VAMP1_RAT
ID VAMP1_RAT Reviewed; 118 AA.
AC Q63666; A6YSN3; O09025; Q56A22; Q8CH14;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vesicle-associated membrane protein 1;
DE Short=VAMP-1;
DE AltName: Full=Synaptobrevin-1;
GN Name=Vamp1; Synonyms=Syb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2472388; DOI=10.1016/s0021-9258(18)60426-0;
RA Elferink L.A., Trimble W.S., Scheller R.H.;
RT "Two vesicle-associated membrane protein genes are differentially expressed
RT in the rat central nervous system.";
RL J. Biol. Chem. 264:11061-11064(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9358054; DOI=10.1016/s0378-1119(97)00244-8;
RA Mandic R., Trimble W.S., Lowe A.W.;
RT "Tissue-specific alternative RNA splicing of rat vesicle-associated
RT membrane protein-1 (VAMP-1).";
RL Gene 199:173-179(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=Wistar; TISSUE=Osteoblast;
RX PubMed=12490191; DOI=10.1006/excr.2002.5668;
RA Prele C.M., Horton M.A., Caterina P., Stenbeck G.;
RT "Identification of the molecular mechanisms contributing to polarized
RT trafficking in osteoblasts.";
RL Exp. Cell Res. 282:24-34(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=Brown Norway; TISSUE=Cochlear nucleus;
RA Friedland D.R., Eernisse R., Popper P.;
RT "Identification of a novel Vamp1 splice variant in the cochlear nucleus
RT containing intra-vesicular kinase recognition sites.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 61-84, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION)
RP BY C.BOTULINUM NEUROTOXIN TYPE F.
RX PubMed=8505288; DOI=10.1016/s0021-9258(19)50230-7;
RA Schiavo G., Shone C.C., Rossetto O., Alexander F.C., Montecucco C.;
RT "Botulinum neurotoxin serotype F is a zinc endopeptidase specific for
RT VAMP/synaptobrevin.";
RL J. Biol. Chem. 268:11516-11519(1993).
RN [7]
RP PROTEIN SEQUENCE OF 94-101, AND NOT TARGET OF TETANUS OR C.BOTULINUM
RP NEUROTOXIN TYPE B.
RX PubMed=1331807; DOI=10.1038/359832a0;
RA Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P.,
RA Dasgupta B.R., Montecucco C.;
RT "Tetanus and botulinum-B neurotoxins block neurotransmitter release by
RT proteolytic cleavage of synaptobrevin.";
RL Nature 359:832-835(1992).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP D AND F.
RX PubMed=8175689; DOI=10.1016/s0021-9258(18)99941-2;
RA Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
RA Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
RT "Cleavage of members of the synaptobrevin/VAMP family by types D and F
RT botulinal neurotoxins and tetanus toxin.";
RL J. Biol. Chem. 269:12764-12772(1994).
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 -!- INTERACTION:
CC Q63666; G3V7P1: Stx12; NbExp=3; IntAct=EBI-2029956, EBI-915654;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane; Single-pass type IV membrane
CC protein. Synapse, synaptosome {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle membrane;
CC Single-pass type IV membrane protein. Note=Isoforms 2 and 3 are found
CC in perinuclear as well as peripheral punctate structures in
CC osteoblasts.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane;
CC Single-pass type IV membrane protein. Note=Isoforms 2 and 3 are found
CC in perinuclear as well as peripheral punctate structures in
CC osteoblasts. {ECO:0000250|UniProtKB:P23763}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Vamp1a;
CC IsoId=Q63666-1; Sequence=Displayed;
CC Name=2; Synonyms=Vamp1b;
CC IsoId=Q63666-2; Sequence=VSP_029188;
CC Name=3; Synonyms=Vamp1-ob;
CC IsoId=Q63666-3; Sequence=VSP_029187;
CC Name=4;
CC IsoId=Q63666-4; Sequence=VSP_029189;
CC -!- TISSUE SPECIFICITY: Expressed in brain and spleen (at protein level).
CC Isoform 1 expressed at very high level in brain. Even higher level
CC found in spinal cord. Isoform 3 expressed in kidney, spleen and liver.
