NDB44_MESMA
ID NDB44_MESMA Reviewed; 70 AA.
AC Q6JQN2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Peptide BmKn2;
DE Short=Kn2;
DE AltName: Full=Non-disulfide-bridged peptide 4.4 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.4 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.4 {ECO:0000303|PubMed:16036557};
DE Short=NDBP-5.4 {ECO:0000303|PubMed:16036557};
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, AMIDATION AT PHE-36, AND
RP FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=15062994; DOI=10.1016/j.peptides.2003.12.003;
RA Zeng X.-C., Wang S.-X., Zhu Y., Zhu S.-Y., Li W.-X.;
RT "Identification and functional characterization of novel scorpion venom
RT peptides with no disulfide bridge from Buthus martensii Karsch.";
RL Peptides 25:143-150(2004).
RN [2]
RP SYNTHESIS OF 24-36 (BMKN2 AND KN2-7), FUNCTION OF BMKN2, FUNCTION OF MUTANT
RP KN2-7, AND MUTAGENESIS OF 26-GLY-ALA-27 AND SER-33.
RX PubMed=22536342; DOI=10.1371/journal.pone.0034947;
RA Chen Y., Cao L., Zhong M., Zhang Y., Han C., Li Q., Yang J., Zhou D.,
RA Shi W., He B., Liu F., Yu J., Sun Y., Cao Y., Li Y., Li W., Guo D., Cao Z.,
RA Yan H.;
RT "Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7.";
RL PLoS ONE 7:E34947-E34947(2012).
RN [3]
RP FUNCTION OF BMKN2, AND MUTAGENESIS OF 31-LEU--PHE-36; 32-LEU--PHE-36;
RP 33-SER--PHE-36; 34-LYS--PHE-36; 35-ILE--PHE-36 AND PHE-36.
RX PubMed=24184420; DOI=10.1016/j.peptides.2013.10.020;
RA Arpornsuwan T., Buasakul B., Jaresitthikunchai J., Roytrakul S.;
RT "Potent and rapid antigonococcal activity of the venom peptide BmKn2 and
RT its derivatives against different Maldi biotype of multidrug-resistant
RT Neisseria gonorrhoeae.";
RL Peptides 53:315-320(2014).
RN [4]
RP NOMENCLATURE.
RX PubMed=16036557; DOI=10.1080/15216540500058899;
RA Zeng X.C., Corzo G., Hahin R.;
RT "Scorpion venom peptides without disulfide bridges.";
RL IUBMB Life 57:13-21(2005).
RN [5]
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).
CC -!- FUNCTION: Peptide BmKn2: has strong antibacterial activity against
CC Gram-positive bacteria S.aureus, M.luteus, B.subtilis, and Gram-
CC negative bacteria E.coli, P.aeruginosa and N.gonorrhoeae. Also shows
CC low activity against HIV-1 PV.
CC -!- FUNCTION: Mutant Kn2-7: shows antiviral activities against HIV-1
CC (EC(50)=2.76 ug/ml). This activity is correlated with a direct
CC interaction between the mutant and HIV-1 envelope.
CC -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms an
CC alpha-helical membrane channel in the prey.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
CC -!- CAUTION: Studies from PubMed:24184420 describe a peptide with an Arg-30
CC instead of an Asn-30. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY323830; AAQ89934.1; -; mRNA.
DR AlphaFoldDB; Q6JQN2; -.
DR SMR; Q6JQN2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Antiviral protein;
KW Cleavage on pair of basic residues; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane; Transmembrane.
FT SIGNAL 1..23
FT PEPTIDE 24..36
FT /note="Peptide BmKn2"
FT /id="PRO_0000231500"
FT PROPEP 40..70
FT /id="PRO_0000231501"
FT MOD_RES 36
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:15062994"
FT MUTAGEN 26..27
FT /note="GA->KR: Shows a higher anti-HIV-1 activity; when
FT associated with R-33 (mutant Kn2-7)."
FT /evidence="ECO:0000269|PubMed:22536342"
FT MUTAGEN 31..36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn26)."
FT /evidence="ECO:0000269|PubMed:24184420"
FT MUTAGEN 32..36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn25)."
FT /evidence="ECO:0000269|PubMed:24184420"
FT MUTAGEN 33..36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn24)."
FT /evidence="ECO:0000269|PubMed:24184420"
FT MUTAGEN 33
FT /note="S->R: Shows a higher anti-HIV-1 activity; when
FT associated with 26-K-R-27 (mutant Kn2-7)."
FT /evidence="ECO:0000269|PubMed:22536342"
FT MUTAGEN 34..36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn23)."
FT /evidence="ECO:0000269|PubMed:24184420"
FT MUTAGEN 35..36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn22)."
FT /evidence="ECO:0000269|PubMed:24184420"
FT MUTAGEN 36
FT /note="Missing: Important decrease in inhibition of
FT N.gonorrhoeae (mutant BmKn21)."
FT /evidence="ECO:0000269|PubMed:24184420"
SQ SEQUENCE 70 AA; 7985 MW; 9A516E9BAC8E3860 CRC64;
MKSQTFFLLF LVVLLLAISQ SEAFIGAIAN LLSKIFGKRS MRDMDTMKYL YDPSLSAADL
KTLQKLMENY
