ID VAMP1_MOUSE Reviewed; 118 AA.
AC Q62442; Q6PFF3; Q810K6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Vesicle-associated membrane protein 1;
DE Short=VAMP-1;
DE AltName: Full=Synaptobrevin-1;
GN Name=Vamp1; Synonyms=Syb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Martin S., Tellam J.T., Livington C., Slot J.W., Gould G.W., James D.E.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Olken S.K., Doerre S., Corley R.B.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 PROTEIN SEQUENCE OF 34-49; 50-58 AND 62-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP TISSUE SPECIFICITY, INVOLVEMENT IN LEW, AND VARIANT LEW 64-GLU--THR-118
RP DEL.
RX PubMed=17102983; DOI=10.1007/s10048-006-0068-7;
RA Nystuen A.M., Schwendinger J.K., Sachs A.J., Yang A.W., Haider N.B.;
RT "A null mutation in VAMP1/synaptobrevin is associated with neurological
RT defects and prewean mortality in the lethal-wasting mouse mutant.";
RL Neurogenetics 8:1-10(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP X.
RX PubMed=28770820; DOI=10.1038/ncomms14130;
RA Zhang S., Masuyer G., Zhang J., Shen Y., Lundin D., Henriksson L.,
RA Miyashita S.I., Martinez-Carranza M., Dong M., Stenmark P.;
RT "Identification and characterization of a novel botulinum neurotoxin.";
RL Nat. Commun. 8:14130-14130(2017).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane.
CC -!- SUBUNIT: Interacts with VAPA and VAPB. {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62442-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62442-2; Sequence=VSP_029186;
CC -!- TISSUE SPECIFICITY: Highly expressed in the zona incerta and rostral
CC periolivary region of the brain. Other neuroanatomical regions show
CC negligible expression. Expressed in the retina, expression observed in
CC the outer segments of the photoreceptors, in the outer and inner
CC plexiform layers, and in a subset of ganglion cells.
CC {ECO:0000269|PubMed:17102983}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type X (BoNT/X) which hydrolyzes the 68-Arg-|-Ala-69 bond
CC and probably inhibits neurotransmitter release (PubMed:28770820). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:28770820}.
CC -!- DISEASE: Note=Defects in Vamp1 are the cause of lethal-wasting (lew)
CC phenotype, a mice mutant strain. The lew mutant phenotype is inherited
CC in an autosomal recessive manner and manifests with neurological signs.
CC Lew animals are characterized by a general lack of movement and
CC wasting, eventually leading to death before weaning. The affected
CC animals die near postnatal day 15 (P15). By P10, the mutants are
CC noticeably immobile and lay on their side. Before this stage, mutants
CC can be identified by a failure to attempt to right themselves. In
CC earlier perinatal stages, the mutants are of normal size and difficult
CC to discern from their normal littermates. The affected mice can move
CC their limbs although not in any purposeful manner. No protein is
CC detectable in homozygous mutant animals. {ECO:0000269|PubMed:17102983}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; U61751; AAB03491.1; -; mRNA.
DR EMBL; AF007167; AAB62930.1; -; mRNA.
DR EMBL; AK018783; BAB31407.1; -; mRNA.
DR EMBL; AK078156; BAC37151.1; -; mRNA.
DR EMBL; BC049902; AAH49902.2; -; mRNA.
DR EMBL; BC057587; AAH57587.1; -; mRNA.
DR CCDS; CCDS20546.1; -. [Q62442-1]
DR CCDS; CCDS39637.1; -. [Q62442-2]
DR RefSeq; NP_001074026.1; NM_001080557.1. [Q62442-2]
DR RefSeq; NP_033522.1; NM_009496.3. [Q62442-1]
DR AlphaFoldDB; Q62442; -.
DR SMR; Q62442; -.
DR BioGRID; 204494; 12.
DR STRING; 10090.ENSMUSP00000032487; -.
DR iPTMnet; Q62442; -.
DR PhosphoSitePlus; Q62442; -.
DR SwissPalm; Q62442; -.
DR MaxQB; Q62442; -.
DR PaxDb; 10090-ENSMUSP00000032487; -.
DR ProteomicsDB; 300209; -. [Q62442-1]
DR ProteomicsDB; 300210; -. [Q62442-2]
DR Pumba; Q62442; -.
DR Antibodypedia; 3460; 461 antibodies from 44 providers.
DR DNASU; 22317; -.
DR Ensembl; ENSMUST00000032487.14; ENSMUSP00000032487.8; ENSMUSG00000030337.17. [Q62442-1]
DR Ensembl; ENSMUST00000100942.9; ENSMUSP00000098503.3; ENSMUSG00000030337.17. [Q62442-2]
DR GeneID; 22317; -.
DR KEGG; mmu:22317; -.
DR UCSC; uc009dtx.1; mouse. [Q62442-1]
DR UCSC; uc009dty.1; mouse. [Q62442-2]
DR AGR; MGI:1313276; -.
DR CTD; 6843; -.
DR MGI; MGI:1313276; Vamp1.
DR VEuPathDB; HostDB:ENSMUSG00000030337; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000161390; -.
DR HOGENOM; CLU_064620_4_0_1; -.
DR InParanoid; Q62442; -.
DR OMA; IFCKYNV; -.
DR OrthoDB; 364881at2759; -.
DR PhylomeDB; Q62442; -.
DR TreeFam; TF313666; -.
DR BioGRID-ORCS; 22317; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Vamp1; mouse.
DR PRO; PR:Q62442; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62442; Protein.
DR Bgee; ENSMUSG00000030337; Expressed in pontine nuclear group and 194 other cell types or tissues.
DR ExpressionAtlas; Q62442; baseline and differential.
DR Genevisible; Q62442; MM.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070821; C:tertiary granule membrane; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd15870; R-SNARE_VAMP2; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR InterPro; IPR001388; Synaptobrevin-like.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45701; SYNAPTOBREVIN FAMILY MEMBER; 1.
DR PANTHER; PTHR45701:SF1; VESICLE-ASSOCIATED MEMBRANE PROTEIN 1; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW Direct protein sequencing; Disease variant; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..118
FT /note="Vesicle-associated membrane protein 1"
FT /id="PRO_0000206720"
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 68..69
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000269|PubMed:28770820"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 114..118
FT /note="IYFFT -> SKYR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029186"
FT VARIANT 64..118
FT /note="Missing (in lew)"
FT /evidence="ECO:0000269|PubMed:17102983"
SQ SEQUENCE 118 AA; 12890 MW; 31CB8701446A7FB0 CRC64;
MSAPAQPPAE GTEGAAPGGG PPGPPPNMTS NRRLQQTQAQ VEEVVDIMRV NVDKVLERDQ
KLSELDDRAD ALQAGASQFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVIYFFT
//
