P0C8G7 (PV22_POMCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Perivitellin-2 31 kDa subunit Short name=PV2 31 kDa subunit
Organism	Pomacea canaliculata (Golden apple snail)
Taxonomic identifier	400727 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Gastropoda › Caenogastropoda › Architaenioglossa › Ampullarioidea › Ampullariidae › Pomacea

Protein attributes

Sequence length	15 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is a source of both structural and energetic molecules during embryonic development. Ref.3 Ref.6 Neurotoxin. Intraperitoneal injection into mice causes damage mostly in spinal cord. Ref.3 Ref.6
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.2 Ref.7
Tissue specificity	Produced by albumen secretory cells. Found in developing eggs. Ref.5
Developmental stage	Albumen secretory cells produce perivitellin-2 during the reproductive period. Ref.5
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.4 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.6
Miscellaneous	Mice receiving sublethal doses of toxin become immunized towards the toxin and doses up to LD(100) do not kill them.

Ontologies

Keywords
Molecular function	Neurotoxin Storage protein Toxin
PTM	Disulfide bond Glycoprotein Lipoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular_function	nutrient reservoir activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›15	›15	Perivitellin-2 31 kDa subunit		PRO_0000355072
Experimental info
	Non-terminal residue	15	1

Sequences

	Sequence		Length	Mass (Da)
	P0C8G7 [UniParc]. Last modified November 25, 2008. Version 1. Checksum: 7B142696B974486A	FASTA	15	1,907
	10 FTSVKMPRDE HWPYN

References

[1]	"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. Tissue: Albumen gland.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

PV22_POMCA

Accession

Primary (citable) accession number: P0C8G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	November 25, 2008
Last modified:	October 3, 2012
This is version 8 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program