CC Isoforms 2 and 3 expressed in osteoblasts of trabecular bone. Also
CC expressed in heart. {ECO:0000269|PubMed:9358054}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type D (BoNT/D, botD) which hydrolyzes the 61-Lys-|-Leu-62
CC bond and inhibits neurotransmitter release (PubMed:8175689). This is a
CC poor substrate for BoNT/D, high concentrations are required to cleave
CC it in vitro (PubMed:8175689). {ECO:0000269|PubMed:1331807}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type F (BoNT/F, botF) which hydrolyzes the 60-Gln-|-Lys-61
CC bond and inhibits neurotransmitter release (PubMed:8505288).
CC {ECO:0000269|PubMed:1331807, ECO:0000269|PubMed:8505288,
CC ECO:0000305|PubMed:8175689}.
CC -!- MISCELLANEOUS: Is not targeted by C.botulinum neurotoxin type B
CC (BoNT/B) or by C.tetani toxin (tetX) as their target sequence is not
CC conserved in this protein (PubMed:1331807, PubMed:8175689).
CC {ECO:0000269|PubMed:1331807, ECO:0000269|PubMed:8175689}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M24104; AAA42322.1; -; mRNA.
DR EMBL; U74621; AAC53427.1; -; mRNA.
DR EMBL; AF498262; AAN85832.1; -; mRNA.
DR EMBL; EF653274; ABR68027.1; -; mRNA.
DR EMBL; EF653275; ABR68028.1; -; mRNA.
DR EMBL; BC092206; AAH92206.1; -; mRNA.
DR PIR; A34288; A34288.
DR RefSeq; NP_037222.2; NM_013090.2. [Q63666-1]
DR AlphaFoldDB; Q63666; -.
DR SMR; Q63666; -.
DR BioGRID; 247653; 2.
DR IntAct; Q63666; 6.
DR MINT; Q63666; -.
DR STRING; 10116.ENSRNOP00000025081; -.
DR iPTMnet; Q63666; -.
DR PhosphoSitePlus; Q63666; -.
DR SwissPalm; Q63666; -.
DR PaxDb; Q63666; -.
DR PRIDE; Q63666; -.
DR Ensembl; ENSRNOT00000025081; ENSRNOP00000025081; ENSRNOG00000019219. [Q63666-1]
DR Ensembl; ENSRNOT00000096098; ENSRNOP00000076937; ENSRNOG00000019219. [Q63666-4]
DR GeneID; 25624; -.
DR KEGG; rno:25624; -.
DR UCSC; RGD:3948; rat. [Q63666-1]
DR CTD; 6843; -.
DR RGD; 3948; Vamp1.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000161390; -.
DR HOGENOM; CLU_064620_4_0_1; -.
DR InParanoid; Q63666; -.
DR OMA; WESPRIF; -.
DR OrthoDB; 1606985at2759; -.
DR PhylomeDB; Q63666; -.
DR TreeFam; TF313666; -.
DR PRO; PR:Q63666; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000019219; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q63666; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0070821; C:tertiary granule membrane; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; TAS:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:RGD.
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; Cytoplasmic vesicle;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT CHAIN 1..118
FT /note="Vesicle-associated membrane protein 1"
FT /id="PRO_0000206721"
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..38
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:0000269|PubMed:1331807,
FT ECO:0000269|PubMed:8505288"
FT SITE 61..62
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type D (BoNT/D, botD)"
FT /evidence="ECO:0000269|PubMed:8175689"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62442"
FT VAR_SEQ 114..118
FT /note="IYIFT -> SKYR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12490191,
FT ECO:0000303|PubMed:9358054"
FT /id="VSP_029188"
FT VAR_SEQ 114..118
FT /note="IYIFT -> RQD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12490191, ECO:0000303|Ref.4"
FT /id="VSP_029187"
FT VAR_SEQ 114..118
FT /note="IYIFT -> NSGTEDRSCSVCFGSFC (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_029189"
FT CONFLICT 48
FT /note="M -> I (in Ref. 1; AAA42322)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="R -> C (in Ref. 5; AAH92206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 12797 MW; E34D4D735CFBF6A8 CRC64;
MSAPAQPPAE GTEGAAPGGG PPGPPPNTTS NRRLQQTQAQ VEEVVDIMRV NVDKVLERDQ
KLSELDDRAD ALQAGASVFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVIYIFT
