAIL GNTIFASFVG ITKVVPILLA
AASLVGGGLI ALRLPETREQ VLM
