VAMP1_HUMAN
ID VAMP1_HUMAN Reviewed; 118 AA.
AC P23763; A8MVP3; D3DUR3; O75468; Q15857; Q6FG94; Q8IVC9;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Vesicle-associated membrane protein 1;
DE Short=VAMP-1;
DE AltName: Full=Synaptobrevin-1;
GN Name=VAMP1; Synonyms=SYB1;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1976629; DOI=10.1016/s0021-9258(17)44898-8;
RA Archer B.T. III, Oezcelik T., Jahn R., Francke U., Suedhof T.C.;
RT "Structures and chromosomal localizations of two human genes encoding
RT synaptobrevins 1 and 2.";
RL J. Biol. Chem. 265:17267-17273(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND SUBCELLULAR LOCATION.
RC TISSUE=Umbilical vein;
RX PubMed=9658161; DOI=10.1091/mbc.9.7.1649;
RA Isenmann S., Khew-Goodall Y., Gamble J., Vadas M., Wattenberg B.W.;
RT "A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1)
RT contains a mitochondrial targeting signal.";
RL Mol. Biol. Cell 9:1649-1660(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Gough K.H., Verkuylen A., Cosgrove L., Frenkel M.J., Ward C.W.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [9]
RP INVOLVEMENT IN SPAX1.
RX PubMed=22958904; DOI=10.1016/j.ajhg.2012.07.018;
RA Bourassa C.V., Meijer I.A., Merner N.D., Grewal K.K., Stefanelli M.G.,
RA Hodgkinson K., Ives E.J., Pryse-Phillips W., Jog M., Boycott K.,
RA Grimes D.A., Goobie S., Leckey R., Dion P.A., Rouleau G.A.;
RT "VAMP1 mutation causes dominant hereditary spastic ataxia in Newfoundland
RT families.";
RL Am. J. Hum. Genet. 91:548-552(2012).
RN [10]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP B; D AND F, AND MUTAGENESIS OF GLU-42; ILE-48 AND SER-81.
RX PubMed=22289120; DOI=10.1111/j.1348-0421.2012.00434.x;
RA Yamamoto H., Ida T., Tsutsuki H., Mori M., Matsumoto T., Kohda T.,
RA Mukamoto M., Goshima N., Kozaki S., Ihara H.;
RT "Specificity of botulinum protease for human VAMP family proteins.";
RL Microbiol. Immunol. 56:245-253(2012).
RN [11]
RP INVOLVEMENT IN CMS25.
RX PubMed=28168212; DOI=10.1002/acn3.387;
RA Shen X.M., Scola R.H., Lorenzoni P.J., Kay C.S., Werneck L.C., Brengman J.,
RA Selcen D., Engel A.G.;
RT "Novel synaptobrevin-1 mutation causes fatal congenital myasthenic
RT syndrome.";
RL Ann. Clin. Transl. Neurol. 4:130-138(2017).
RN [12]
RP INVOLVEMENT IN CMS25, AND VARIANT CMS25 PRO-49.
RX PubMed=28253535; DOI=10.1002/ana.24905;
RG SYNAPS Study Group;
RA Salpietro V., Lin W., Delle Vedove A., Storbeck M., Liu Y., Efthymiou S.,
RA Manole A., Wiethoff S., Ye Q., Saggar A., McElreavey K., Krishnakumar S.S.,
RA Pitt M., Bello O.D., Rothman J.E., Basel-Vanagaite L., Hubshman M.W.,
RA Aharoni S., Manzur A.Y., Wirth B., Houlden H.;
RT "Homozygous mutations in VAMP1 cause a presynaptic congenital myasthenic
RT syndrome.";
RL Ann. Neurol. 81:597-603(2017).
RN [13]
RP INVOLVEMENT IN CMS25.
