VAMP8_RAT
ID VAMP8_RAT Reviewed; 100 AA.
AC Q9WUF4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Vesicle-associated membrane protein 8 {ECO:0000303|PubMed:10336434};
DE Short=VAMP-8 {ECO:0000303|PubMed:10336434};
DE AltName: Full=Endobrevin {ECO:0000250|UniProtKB:Q9BV40};
DE Short=EDB {ECO:0000250|UniProtKB:Q9BV40};
GN Name=Vamp8 {ECO:0000303|PubMed:10336434};
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], AND IDENTIFICATION IN A TERNARY COMPLEX WITH
RP STX1A AND SNAP25.
RX PubMed=10336434; DOI=10.1074/jbc.274.22.15440;
RA Fasshauer D., Antonin W., Margittai M., Pabst S., Jahn R.;
RT "Mixed and non-cognate SNARE complexes. Characterization of assembly and
RT biophysical properties.";
RL J. Biol. Chem. 274:15440-15446(1999).
RN [2]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH NAPA.
RX PubMed=9614193; DOI=10.1091/mbc.9.6.1549;
RA Wong S.H., Zhang T., Xu Y., Subramaniam V.N., Griffiths G., Hong W.;
RT "Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially
RT associated with the early endosome.";
RL Mol. Biol. Cell 9:1549-1563(1998).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11208143; DOI=10.1034/j.1600-0854.2000.010705.x;
RA Steegmaier M., Lee K.C., Prekeris R., Scheller R.H.;
RT "SNARE protein trafficking in polarized MDCK cells.";
RL Traffic 1:553-560(2000).
RN [4]
RP INTERACTION WITH STX7, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10982406; DOI=10.1091/mbc.11.9.3137;
RA Mullock B.M., Smith C.W., Ihrke G., Bright N.A., Lindsay M.,
RA Parkinson E.J., Brooks D.A., Parton R.G., James D.E., Luzio J.P.,
RA Piper R.C.;
RT "Syntaxin 7 is localized to late endosome compartments, associates with
RT Vamp 8, and Is required for late endosome-lysosome fusion.";
RL Mol. Biol. Cell 11:3137-3153(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11029036; DOI=10.1091/mbc.11.10.3289;
RA Antonin W., Holroyd C., Tikkanen R., Honing S., Jahn R.;
RT "The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes
RT and late endosomes.";
RL Mol. Biol. Cell 11:3289-3298(2000).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12414999; DOI=10.1242/jcs.00116;
RA Low S.H., Marmorstein L.Y., Miura M., Li X., Kudo N., Marmorstein A.D.,
RA Weimbs T.;
RT "Retinal pigment epithelial cells exhibit unique expression and
RT localization of plasma membrane syntaxins which may contribute to their
RT trafficking phenotype.";
RL J. Cell Sci. 115:4545-4553(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12737809; DOI=10.1016/s1534-5807(03)00122-9;
RA Low S.H., Li X., Miura M., Kudo N., Quinones B., Weimbs T.;
RT "Syntaxin 2 and endobrevin are required for the terminal step of
RT cytokinesis in mammalian cells.";
RL Dev. Cell 4:753-759(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-66 IN COMPLEX WITH STX7; STX8
RP AND VTI1B, AND INTERACTION WITH STX8.
RX PubMed=11786915; DOI=10.1038/nsb746;
RA Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.;
RT "Crystal structure of the endosomal SNARE complex reveals common structural
RT principles of all SNAREs.";
RL Nat. Struct. Biol. 9:107-111(2002).
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 (By similarity). Also required for dense-granule
CC secretion in platelets (By similarity). Also plays a role in regulated
CC enzyme secretion in pancreatic acinar cells (By similarity). Involved
CC in the abscission of the midbody during cell division, which leads to
CC completely separate daughter cells (PubMed:12737809). Involved in the
CC homotypic fusion of early and late endosomes (PubMed:10982406,
CC PubMed:11029036). Participates also in the activation of type I
CC interferon antiviral response through a TRIM6-dependent mechanism (By
CC similarity). {ECO:0000250|UniProtKB:Q9BV40,
CC ECO:0000269|PubMed:10982406, ECO:0000269|PubMed:11029036,
CC ECO:0000269|PubMed:12737809}.
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 (PubMed:10336434, PubMed:9614193,
CC PubMed:11786915). Interacts with PICALM (By similarity). SNARE complex
CC formation and binding by PICALM are mutually exclusive processes for
CC VAMP8 (By similarity). Interacts with SBF2/MTMR13 (By similarity).
CC Interacts with RAB21 (in GTP-bound form) in response to starvation; the
CC interaction probably regulates VAMP8 endolysosomal trafficking (By
CC similarity). Interacts with STX17; this interaction is increased in the
CC absence of TMEM39A (By similarity). Interacts with TRIM6 (By
CC similarity). {ECO:0000250|UniProtKB:O70404,
CC ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:10336434,
CC ECO:0000269|PubMed:11786915, ECO:0000269|PubMed:9614193}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:10982406};
CC Single-pass type IV membrane protein {ECO:0000305}. Late endosome
CC membrane {ECO:0000269|PubMed:10982406, ECO:0000269|PubMed:11029036};
CC Single-pass type IV membrane protein {ECO:0000305}. Early endosome
CC membrane {ECO:0000269|PubMed:11029036, ECO:0000269|PubMed:9614193};
CC Single-pass type IV membrane protein {ECO:0000305}. Midbody
CC {ECO:0000269|PubMed:12737809}. Cell membrane
CC {ECO:0000250|UniProtKB:O70404}; Single-pass type IV membrane protein
CC {ECO:0000305}. Zymogen granule membrane {ECO:0000250|UniProtKB:O70404};
CC Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear
CC vesicular structures of the early and late endosomes, coated pits, and
CC trans-Golgi (PubMed:9614193). Sub-tight junctional domain in retinal
CC pigment epithelium cells (PubMed:11029036). Midbody region during
CC cytokinesis (PubMed:12414999). Lumenal oriented, apical membranes of
CC nephric tubular cell (PubMed:11208143). Cycles through the apical but
CC not through the basolateral plasma membrane (By similarity). Apical
CC region of acinar cells; in zymogen granule membranes (By similarity).
CC {ECO:0000250|UniProtKB:O70404, ECO:0000269|PubMed:11029036,
CC ECO:0000269|PubMed:11208143, ECO:0000269|PubMed:12414999,
CC ECO:0000269|PubMed:12737809, ECO:0000269|PubMed:9614193}.
CC -!- TISSUE SPECIFICITY: Expressed (at protein level) at a high level in
CC kidney, lung and spleen; at a lower level in testis, liver, brain and
CC heart. Expressed in kidney and retinal pigment epithelium derived cell
CC line. {ECO:0000269|PubMed:11208143, ECO:0000269|PubMed:12414999}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF132812; AAD33595.1; -; mRNA.
DR RefSeq; NP_114015.1; NM_031827.1.
DR PDB; 1GL2; X-ray; 1.90 A; A=6-66.
DR PDBsum; 1GL2; -.
DR AlphaFoldDB; Q9WUF4; -.
DR SMR; Q9WUF4; -.
DR CORUM; Q9WUF4; -.
DR DIP; DIP-43964N; -.
DR IntAct; Q9WUF4; 8.
DR MINT; Q9WUF4; -.
DR STRING; 10116.ENSRNOP00000017301; -.
DR iPTMnet; Q9WUF4; -.
DR PhosphoSitePlus; Q9WUF4; -.
DR PaxDb; Q9WUF4; -.
DR PRIDE; Q9WUF4; -.
DR Ensembl; ENSRNOT00000096938; ENSRNOP00000083978; ENSRNOG00000012748.
DR GeneID; 83730; -.
DR KEGG; rno:83730; -.
DR UCSC; RGD:620421; rat.
DR CTD; 8673; -.
DR RGD; 620421; Vamp8.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000160325; -.
DR InParanoid; Q9WUF4; -.
DR OrthoDB; 1614157at2759; -.
DR PhylomeDB; Q9WUF4; -.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; Q9WUF4; -.
DR PRO; PR:Q9WUF4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0035577; C:azurophil granule membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0030496; C:midbody; IDA:CACAO.
DR GO; GO:0098594; C:mucin granule; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0042588; C:zymogen granule; ISO:RGD.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IPI:RGD.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0061025; P:membrane fusion; IDA:RGD.
DR GO; GO:0070254; P:mucus secretion; ISO:RGD.
DR GO; GO:1903531; P:negative regulation of secretion by cell; ISO:RGD.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:RGD.
DR GO; GO:1902278; P:positive regulation of pancreatic amylase secretion; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:RGD.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
DR GO; GO:0070625; P:zymogen granule exocytosis; ISO: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 3D-structure; 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_0000206739"
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="Binding to STX8"
FT /evidence="ECO:0000269|PubMed:11786915"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 17
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"
FT HELIX 12..62
FT /evidence="ECO:0007829|PDB:1GL2"
SQ SEQUENCE 100 AA; 11320 MW; D4449EAF44F03672 CRC64;
MEASGSAGND RVRNLQSEVE GVKNIMTQNV ERILARGENL DHLRNKTEDL EATSEHFKTT
SQKVARKFWW KNVKMIVIIC VIVLIILILI ILFATGTIPT
