NDB4S_HOFGE
ID NDB4S_HOFGE Reviewed; 71 AA.
AC P0C8W1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Non-disulfide-bridged peptide 5.5 {ECO:0000303|PubMed:17506894};
DE Short=NDBP-5.5 {ECO:0000303|PubMed:17506894};
DE Flags: Precursor;
OS Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Iuroidea; Hadrurus.
OX NCBI_TaxID=380989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND NOMENCLATURE.
RC TISSUE=Venom gland;
RX PubMed=17506894; DOI=10.1186/1471-2164-8-119;
RA Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D.;
RT "Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus
RT gertschi (Arachnida: Scorpiones).";
RL BMC Genomics 8:119-119(2007).
RN [2]
RP FUNCTION, SYNTHESIS OF 24-36, AND PROBABLE AMIDATION AT LEU-36.
RX PubMed=28275372; DOI=10.3389/fmicb.2017.00273;
RA Trentini M.M., das Neves R.C., Santos B.P., DaSilva R.A., de Souza A.C.,
RA Mortari M.R., Schwartz E.F., Kipnis A., Junqueira-Kipnis A.P.;
RT "Non-disulfide-bridge peptide 5.5 from the scorpion Hadrurus gertschi
RT inhibits the growth of Mycobacterium abscessus subsp. massiliense.";
RL Front. Microbiol. 8:273-273(2017).
CC -!- FUNCTION: Antimicrobial peptide (PubMed:28275372). Is active on
CC Mycobacterium abscessus subsp. massiliense (MBC=200 uM), a rapidly
CC growing and emerging pathogen associated with healthcare infections
CC (PubMed:28275372). Also shows antifungal activities (By similarity).
CC Has a weak hemolytic activity on human erythrocytes (10% at 610 uM),
CC indicating a low toxicity (therapeutic index (TI)=3.05)
CC (PubMed:28275372). In addition, treatment of infected macrophages
CC reduces the bacterial load (PubMed:28275372). In vivo, treatment of
CC M.abscessus-infected mice causes a decrease in the bacterial load in
CC the lungs and liver (PubMed:28275372). {ECO:0000250|UniProtKB:E4VP07,
CC ECO:0000269|PubMed:28275372}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28275372}. Target
CC cell membrane {ECO:0000305|PubMed:28275372}. Note=Has an amphipathic
CC alpha-helical conformation. {ECO:0000305|PubMed:28275372}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:28275372}.
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
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DR EMBL; EL698901; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C8W1; -.
DR SMR; P0C8W1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Fungicide; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PEPTIDE 24..36
FT /note="Non-disulfide-bridged peptide 5.5"
FT /evidence="ECO:0000305|PubMed:17506894,
FT ECO:0000305|PubMed:28275372"
FT /id="PRO_0000366097"
FT PROPEP 40..71
FT /evidence="ECO:0000250"
FT /id="PRO_0000366098"
FT MOD_RES 36
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:28275372"
SQ SEQUENCE 71 AA; 8081 MW; 9DD96D3BA3EC747F CRC64;
MKTQFIVLIV AIVFLQLLSQ SEAIFSAIAG LLSNLLGKRD LRHLDLDQFD DMFDQPEISA
ADMKFLQDLL R