RX PubMed=28600779; DOI=10.1007/s00439-017-1821-8;
RA Monies D., Abouelhoda M., AlSayed M., Alhassnan Z., Alotaibi M.,
RA Kayyali H., Al-Owain M., Shah A., Rahbeeni Z., Al-Muhaizea M.A.,
RA Alzaidan H.I., Cupler E., Bohlega S., Faqeih E., Faden M., Alyounes B.,
RA Jaroudi D., Goljan E., Elbardisy H., Akilan A., Albar R., Aldhalaan H.,
RA Gulab S., Chedrawi A., Al Saud B.K., Kurdi W., Makhseed N., Alqasim T.,
RA El Khashab H.Y., Al-Mousa H., Alhashem A., Kanaan I., Algoufi T.,
RA Alsaleem K., Basha T.A., Al-Murshedi F., Khan S., Al-Kindy A., Alnemer M.,
RA Al-Hajjar S., Alyamani S., Aldhekri H., Al-Mehaidib A., Arnaout R.,
RA Dabbagh O., Shagrani M., Broering D., Tulbah M., Alqassmi A., Almugbel M.,
RA AlQuaiz M., Alsaman A., Al-Thihli K., Sulaiman R.A., Al-Dekhail W.,
RA Alsaegh A., Bashiri F.A., Qari A., Alhomadi S., Alkuraya H., Alsebayel M.,
RA Hamad M.H., Szonyi L., Abaalkhail F., Al-Mayouf S.M., Almojalli H.,
RA Alqadi K.S., Elsiesy H., Shuaib T.M., Seidahmed M.Z., Abosoudah I.,
RA Akleh H., AlGhonaium A., Alkharfy T.M., Al Mutairi F., Eyaid W.,
RA Alshanbary A., Sheikh F.R., Alsohaibani F.I., Alsonbul A., Al Tala S.,
RA Balkhy S., Bassiouni R., Alenizi A.S., Hussein M.H., Hassan S., Khalil M.,
RA Tabarki B., Alshahwan S., Oshi A., Sabr Y., Alsaadoun S., Salih M.A.,
RA Mohamed S., Sultana H., Tamim A., El-Haj M., Alshahrani S., Bubshait D.K.,
RA Alfadhel M., Faquih T., El-Kalioby M., Subhani S., Shah Z., Moghrabi N.,
RA Meyer B.F., Alkuraya F.S.;
RT "The landscape of genetic diseases in Saudi Arabia based on the first 1000
RT diagnostic panels and exomes.";
RL Hum. Genet. 136:921-939(2017).
RN [14]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP X.
RX PubMed=29540745; DOI=10.1038/s41598-018-22842-4;
RA Masuyer G., Zhang S., Barkho S., Shen Y., Henriksson L., Kosenina S.,
RA Dong M., Stenmark P.;
RT "Structural characterisation of the catalytic domain of botulinum
RT neurotoxin X - high activity and unique substrate specificity.";
RL Sci. Rep. 8:4518-4518(2018).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane.
CC -!- SUBUNIT: Interacts with VAPA and VAPB.
