Descriptions

VAMP7 is involved in the targeting and/or fusion of transport vesicles to their target membrane. Longin domain negatively regulates the ability of VAMP7 like other SNARE attachment proteins including Ykt6.

Autoinhibitory domains (AIDs)

Target domain

125-185 (v-SNARE coiled-coil homology)

Relief mechanism

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q17QI5

Entry ID Method Resolution Chain Position Source
AF-Q17QI5-F1 Predicted AlphaFoldDB

No variants for Q17QI5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q17QI5

No associated diseases with Q17QI5

No regional properties for Q17QI5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q17QI5

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass type IV membrane protein
  • Golgi apparatus, trans-Golgi network membrane ; Single-pass type IV membrane protein
  • Late endosome membrane ; Single-pass type IV membrane protein
  • Lysosome membrane ; Single-pass type IV membrane protein
  • Endoplasmic reticulum membrane ; Single-pass type IV membrane protein
  • Cytoplasmic vesicle, phagosome membrane ; Single-pass type IV membrane protein
  • Synapse, synaptosome
  • In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region
  • Colocalizes with LAMP1 in kidney cells
  • Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
late endosome membrane The lipid bilayer surrounding a late endosome.
lysosomal membrane The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
phagocytic vesicle membrane The lipid bilayer surrounding a phagocytic vesicle.
SNARE complex A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
transport vesicle membrane The lipid bilayer surrounding a transport vesicle.

2 GO annotations of molecular function

Name Definition
SNAP receptor activity Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.

10 GO annotations of biological process

Name Definition
calcium-ion regulated exocytosis The release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle by fusion of the vesicle with the plasma membrane of a cell, induced by a rise in cytosolic calcium-ion levels.
endoplasmic reticulum to Golgi vesicle-mediated transport The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
endosome to lysosome transport The directed movement of substances from endosomes to lysosomes.
eosinophil degranulation The regulated exocytosis of secretory granules containing preformed mediators such as major basic protein, eosinophil peroxidase, and eosinophil cationic protein by an eosinophil.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
neutrophil degranulation The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
phagocytosis, engulfment The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
vesicle fusion Fusion of the membrane of a transport vesicle with its target membrane.
vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12255 NYV1 Vacuolar v-SNARE NYV1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q5ZL74 VAMP7 Vesicle-associated membrane protein 7 Gallus gallus (Chicken) SS
P51809 VAMP7 Vesicle-associated membrane protein 7 Homo sapiens (Human) EV
P70280 Vamp7 Vesicle-associated membrane protein 7 Mus musculus (Mouse) SS
Q9JHW5 Vamp7 Vesicle-associated membrane protein 7 Rattus norvegicus (Rat) SS
Q9FMR5 VAMP714 Vesicle-associated membrane protein 714 Arabidopsis thaliana (Mouse-ear cress) PR
O49377 VAMP711 Vesicle-associated membrane protein 711 Arabidopsis thaliana (Mouse-ear cress) SS
Q9LFP1 VAMP713 Vesicle-associated membrane protein 713 Arabidopsis thaliana (Mouse-ear cress) SS
Q9SIQ9 VAMP712 Vesicle-associated membrane protein 712 Arabidopsis thaliana (Mouse-ear cress) SS
Q9M376 VAMP727 Vesicle-associated membrane protein 727 Arabidopsis thaliana (Mouse-ear cress) SS
10 20 30 40 50 60
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI
70 80 90 100 110 120
VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN
130 140 150 160 170 180
KGLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR
190 200 210
AMCMKNLKLT IIIIIISVVF IYIIVSPLCG GFTWPNCVKK