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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
 
 
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