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P0C8G7 (PV22_POMCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perivitellin-2 31 kDa subunit

Short name=PcPV2 31 kDa subunit
Short name=PcPV2-31
Alternative name(s):
PV2 tachylectin subunit
OrganismPomacea canaliculata (Golden apple snail)
Taxonomic identifier400727 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaArchitaenioglossaAmpullarioideaAmpullariidaePomacea

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is a source of both structural and energetic molecules during embryonic development. Ref.4 Ref.7

Neurotoxin present in eggs that is lethal when ingested. Shows wide pH range stability and is resistant to proteases trypsin and pepsin (gastric and intestinal digestion). Specifically binds mature enterocytes (binding due to the tachylectin subunit). May traverse the intestinal barrier, since it is able to orally stimulate the immune system in rats and mice. Also shows hemagglutinating activity against rabbit erythrocytes. Ref.4 Ref.7

Subunit structure

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. Ref.3 Ref.8

Tissue specificity

Produced by albumen secretory cells. Found in developing eggs. Ref.6

Developmental stage

Albumen secretory cells produce perivitellin-2 during the reproductive period. Ref.6

Post-translational modification

Glycosylated. 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). Ref.5

Very high density lipoprotein (VHDL). 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.

Toxic dose

LD50 is 250 µg/kg by intraperitoneal injection into mice. Ref.7

Miscellaneous

Mice receiving sublethal doses of toxin become immunized towards the toxin and doses up to LD(100) do not kill them.

Does not show hemolytic activity nor caco-2 (human colorectal adenocarcinoma cells) or rat intestinal cell disruption activity (Ref.1).

Ontologies

Keywords
   DomainSignal
   LigandLectin
   Molecular functionHemagglutinin
Neurotoxin
Storage protein
Toxin
   PTMDisulfide bond
Glycoprotein
Lipoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionnutrient reservoir activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.2
Chain31 – 286256Perivitellin-2 31 kDa subunit
PRO_0000355072

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P0C8G7 [UniParc].

Last modified July 24, 2013. Version 2.
Checksum: 3DB891F4E71253CC

FASTA28631,584
        10         20         30         40         50         60 
MVKKIHFIME RHASIVAFLL AVLALTESQA FTSVKLPRDE HWPYNYVSIG PAGVWAVNRQ 

        70         80         90        100        110        120 
NKLFYRTGTY GDNANMGSGW QFKQDGVGQV DVGKDKVGYI NLSGGSLFRI DGISQGNPVG 

       130        140        150        160        170        180 
GSPKSWEWWT KYIGMSLRED TRFSSRIENQ NKVLTFTFRT CFWASRITNW CFADSSYTET 

       190        200        210        220        230        240 
VTAGGSGTWI TKSQLKYKSG TFGNPDTEGG DWITVDSGSF QHVSSGSGVV LAVRSNGELV 

       250        260        270        280 
KRTGITCSLP QGSGWTSMLN GMSRVDTYGT VAWAVDTYGD LYFINL 

« Hide

References

[1]"Novel animal defenses against predation: a snail egg neurotoxin combining lectin and pore-forming chains that resembles plant defense and bacteria attack toxins."
Dreon M.S., Frassa M.V., Ceolin M., Ituarte S., Qiu J.W., Sun J., Fernandez P.E., Heras H.
PLoS ONE 8:E63782-E63782(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Albumen gland.
[2]"Synthesis, distribution, and levels of an egg lipoprotein from the apple snail Pomacea canaliculata (Mollusca: Gastropoda)."
Dreon M., Lavarias S., Garin C.F., Heras H., Pollero R.J.
J. Exp. Zool. 292:323-330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-45.
Tissue: Albumen gland.
[3]"Lipoproteins of the egg perivitelline fluid of Pomacea canaliculata snails (Mollusca: Gastropoda)."
Garin C.F., Heras H., Pollero R.J.
J. Exp. Zool. 276:307-314(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, LIPID COMPOSITION.
[4]"Biochemical composition and energy sources during embryo development and in early juveniles of the snail Pomacea canaliculata (Mollusca: Gastropoda)."
Heras H., Garin C.F., Pollero R.J.
J. Exp. Zool. 280:375-383(1998)
Cited for: FUNCTION.
[5]"Characterization of the major egg glycolipoproteins from the perivitellin fluid of the apple snail Pomacea canaliculata."
Dreon M.S., Heras H., Pollero R.J.
Mol. Reprod. Dev. 68:359-364(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CARBOHYDRATE COMPOSITION, GLYCOSYLATION PATTERN.
[6]"Pallial oviduct of Pomacea canaliculata (Gastropoda): ultrastructural studies of the parenchymal cellular types involved in the metabolism of perivitellins."
Catalan M., Dreon M.S., Heras H., Pollero R.J., Fernandez S.N., Winik B.
Cell Tissue Res. 324:523-533(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"First egg protein with a neurotoxic effect on mice."
Heras H., Frassa M.V., Fernandez P.E., Galosi C.M., Gimeno E.J., Dreon M.S.
Toxicon 52:481-488(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LETHAL DOSE.
[8]"Structure and stability of the neurotoxin PV2 from the eggs of the apple snail Pomacea canaliculata."
Frassa M.V., Ceolin M., Dreon M.S., Heras H.
Biochim. Biophys. Acta 1804:1492-1499(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.

Web resources

Protein Spotlight

A snail's sting - Issue 100 of December 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JX155862 mRNA. Translation: AGG40752.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006624. Beta-propeller_rpt_TECPR.
[Graphical view]
SMARTSM00706. TECPR. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePV22_POMCA
AccessionPrimary (citable) accession number: P0C8G7
Secondary accession number(s): M1TI98
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 24, 2013
Last modified: February 19, 2014
This is version 11 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries