MAST_CHACK
ID MAST_CHACK Reviewed; 18 AA.
AC P0DTK0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Communis-AAAA {ECO:0000303|PubMed:28754346};
DE Contains:
DE RecName: Full=Communis {ECO:0000303|PubMed:28754346};
OS Chartergellus communis (Wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Chartergellus.
OX NCBI_TaxID=743411;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AMIDATION AT ILE-18, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=28754346; DOI=10.1016/j.peptides.2017.07.012;
RA Lopes K.S., Campos G.A.A., Camargo L.C., de Souza A.C.B., Ibituruna B.V.,
RA Magalhaes A.C.M., da Rocha L.F., Garcia A.B., Rodrigues M.C., Ribeiro D.M.,
RA Costa M.C., Lopez M.H.M., Nolli L.M., Zamudio-Zuniga F., Possani L.D.,
RA Schwartz E.F., Mortari M.R.;
RT "Characterization of two peptides isolated from the venom of social wasp
RT Chartergellus communis (Hymenoptera: Vespidae): influence of multiple
RT alanine residues and C-terminal amidation on biological effects.";
RL Peptides 95:84-93(2017).
CC -!- FUNCTION: [Communis-AAAA]: Probable antimicrobial peptide (Probable).
CC Shows a potent hemolytic activity (EC(50)=142.6 uM). In addition, its
CC highest dose (2 nmol/animal) induces hyperalgesia in mice. In contrast
CC to Communis peptide, does not induce edema (PubMed:28754346).
CC {ECO:0000269|PubMed:28754346, ECO:0000305}.
CC -!- FUNCTION: [Communis]: Is able to induce edema but does not present
CC hemolytic or hyperalgesic activity. {ECO:0000269|PubMed:28754346}.
CC -!- SUBCELLULAR LOCATION: [Communis-AAAA]: Secreted
CC {ECO:0000269|PubMed:28754346}. Target cell membrane {ECO:0000305}.
CC Note=Forms an alpha-helice. {ECO:0000305|PubMed:28754346}.
CC -!- SUBCELLULAR LOCATION: [Communis]: Secreted
CC {ECO:0000269|PubMed:28754346}. Target cell membrane {ECO:0000305}.
CC Note=Forms an alpha-helice, which probably inserts into the membrane.
CC {ECO:0000305|PubMed:28754346}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:28754346}.
CC -!- MASS SPECTROMETRY: [Communis-AAAA]: Mass=1836.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28754346};
CC -!- MASS SPECTROMETRY: [Communis]: Mass=1340.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28754346};
CC -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW Membrane; Secreted; Target cell membrane; Target membrane.
FT PEPTIDE 1..18
FT /note="Communis-AAAA"
FT /evidence="ECO:0000269|PubMed:28754346"
FT /id="PRO_0000454973"
FT PEPTIDE 1..12
FT /note="Communis"
FT /evidence="ECO:0000269|PubMed:28754346"
FT /id="PRO_0000454974"
FT MOD_RES 18
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:28754346"
FT UNSURE 18
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:28754346"
SQ SEQUENCE 18 AA; 1837 MW; E6C241E8FBA08EDC CRC64;
INWKAILGKI GKAAAAVI
