XAC2_XYLAI
ID XAC2_XYLAI Reviewed; 17 AA.
AC C0HKQ6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 25-MAY-2022, entry version 7.
DE RecName: Full=Antimicrobial peptide Xac-2 {ECO:0000303|PubMed:28546807};
DE AltName: Full=Xylopinin {ECO:0000303|PubMed:28855917};
OS Xylocopa appendiculata circumvolans (Japanese carpenter bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Xylocopa; Alloxylocopa.
OX NCBI_TaxID=135722 {ECO:0000303|PubMed:28546807};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT PRO-17.
RC TISSUE=Venom {ECO:0000303|PubMed:28546807};
RX PubMed=28546807; DOI=10.1186/s40409-017-0119-6;
RA Kawakami H., Goto S.G., Murata K., Matsuda H., Shigeri Y., Imura T.,
RA Inagaki H., Shinada T.;
RT "Isolation of biologically active peptides from the venom of Japanese
RT carpenter bee, Xylocopa appendiculata.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 23:29-29(2017).
RN [2]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND AMIDATION AT
RP PRO-17.
RC TISSUE=Venom {ECO:0000303|PubMed:28855917};
RX PubMed=28855917; DOI=10.1186/s40409-017-0130-y;
RA Kazuma K., Ando K., Nihei K.I., Wang X., Rangel M., Franzolin M.R.,
RA Mori-Yasumoto K., Sekita S., Kadowaki M., Satake M., Konno K.;
RT "Peptidomic analysis of the venom of the solitary bee Xylocopa
RT appendiculata circumvolans.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 23:40-40(2017).
CC -!- FUNCTION: Antimicrobial and mast cell degranulating peptide which
CC probably acts by forming pores in membranes. Active against Gram-
CC negative bacterium E.coli NBRC 14237 (MIC=3.12 uM), against Gram-
CC positive bacteria S.aureus NBRC 12732 (MIC=3.12 uM) and M.luteus NBRC
CC 12708 (MIC=6.25 uM) as well as against yeast S.cerevisiae NBRC 10217
CC (MIC=25 uM). Has hemolytic activity (at 100 uM).
CC {ECO:0000269|PubMed:28546807}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28546807,
CC ECO:0000269|PubMed:28855917}. Target cell membrane
CC {ECO:0000305|PubMed:28546807}. Note=Assumes an amphipathic alpha-
CC helical conformation in a lipid environment.
CC {ECO:0000269|PubMed:28546807}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:28546807}.
CC -!- MASS SPECTROMETRY: Mass=1900.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28546807};
CC -!- MASS SPECTROMETRY: Mass=1899.267; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28855917};
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DR AlphaFoldDB; C0HKQ6; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Fungicide; Hemolysis; Membrane; Secreted; Target cell membrane;
KW Target membrane.
FT PEPTIDE 1..17
FT /note="Antimicrobial peptide Xac-2"
FT /evidence="ECO:0000269|PubMed:28546807,
FT ECO:0000269|PubMed:28855917"
FT /id="PRO_0000441218"
FT MOD_RES 17
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:28546807,
FT ECO:0000269|PubMed:28855917"
SQ SEQUENCE 17 AA; 1900 MW; FDBF8E1A150C10EF CRC64;
GFVALLKKLP LILKHLP
