MASTP_PROSY
ID MASTP_PROSY Reviewed; 14 AA.
AC P0C1Q5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Mastoparan;
DE AltName: Full=Protonectarina-MP;
OS Protonectarina sylveirae (Brazilian wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Epiponini; Protonectarina.
OX NCBI_TaxID=91438;
RN [1]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT
RP LEU-14.
RC TISSUE=Venom;
RX PubMed=7513243; DOI=10.1002/nt.2620010503;
RA Dohtsu K., Okumura K., Hagiwara K., Palma M.S., Nakajima T.;
RT "Isolation and sequence analysis of peptides from the venom of
RT Protonectarina sylveirae (Hymenoptera-Vespidae).";
RL Nat. Toxins 1:271-276(1993).
CC -!- FUNCTION: Potent antimicrobial peptide against both Gram-positive and
CC Gram-negative bacteria (By similarity). This hemolytic peptide shows
CC potent histamine releasing activities on rat peritoneal mast cells.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC {ECO:0000305}.
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DR TCDB; 1.C.118.1.2; the mastoparin peptide 1 (mpp1) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Hemolysis; Mast cell degranulation; Secreted.
FT PEPTIDE 1..14
FT /note="Mastoparan"
FT /id="PRO_0000247264"
FT MOD_RES 14
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:7513243"
SQ SEQUENCE 14 AA; 1583 MW; 551E9ED7AA71F7A7 CRC64;
INWKALLDAA KKVL