VAMP8_BOVIN
ID VAMP8_BOVIN Reviewed; 100 AA.
AC Q3T0Y8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Vesicle-associated membrane protein 8 {ECO:0000250|UniProtKB:Q9BV40};
DE Short=VAMP-8 {ECO:0000250|UniProtKB:Q9BV40};
DE AltName: Full=Endobrevin {ECO:0000250|UniProtKB:Q9BV40};
DE Short=EDB {ECO:0000250|UniProtKB:Q9BV40};
GN Name=VAMP8 {ECO:0000250|UniProtKB:Q9BV40};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment
CC protein receptors, are essential proteins for fusion of cellular
CC membranes. SNAREs localized on opposing membranes assemble to form a
CC trans-SNARE complex, an extended, parallel four alpha-helical bundle
CC that drives membrane fusion. VAMP8 is a SNARE involved in autophagy
CC through the direct control of autophagosome membrane fusion with the
CC lysososome membrane via its interaction with the STX17-SNAP29 binary t-
CC SNARE complex. Also required for dense-granule secretion in platelets.
CC Also plays a role in regulated enzyme secretion in pancreatic acinar
CC cells. Involved in the abscission of the midbody during cell division,
CC which leads to completely separate daughter cells. Involved in the
CC homotypic fusion of early and late endosomes. Participates also in the
CC activation of type I interferon antiviral response through a TRIM6-
CC dependent mechanism (By similarity). {ECO:0000250|UniProtKB:Q9BV40}.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome (By similarity).
CC Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A,
CC STX4, STX7, STX8 and VTI1B (By similarity). Interacts with PICALM (By
CC similarity). SNARE complex formation and binding by PICALM are mutually
CC exclusive processes for VAMP8 (By similarity). Interacts with
CC SBF2/MTMR13 (By similarity). Interacts with RAB21 (in GTP-bound form)
CC in response to starvation; the interaction probably regulates VAMP8
CC endolysosomal trafficking (By similarity). Interacts with STX17; this
CC interaction is increased in the absence of TMEM39A (By similarity).
CC Interacts with TRIM6 (By similarity). {ECO:0000250|UniProtKB:O70404,
CC ECO:0000250|UniProtKB:Q9BV40}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9WUF4};
CC Single-pass type IV membrane protein {ECO:0000305}. Late endosome
CC membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane
CC protein {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:O70404}; Single-
CC pass type IV membrane protein {ECO:0000305}. Zymogen granule membrane
CC {ECO:0000250|UniProtKB:O70404}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=Perinuclear vesicular structures of the early and
CC late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight
CC junctional domain in retinal pigment epithelium cells (By similarity).
CC Midbody region during cytokinesis (By similarity). Lumenal oriented,
CC apical membranes of nephric tubular cell (By similarity). Cycles
CC through the apical but not through the basolateral plasma membrane (By
CC similarity). Apical region of acinar cells; in zymogen granule
CC membranes (By similarity). {ECO:0000250|UniProtKB:Q9WUF4}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; BC102203; AAI02204.1; -; mRNA.
DR RefSeq; NP_001029462.1; NM_001034290.2.
DR RefSeq; XP_005212816.1; XM_005212759.3.
DR AlphaFoldDB; Q3T0Y8; -.
DR SMR; Q3T0Y8; -.
DR STRING; 9913.ENSBTAP00000032965; -.
DR PaxDb; Q3T0Y8; -.
DR PRIDE; Q3T0Y8; -.
DR Ensembl; ENSBTAT00000033040; ENSBTAP00000032965; ENSBTAG00000023997.
DR GeneID; 507309; -.
DR KEGG; bta:507309; -.
DR CTD; 8673; -.
DR VEuPathDB; HostDB:ENSBTAG00000023997; -.
DR VGNC; VGNC:36760; VAMP8.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000160325; -.
DR HOGENOM; CLU_064620_5_0_1; -.
DR InParanoid; Q3T0Y8; -.
DR OMA; KQTSHKV; -.
DR OrthoDB; 1614157at2759; -.
DR TreeFam; TF320419; -.
DR Reactome; R-BTA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000023997; Expressed in metanephros cortex and 101 other tissues.
DR GO; GO:0035577; C:azurophil granule membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0098594; C:mucin granule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0070254; P:mucus secretion; IBA:GO_Central.
DR GO; GO:1903531; P:negative regulation of secretion by cell; IEA:Ensembl.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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 3: Inferred from homology;
KW Antiviral defense; Autophagy; Cell membrane; Coiled coil;
KW Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..100
FT /note="Vesicle-associated membrane protein 8"
FT /id="PRO_0000273718"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..100
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 11..71
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT SITE 32
FT /note="Interaction with STX8"
FT /evidence="ECO:0000250|UniProtKB:Q9WUF4"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
SQ SEQUENCE 100 AA; 11357 MW; B117EA8A34E10701 CRC64;
MEASGGGGDD RVRNLRDEVE GVKNIMTQNV ERILARGENL DHLRNKTEDL EATSEHFKTT
SQKVARKFWW KNVKMIVLIC VIVFIIILFI VLFATGAIPT