CC -!- INTERACTION:
CC P23763; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10201335, EBI-749265;
CC P23763; O95721: SNAP29; NbExp=3; IntAct=EBI-10201335, EBI-490676;
CC P23763; Q12846: STX4; NbExp=3; IntAct=EBI-10201335, EBI-744942;
CC P23763-3; Q13520: AQP6; NbExp=3; IntAct=EBI-12097582, EBI-13059134;
CC P23763-3; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12097582, EBI-11343438;
CC P23763-3; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-12097582, EBI-17233035;
CC P23763-3; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12097582, EBI-6942903;
CC P23763-3; P00387: CYB5R3; NbExp=3; IntAct=EBI-12097582, EBI-1046040;
CC P23763-3; Q15125: EBP; NbExp=3; IntAct=EBI-12097582, EBI-3915253;
CC P23763-3; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-12097582, EBI-18535450;
CC P23763-3; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-12097582, EBI-10285373;
CC P23763-3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12097582, EBI-781551;
CC P23763-3; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-12097582, EBI-18938272;
CC P23763-3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12097582, EBI-13345167;
CC P23763-3; Q13571: LAPTM5; NbExp=3; IntAct=EBI-12097582, EBI-2865663;
CC P23763-3; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12097582, EBI-7545592;
CC P23763-3; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-12097582, EBI-10192441;
CC P23763-3; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-12097582, EBI-13044680;
CC P23763-3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12097582, EBI-17247926;
CC P23763-3; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-12097582, EBI-2855401;
CC P23763-3; Q8NHU3: SGMS2; NbExp=3; IntAct=EBI-12097582, EBI-10977284;
CC P23763-3; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-12097582, EBI-10262251;
CC P23763-3; Q16623: STX1A; NbExp=3; IntAct=EBI-12097582, EBI-712466;
CC P23763-3; P61266: STX1B; NbExp=3; IntAct=EBI-12097582, EBI-9071709;
CC P23763-3; Q12846: STX4; NbExp=3; IntAct=EBI-12097582, EBI-744942;
CC P23763-3; Q96IK0: TMEM101; NbExp=3; IntAct=EBI-12097582, EBI-3922699;
CC P23763-3; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12097582, EBI-8638294;
CC P23763-3; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-12097582, EBI-11722971;
CC P23763-3; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12097582, EBI-6447886;
CC P23763-3; Q12888: TP53BP1; NbExp=3; IntAct=EBI-12097582, EBI-396540;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass type IV
CC membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle membrane
CC {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
CC Synapse, synaptosome {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane;
CC Single-pass type IV membrane protein {ECO:0000269|PubMed:9658161}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=VAMP-1A;
CC IsoId=P23763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23763-3; Sequence=VSP_029185;
CC Name=3; Synonyms=VAMP-1B;
CC IsoId=P23763-2; Sequence=VSP_006325;
CC -!- TISSUE SPECIFICITY: Nervous system, skeletal muscle and adipose tissue.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type B (BoNT/B, botB) which probably hydrolyzes the 78-
CC Gln-|-Phe-79 bond and inhibits neurotransmitter release
CC (PubMed:22289120). {ECO:0000269|PubMed:22289120,
CC ECO:0000305|PubMed:22289120}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 61-
CC Arg-|-Leu-62 bond and inhibits neurotransmitter release
CC (PubMed:22289120). BoNT/D has low catalytic activity on this protein
CC due to its sequence (PubMed:22289120). Note that humans are not known
CC to be infected by C.botulinum type D. {ECO:0000269|PubMed:22289120,
CC ECO:0000305, ECO:0000305|PubMed:22289120}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type F (BoNT/F, botF) which probably hydrolyzes the 60-
CC Gln-|-Lys-61 bond and inhibits neurotransmitter release
CC (PubMed:22289120). {ECO:0000269|PubMed:22289120,
CC ECO:0000305|PubMed:22289120}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type X (BoNT/X) which probably hydrolyzes the 68-Arg-|-Ala-
CC 69 bond and inhibits neurotransmitter release (PubMed:29540745). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:29540745, ECO:0000305|PubMed:29540745}.
CC -!- DISEASE: Spastic ataxia 1, autosomal dominant (SPAX1) [MIM:108600]: An
CC autosomal dominant form of spastic ataxia, a progressive
CC neurodegenerative disorder characterized by lower-limb spasticity and
CC generalized ataxia with dysarthria, impaired ocular movements, and gait
CC disturbance. {ECO:0000269|PubMed:22958904}. Note=The disease is caused
CC by variants affecting the gene represented in this entry. A mutation
CC affecting a critical donor site for the splicing of VAMP1 isoforms
CC leads to the loss of neuron-specific isoform 1 and subsequently results
CC in haploinsufficiency (PubMed:22958904). Therefore, there would be less
CC neurotransmitter exocytosis in specific regions of the brain, causing
CC the symptoms of SPAX1. {ECO:0000303|PubMed:22958904}.
CC -!- DISEASE: Myasthenic syndrome, congenital, 25, presynaptic (CMS25)
CC [MIM:618323]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features include easy fatigability
CC and muscle weakness. CMS25 is an autosomal recessive form characterized
CC by hypotonia and generalized muscle weakness apparent from birth.
CC Affected individuals have feeding difficulties and delayed motor
CC development, usually never achieving independent ambulation. Additional
CC variable features include eye movement abnormalities, joint
CC contractures, and rigid spine. {ECO:0000269|PubMed:28168212,
CC ECO:0000269|PubMed:28253535, ECO:0000269|PubMed:28600779}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; M36200; AAA60603.1; -; Genomic_DNA.
DR EMBL; M36196; AAA60603.1; JOINED; Genomic_DNA.
DR EMBL; M36197; AAA60603.1; JOINED; Genomic_DNA.
DR EMBL; M36198; AAA60603.1; JOINED; Genomic_DNA.
DR EMBL; M36199; AAA60603.1; JOINED; Genomic_DNA.
DR EMBL; AF060538; AAC28336.1; -; mRNA.
DR EMBL; Z48924; CAA88760.1; -; mRNA.
DR EMBL; CR542214; CAG47010.1; -; mRNA.
DR EMBL; CR542231; CAG47027.1; -; mRNA.
DR EMBL; CR749485; CAH18312.1; -; mRNA.
DR EMBL; AC005840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88792.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88795.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88796.1; -; Genomic_DNA.
DR EMBL; BC023286; AAH23286.1; -; mRNA.
DR CCDS; CCDS31731.1; -. [P23763-3]
DR CCDS; CCDS41740.1; -. [P23763-1]
DR CCDS; CCDS44809.1; -. [P23763-2]
DR PIR; A38315; A38315.
DR PIR; S52747; S52747.
DR RefSeq; NP_001284367.1; NM_001297438.1.
DR RefSeq; NP_055046.1; NM_014231.4. [P23763-1]
DR RefSeq; NP_058439.1; NM_016830.3. [P23763-2]
DR RefSeq; NP_954740.1; NM_199245.2. [P23763-3]
DR AlphaFoldDB; P23763; -.
DR SMR; P23763; -.
DR BioGRID; 112710; 39.
DR CORUM; P23763; -.
DR IntAct; P23763; 33.
DR MINT; P23763; -.
DR STRING; 9606.ENSP00000379602; -.
DR DrugBank; DB00042; Botulinum toxin type B.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; P23763; -.
DR PhosphoSitePlus; P23763; -.
DR SwissPalm; P23763; -.
DR BioMuta; VAMP1; -.
DR DMDM; 135093; -.
DR EPD; P23763; -.
DR jPOST; P23763; -.
DR MassIVE; P23763; -.
DR MaxQB; P23763; -.
DR PaxDb; P23763; -.
DR PeptideAtlas; P23763; -.
DR PRIDE; P23763; -.
DR ProteomicsDB; 54157; -. [P23763-1]
DR ProteomicsDB; 54158; -. [P23763-2]
DR ProteomicsDB; 54159; -. [P23763-3]
DR Antibodypedia; 3460; 395 antibodies from 44 providers.
DR DNASU; 6843; -.
DR Ensembl; ENST00000361716.8; ENSP00000355122.3; ENSG00000139190.17. [P23763-3]
DR Ensembl; ENST00000396308.4; ENSP00000379602.3; ENSG00000139190.17. [P23763-1]
DR Ensembl; ENST00000400911.7; ENSP00000383702.3; ENSG00000139190.17. [P23763-2]
DR GeneID; 6843; -.
DR KEGG; hsa:6843; -.
DR MANE-Select; ENST00000396308.4; ENSP00000379602.3; NM_014231.5; NP_055046.1.
DR UCSC; uc001qoj.4; human. [P23763-1]
DR CTD; 6843; -.
DR DisGeNET; 6843; -.
DR GeneCards; VAMP1; -.
DR HGNC; HGNC:12642; VAMP1.
DR HPA; ENSG00000139190; Tissue enhanced (brain).
DR MalaCards; VAMP1; -.
DR MIM; 108600; phenotype.
DR MIM; 185880; gene.
DR MIM; 618323; phenotype.
DR neXtProt; NX_P23763; -.
DR OpenTargets; ENSG00000139190; -.
DR Orphanet; 251282; Autosomal dominant spastic ataxia type 1.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA37266; -.
DR VEuPathDB; HostDB:ENSG00000139190; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000161390; -.
DR HOGENOM; CLU_064620_4_0_1; -.
DR InParanoid; P23763; -.
DR OMA; WESPRIF; -.
DR OrthoDB; 1606985at2759; -.
DR PhylomeDB; P23763; -.
DR TreeFam; TF313666; -.
DR PathwayCommons; P23763; -.
DR Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (botD).
DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (botF).
DR Reactome; R-HSA-5250989; Toxicity of botulinum toxin type G (botG).
DR SignaLink; P23763; -.
DR BioGRID-ORCS; 6843; 10 hits in 1088 CRISPR screens.
DR ChiTaRS; VAMP1; human.
DR GeneWiki; VAMP1; -.
DR GenomeRNAi; 6843; -.
DR Pharos; P23763; Tbio.
DR PRO; PR:P23763; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P23763; protein.
DR Bgee; ENSG00000139190; Expressed in pons and 184 other tissues.
DR ExpressionAtlas; P23763; baseline and differential.
DR Genevisible; P23763; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
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 PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Congenital myasthenic syndrome;
KW Cytoplasmic vesicle; Disease variant; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..118
FT /note="Vesicle-associated membrane protein 1"
FT /id="PRO_0000206719"
FT TOPO_DOM 1..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..118
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 33..93
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 60..61
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type F (BoNT/F, botF)"
FT /evidence="ECO:0000305|PubMed:22289120"
FT SITE 61..62
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type D (BoNT/D, botD)"
FT /evidence="ECO:0000305|PubMed:22289120"
FT SITE 68..69
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000305|PubMed:29540745"
FT SITE 78..79
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type B (BoNT/B, botB)"
FT /evidence="ECO:0000305|PubMed:22289120"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62442"
FT VAR_SEQ 114..118
FT /note="IYFFT -> SKYR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_029185"
FT VAR_SEQ 114..118
FT /note="IYFFT -> RRD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9658161, ECO:0000303|Ref.4"
FT /id="VSP_006325"
FT VARIANT 49
FT /note="R -> P (in CMS25; unknown pathological significance;
FT dbSNP:rs754046104)"
FT /evidence="ECO:0000269|PubMed:28253535"
FT /id="VAR_082265"
FT MUTAGEN 42
FT /note="E->D: No change in susceptibility to C.botulinum
FT BoNT/B, BoNT/D or BoNT/F."
FT /evidence="ECO:0000269|PubMed:22289120"
FT MUTAGEN 48
FT /note="I->M: 1000-fold increase in susceptibility to
FT C.botulinum BoNT/D, no change in susceptibility to BoNT/B
FT or BoNT/F."
FT /evidence="ECO:0000269|PubMed:22289120"
FT MUTAGEN 81
FT /note="S->T: No change in susceptibility to C.botulinum
FT BoNT/B, BoNT/D or BoNT/F."
FT /evidence="ECO:0000269|PubMed:22289120"
FT CONFLICT 103
FT /note="A -> T (in Ref. 3; CAA88760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 12902 MW; 64CE9615447B686B CRC64;
MSAPAQPPAE GTEGTAPGGG PPGPPPNMTS NRRLQQTQAQ VEEVVDIIRV NVDKVLERDQ
KLSELDDRAD ALQAGASQFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVIYFFT
