PV21_POMCA
ID PV21_POMCA Reviewed; 565 AA.
AC P0C8G6; M1TA54;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Perivitellin-2 67 kDa subunit {ECO:0000305};
DE Short=PcPV2 67 kDa subunit {ECO:0000305};
DE Short=PcPV2-67 {ECO:0000303|PubMed:23737950};
DE AltName: Full=PV2 MACPF subunit {ECO:0000305};
DE Flags: Precursor;
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Albumen gland;
RX PubMed=23737950; DOI=10.1371/journal.pone.0063782;
RA Dreon M.S., Frassa M.V., Ceolin M., Ituarte S., Qiu J.W., Sun J.,
RA Fernandez P.E., Heras H.;
RT "Novel animal defenses against predation: a snail egg neurotoxin combining
RT lectin and pore-forming chains that resembles plant defense and bacteria
RT attack toxins.";
RL PLoS ONE 8:E63782-E63782(2013).
RN [2]
RP PROTEIN SEQUENCE OF 27-44.
RC TISSUE=Albumen gland;
RX PubMed=11857466; DOI=10.1002/jez.10043;
RA Dreon M., Lavarias S., Garin C.F., Heras H., Pollero R.J.;
RT "Synthesis, distribution, and levels of an egg lipoprotein from the apple
RT snail Pomacea canaliculata (Mollusca: Gastropoda).";
RL J. Exp. Zool. 292:323-330(2002).
RN [3]
RP SUBUNIT, AND LIPID COMPOSITION.
RX PubMed=8972583;
RX DOI=10.1002/(sici)1097-010x(19961201)276:5<307::aid-jez1>3.0.co;2-s;
RA Garin C.F., Heras H., Pollero R.J.;
RT "Lipoproteins of the egg perivitelline fluid of Pomacea canaliculata snails
RT (Mollusca: Gastropoda).";
RL J. Exp. Zool. 276:307-314(1996).
RN [4]
RP FUNCTION.
RA Heras H., Garin C.F., Pollero R.J.;
RT "Biochemical composition and energy sources during embryo development and
RT in early juveniles of the snail Pomacea canaliculata (Mollusca:
RT Gastropoda).";
RL J. Exp. Zool. 280:375-383(1998).
RN [5]
RP CARBOHYDRATE COMPOSITION.
RX PubMed=15112330; DOI=10.1002/mrd.20078;
RA Dreon M.S., Heras H., Pollero R.J.;
RT "Characterization of the major egg glycolipoproteins from the perivitellin
RT fluid of the apple snail Pomacea canaliculata.";
RL Mol. Reprod. Dev. 68:359-364(2004).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16453107; DOI=10.1007/s00441-005-0132-x;
RA Catalan M., Dreon M.S., Heras H., Pollero R.J., Fernandez S.N., Winik B.;
RT "Pallial oviduct of Pomacea canaliculata (Gastropoda): ultrastructural
RT studies of the parenchymal cellular types involved in the metabolism of
RT perivitellins.";
RL Cell Tissue Res. 324:523-533(2006).
RN [7]
RP FUNCTION, AND TOXIC DOSE.
RX PubMed=18640143; DOI=10.1016/j.toxicon.2008.06.022;
RA Heras H., Frassa M.V., Fernandez P.E., Galosi C.M., Gimeno E.J.,
RA Dreon M.S.;
RT "First egg protein with a neurotoxic effect on mice.";
RL Toxicon 52:481-488(2008).
RN [8]
RP SUBUNIT.
RX PubMed=20215051; DOI=10.1016/j.bbapap.2010.02.013;
RA Frassa M.V., Ceolin M., Dreon M.S., Heras H.;
RT "Structure and stability of the neurotoxin PV2 from the eggs of the apple
RT snail Pomacea canaliculata.";
RL Biochim. Biophys. Acta 1804:1492-1499(2010).
CC -!- FUNCTION: The egg defensive protein perivitellin-2 is a pore-forming
CC two-subunit glycoprotein that affects both the nervous and digestive
CC systems of mammals (PubMed:23737950, PubMed:18640143). In addition, it
CC is a source of both structural and energetic molecules during embryonic
CC development (Probable). The tachylectin subunit (31 kDa) binds target
CC membranes while the MACPF subunit (67 kDa) disrupts lipid bilayers
CC forming large pores altering the plasma membrance conductance
CC (PubMed:23737950). Both in vivo and in vitro, the protein shows wide pH
CC range stability and is resistant to enzymatic proteolysis from
CC gastrointestinal environments (PubMed:23737950). It specifically binds
CC mature enterocytes but does not cause cell disruption on caco-2 (human
CC colorectal adenocarcinoma cells) or rat intestinal cells
CC (PubMed:23737950). After oral administration to mice, it binds
CC enterocytes and induces large dose-dependent morphological changes on
CC their small intestine mucosa, reducing the absorptive surface (By
CC similarity). Additionally, it is detected in the Peyer's patches where
CC it activates lymphoid follicles and triggers apoptosis (By similarity).
