PAP1_HELVI
ID PAP1_HELVI Reviewed; 23 AA.
AC P30251;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Paralytic peptide 1;
DE AltName: Full=Paralytic peptide I;
DE Short=PP I;
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Hemolymph;
RX PubMed=2071576; DOI=10.1016/s0021-9258(18)98775-2;
RA Skinner W.S., Dennis P.A., Li J.P., Summerfelt R.M., Carney R.L.,
RA Quistad G.B.;
RT "Isolation and identification of paralytic peptides from hemolymph of the
RT lepidopteran insects Manduca sexta, Spodoptera exigua, and Heliothis
RT virescens.";
RL J. Biol. Chem. 266:12873-12877(1991).
CC -!- FUNCTION: Causes rapid, rigid paralysis when injected into Lepidopteran
CC larvae. The physiological role may be to reduce hemolymph loss
CC following injury and promote wound healing.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- SIMILARITY: Belongs to the GBP/PSP1/paralytic peptide family.
CC {ECO:0000305}.
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DR PIR; F39855; F39855.
DR AlphaFoldDB; P30251; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR InterPro; IPR003463; GBP_PSP.
DR Pfam; PF02425; GBP_PSP; 1.
PE 1: Evidence at protein level;
KW Cytokine; Direct protein sequencing; Disulfide bond.
FT PEPTIDE 1..23
FT /note="Paralytic peptide 1"
FT /id="PRO_0000043909"
FT DISULFID 7..19
FT /evidence="ECO:0000250"
SQ SEQUENCE 23 AA; 2524 MW; 2236CB436D655AFA CRC64;
ENFSGGCIPG YMRTADGRCK PTY