ID   CXP1_PARCG              Reviewed;          93 AA.
AC   A0A0P0BQD2;
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 P1 {ECO:0000303|PubMed:26435341};
DE   AltName: Full=Parbolysin 1;
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:ALI86905.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], RECOMBINANT EXPRESSION IN E.COLI, AND
RP   3D-STRUCTURE MODELING.
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) (By similarity). This hemolytic
CC       activity is completely inhibited by small unilamelar vesicles composed
CC       of PC/PG, PC/PI and PC/PS in 1:1 molar ratios (with at least 100 mg/ml
CC       concentration) (By similarity). The recombinant protein does not show
CC       hemolytic activity, suggesting that it is not properly folded or that
CC       it requires a free N-terminal end for its activity (Probable).
CC       {ECO:0000250|UniProtKB:A0A0N7HUN6, ECO:0000305|PubMed:26435341}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KT693314; ALI86905.1; -; 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 P1"
FT                   /evidence="ECO:0000305|PubMed:26435341"
FT                   /id="PRO_0000454510"
FT   DISULFID        16..37
FT                   /evidence="ECO:0000305|PubMed:26435341"
FT   DISULFID        22..33
FT                   /evidence="ECO:0000305|PubMed:26435341"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000305|PubMed:26435341"
SQ   SEQUENCE   93 AA;  10075 MW;  7FF1039FF69496AA CRC64;
     GWPAYPGRNG IRSSVCQKKL GCGWRKLASL PVCKAFCLAR KRFWQKCGKN GSSGKGSKIC
     KSVIAHTFEK AGKGLIKLTD MAVATIIKYA GKK