CC The toxin can also traverse the intestinal barrier and induce oral
CC adaptive immunity with evidence of circulating antibody response
CC (PubMed:23737950). The toxin also shows hemagglutination properties
CC thanks to the tachylectin subunit, but does not show hemolytic activity
CC (PubMed:23737950). In addition to enterotoxin activity, the toxin also
CC acts as a neurotoxin, since an intraperitoneal injection induces
CC paralysis of the mice rear limbs, followed by death (PubMed:23737950).
CC {ECO:0000250|UniProtKB:P0DQO9, ECO:0000269|PubMed:18640143,
CC ECO:0000269|PubMed:23737950, ECO:0000305|Ref.4}.
CC -!- SUBUNIT: Perivitellin-2 is a heterooctamer of 4 identical 98 kDa
CC heterodimers, each composed of one 31 kDa and one 67 kDa subunits. The
CC 98 kDa heterodimer subunits are held together by disulfide bridges
CC while the heterodimers are assembled into the native perivitellin-2
CC octamer by non-covalent forces. {ECO:0000269|PubMed:20215051,
CC ECO:0000269|PubMed:8972583}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000269|PubMed:23737950}.
CC -!- TISSUE SPECIFICITY: Produced by albumen secretory cells. Found in
CC developing eggs. {ECO:0000269|PubMed:16453107}.
CC -!- DEVELOPMENTAL STAGE: Albumen secretory cells produce perivitellin-2
CC during the reproductive period. {ECO:0000269|PubMed:16453107}.
CC -!- PTM: Glycosylated. Contains four O-linked and one N-linked
CC oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high
CC levels of mannose, galactose, and NAcGlucosamine, and small amounts of
CC NacGalactosamine). {ECO:0000269|PubMed:15112330}.
CC -!- PTM: PV2 is a very high density lipoprotein (VHDL). It contains 3.75%
CC of lipids. The major lipid classes are free sterols and phospholipids
CC and also have significant quantities of energy-providing
CC triacylglycerides and free fatty acids. {ECO:0000269|PubMed:8972583}.
CC -!- TOXIC DOSE: LD(50) is 250 ug/kg by intraperitoneal injection into mice.
CC {ECO:0000269|PubMed:18640143}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A snail's sting - Issue 100
CC of December 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/100";
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DR EMBL; JX155861; AGG40751.1; -; mRNA.
DR AlphaFoldDB; P0C8G6; -.
DR SASBDB; P0C8G6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR020863; MACPF_CS.
DR Pfam; PF01823; MACPF; 1.
DR PROSITE; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Enterotoxin; Glycoprotein;
KW Hemagglutinin; Lipoprotein; Membrane; Neurotoxin; Secreted; Signal;
KW Storage protein; Target cell membrane; Target membrane; Toxin.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11857466"
FT CHAIN 27..565
FT /note="Perivitellin-2 67 kDa subunit"
FT /id="PRO_0000355071"
FT DOMAIN 27..340
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DISULFID 398
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P0DQO9"
SQ SEQUENCE 565 AA; 62518 MW; ED003AC8B36F1486 CRC64;
MSQLRWWVVS QLLLLIVVCI LDHSEGARVC PKIVPGLDKL RVGVDITKLD LLPLFDLGDN
GFRSAVADYT CDRGQTTVVD GESFDVPDQV DSVVIESSGQ QTSSVTTIKS ESQISQALSI
SAGISVDTAK AGFSSSASYA EMQEAITKYG RTVSQMSAVY TTCSANLSPN LLLGQNPLQT
LSRLPSDFTA DTEGYYDFIK TYGTHYFNKG KLGGMFLFTS ETDMSYFQNK NSQQVEANIK
ATFASILSTE TGGSSDQSKE VIEFKESSLI TAKFFGGRTN LAADGLTKWQ PTIAKLPYFM
SGTLSTISSL IADTTKRASM ELAVKNYLLK AKVANLDRLT YIRLNSWTVG HNELRDLSAQ
LQNLKKKTIF SDEDEKLLQS IEDQVSVPAW FSDRTTFCFR STAVGSADQC NGQSTSTLCA
EPNRYTQQYM DKTYLGDTGC RLVWKLSTTE SSDWFKSVKV NFRWYPTWSP CACGPVGTPF
TISAPANSWT QDYLDVTNPK FGECMLQWMI EVPPTATLWA KNLEFCIDFT CGKKKQCVDA
NHWTEPYLDI SAHEACGMSW ALIAK
