P0C8G7 · PV22_POMCA
- ProteinPerivitellin-2 31 kDa subunit
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids286 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals (PubMed:18640143, PubMed:23737950).
In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin subunit (31 kDa) binds target membranes while the MACPF subunit (67 kDa) disrupts lipid bilayers forming large pores altering the plasma membrance conductance (PubMed:23737950).
Both in vivo and in vitro, the protein shows wide pH range stability and is resistant to enzymatic proteolysis from gastrointestinal environments (PubMed:23737950).
It specifically binds mature enterocytes but does not cause cell disruption on caco-2 (human colorectal adenocarcinoma cells) or rat intestinal cells (PubMed:23737950).
After oral administration to mice, it binds enterocytes and induces large dose-dependent morphological changes on their small intestine mucosa, reducing the absorptive surface (By similarity).
Additionally, it is detected in the Peyer's patches where it activates lymphoid follicles and triggers apoptosis (By similarity).
The toxin can also traverse the intestinal barrier and induce oral adaptive immunity with evidence of circulating antibody response (PubMed:23737950).
The toxin also shows hemagglutination properties thanks to the tachylectin subunit, but does not show hemolytic activity (PubMed:23737950).
In addition to enterotoxin activity, the toxin also acts as a neurotoxin, since an intraperitoneal injection induces paralysis of the mice rear limbs, followed by death (PubMed:23737950).
In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin subunit (31 kDa) binds target membranes while the MACPF subunit (67 kDa) disrupts lipid bilayers forming large pores altering the plasma membrance conductance (PubMed:23737950).
Both in vivo and in vitro, the protein shows wide pH range stability and is resistant to enzymatic proteolysis from gastrointestinal environments (PubMed:23737950).
It specifically binds mature enterocytes but does not cause cell disruption on caco-2 (human colorectal adenocarcinoma cells) or rat intestinal cells (PubMed:23737950).
After oral administration to mice, it binds enterocytes and induces large dose-dependent morphological changes on their small intestine mucosa, reducing the absorptive surface (By similarity).
Additionally, it is detected in the Peyer's patches where it activates lymphoid follicles and triggers apoptosis (By similarity).
The toxin can also traverse the intestinal barrier and induce oral adaptive immunity with evidence of circulating antibody response (PubMed:23737950).
The toxin also shows hemagglutination properties thanks to the tachylectin subunit, but does not show hemolytic activity (PubMed:23737950).
In addition to enterotoxin activity, the toxin also acts as a neurotoxin, since an intraperitoneal injection induces paralysis of the mice rear limbs, followed by death (PubMed:23737950).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | other organism cell membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | nutrient reservoir activity | |
Molecular Function | toxin activity |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended namePerivitellin-2 31 kDa subunit
- Short namesPcPV2 31 kDa subunit ; PcPV2-31
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Gastropoda > Caenogastropoda > Architaenioglossa > Ampullarioidea > Ampullariidae > Pomacea
Accessions
- Primary accessionP0C8G7
- Secondary accessions
Subcellular Location
Phenotypes & Variants
Toxic dose
LD50 is 250 ug/kg by intraperitoneal injection into mice.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MVKKIHFIMERHASIVAFLLAVLALTESQA | ||||||
Chain | PRO_0000355072 | 31-286 | Perivitellin-2 31 kDa subunit | |||
Sequence: FTSVKLPRDEHWPYNYVSIGPAGVWAVNRQNKLFYRTGTYGDNANMGSGWQFKQDGVGQVDVGKDKVGYINLSGGSLFRIDGISQGNPVGGSPKSWEWWTKYIGMSLREDTRFSSRIENQNKVLTFTFRTCFWASRITNWCFADSSYTETVTAGGSGTWITKSQLKYKSGTFGNPDTEGGDWITVDSGSFQHVSSGSGVVLAVRSNGELVKRTGITCSLPQGSGWTSMLNGMSRVDTYGTVAWAVDTYGDLYFINL | ||||||
Glycosylation | 101 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 161 | Interchain | ||||
Sequence: C |
Post-translational modification
Glycosylated. PV2 contains four O-linked and one N-linked oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high levels of mannose, galactose, and NAcGlucosamine, and small amounts of NacGalactosamine).
PV2 is a very high density lipoprotein (VHDL). It contains 3.75% of lipids. The major lipid classes are free sterols and phospholipids and also have significant quantities of energy-providing triacylglycerides and free fatty acids.
Keywords
- PTM
Expression
Tissue specificity
Produced by albumen secretory cells. Found in developing eggs.
Developmental stage
Albumen secretory cells produce perivitellin-2 during the reproductive period.
Interaction
Subunit
Perivitellin-2 is a heterooctamer of 4 identical 98 kDa heterodimers, each composed of one 31 kDa and one 67 kDa subunits. The 98 kDa heterodimer subunits are held together by disulfide bridges while the heterodimers are assembled into the native perivitellin-2 octamer by non-covalent forces.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length286
- Mass (Da)31,584
- Last updated2013-07-24 v2
- Checksum3DB891F4E71253CC
Keywords
- Technical term