NDB47_ISOMC
ID NDB47_ISOMC Reviewed; 74 AA.
AC C7B247;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Imcroporin {ECO:0000303|PubMed:28941793};
DE AltName: Full=Non-disulfide-bridged peptide 4.7 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.7 {ECO:0000303|PubMed:24184590};
DE Flags: Precursor;
OS Isometrus maculatus (Lesser brown scorpion) (Scorpio maculatus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Isometrus.
OX NCBI_TaxID=497827;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=19451300; DOI=10.1128/aac.01436-08;
RA Zhao Z., Ma Y., Dai C., Zhao R., Li S., Wu Y., Cao Z., Li W.;
RT "Imcroporin, a new cationic antimicrobial peptide from the venom of the
RT scorpion Isometrus maculates.";
RL Antimicrob. Agents Chemother. 53:3472-3477(2009).
RN [2]
RP NOMENCLATURE.
RX PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA Almaaytah A., Albalas Q.;
RT "Scorpion venom peptides with no disulfide bridges: a review.";
RL Peptides 51:35-45(2014).
RN [3]
RP PROTEIN SEQUENCE OF 23-39, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT LYS-39.
RC TISSUE=Venom {ECO:0000303|PubMed:28941793};
RX PubMed=28941793; DOI=10.1016/j.toxicon.2017.09.010;
RA Miyashita M., Kitanaka A., Yakio M., Yamazaki Y., Nakagawa Y., Miyagawa H.;
RT "Complete de novo sequencing of antimicrobial peptides in the venom of the
RT scorpion Isometrus maculatus.";
RL Toxicon 139:1-12(2017).
CC -!- FUNCTION: Has potent antibacterial activity against Gram-positive
CC bacteria M.luteus, B.thuringiensis, S.aureus and B.subtilis, but not
CC Gram-negative bacteria. Shows a weak cytotoxicity effect against
CC mammalian cell lines and relatively low hemolytic activity against
CC human erythrocytes. {ECO:0000269|PubMed:19451300}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28941793}. Target
CC cell membrane {ECO:0000305|PubMed:28941793}. Note=Probably forms a
CC helical membrane channel in the prey. {ECO:0000305|PubMed:28941793}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19451300}.
CC -!- MASS SPECTROMETRY: Mass=1760.0; Method=MALDI; Note=Amidated.;
CC Evidence={ECO:0000269|PubMed:28941793};
CC -!- MASS SPECTROMETRY: Mass=1761.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28941793};
CC -!- MISCELLANEOUS: A fragment comprising residues 4-17 has been detected in
CC venom but it is unclear whether it has a physiological role or is
CC simply due to degradation. {ECO:0000305|PubMed:28941793}.
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; FJ750949; ACT78488.1; -; mRNA.
DR AlphaFoldDB; C7B247; -.
DR SMR; C7B247; -.
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.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:28941793"
FT PEPTIDE 23..39
FT /note="Imcroporin"
FT /evidence="ECO:0000269|PubMed:28941793"
FT /id="PRO_0000393447"
FT PROPEP 45..74
FT /evidence="ECO:0000305|PubMed:28941793"
FT /id="PRO_0000393448"
FT MOD_RES 39
FT /note="Lysine amide; partial"
FT /evidence="ECO:0000269|PubMed:28941793"
SQ SEQUENCE 74 AA; 8777 MW; CFF4AE6A2C2F1529 CRC64;
MKFQYLLAVF LIVLVVTDHC QAFFSLLPSL IGGLVSAIKG RRRRQLEARF EPKQRNFRKR
ELDFEKLFAN MPDY