ID   CXP3_PARCG              Reviewed;          93 AA.
AC   A0A0P0BZQ8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Parbolysin P3 {ECO:0000303|PubMed:26435341};
DE   AltName: Full=Parbolysin 3;
OS   Parborlasia corrugatus (Antarctic nemertean worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Nemertea; Pilidiophora;
OC   Heteronemertea; Lineidae; Parborlasia.
OX   NCBI_TaxID=187802;
RN   [1] {ECO:0000312|EMBL:ALI86907.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=26435341; DOI=10.1016/j.toxicon.2015.09.044;
RA   Butala M., Sega D., Tomc B., Podlesek Z., Kem W.R., Kupper F.C., Turk T.;
RT   "Recombinant expression and predicted structure of parborlysin, a cytolytic
RT   protein from the Antarctic heteronemertine Parborlasia corrugatus.";
RL   Toxicon 108:32-37(2015).
CC   -!- FUNCTION: Cytolysin that shows hemolytic activity (on bovine
CC       erythrocytes, HC(50)=5.75 mg/ml). This hemolytic activity is completely
CC       inhibited by small unilamelar vesicles composed of PC/PG, PC/PI and
CC       PC/PS in 1:1 molar ratios (with at least 100 mg/ml concentration).
CC       {ECO:0000250|UniProtKB:A0A0N7HUN6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26435341}.
CC   -!- TISSUE SPECIFICITY: Localized within the skin and proboscis and are
CC       most readily isolated from body mucus secretions.
CC       {ECO:0000305|PubMed:26435341}.
CC   -!- SIMILARITY: Belongs to the worm cytolysin family. {ECO:0000305}.
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DR   EMBL; KT693316; ALI86907.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cytolysis; Disulfide bond; Hemolysis; Secreted; Toxin.
FT   CHAIN           1..93
FT                   /note="Parbolysin P3"
FT                   /evidence="ECO:0000305|PubMed:26435341"
FT                   /id="PRO_0000454512"
FT   DISULFID        16..37
FT                   /evidence="ECO:0000250|UniProtKB:P01527"
FT   DISULFID        22..33
FT                   /evidence="ECO:0000250|UniProtKB:P01527"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P01527"
SQ   SEQUENCE   93 AA;  9638 MW;  258DB6A291B80223 CRC64;
     GWPAYPGSNG IRSSVCQKKL GCGSKNLASL GVCKAFCPGR KRFWQKCGKN GSSGKGSRIC
     NPVPAHAVEK AGKGLIKVTD MAVAAIAKYA GKK