ID   NDB4A_CHATC             Reviewed;          75 AA.
AC   G1FE62;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Antimicrobial peptide ctriporin {ECO:0000303|PubMed:21876042};
DE            Short=Riporin;
DE   AltName: Full=Non-disulfide-bridged peptide 4.10 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-4.10 {ECO:0000303|PubMed:24184590};
DE   Flags: Precursor;
OS   Chaerilus tricostatus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Chaerilida; Chaeriloidea; Chaerilidae; Chaerilus.
OX   NCBI_TaxID=1055734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 23-41, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=21876042; DOI=10.1128/aac.00369-11;
RA   Fan Z., Cao L., He Y., Hu J., Di Z., Wu Y., Li W., Cao Z.;
RT   "Ctriporin, a new anti-methicillin-resistant Staphylococcus aureus peptide
RT   from the venom of the scorpion Chaerilus tricostatus.";
RL   Antimicrob. Agents Chemother. 55:5220-5229(2011).
RN   [2]
RP   SYNTHESIS OF 23-41.
RX   PubMed=22791717; DOI=10.1074/jbc.m112.370312;
RA   Zhao Z., Hong W., Zeng Z., Wu Y., Hu K., Tian X., Li W., Cao Z.;
RT   "Mucroporin-M1 inhibits hepatitis B virus replication by activating the
RT   mitogen-activated protein kinase (MAPK) pathway and down-regulating
RT   HNF4alpha in vitro and in vivo.";
RL   J. Biol. Chem. 287:30181-30190(2012).
RN   [3]
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: Antimicrobial peptide that acts by breaking the cell wall. Is
CC       active against Gram-positive bacteria, fungi and antibiotic-resistant
CC       pathogens: S.aureus (MIC=5 ug/ml), M.luteus (MIC=5 ug/ml),
CC       B.thuringiensis (MIC=10 ug/ml), B.subtilis (MIC=10 ug/ml), C.albicans
CC       (MIC=20 ug/ml), methicillin-resistant S.aureus (MIC=5-10 ug/ml), and
CC       penicillin-resistant S.epidermidis (MIC=10 ug/ml). Is efficient in
CC       curing staphylococcal skin infection in mice, when externally applied.
CC       {ECO:0000269|PubMed:21876042}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Has no activity against Gram-negative bacteria (E.coli
CC       and P.aeruginosa) (PubMed:21876042). Inhibits hepatitis B virus
CC       replication in the HepG2.2.15 cell line by about 30% (PubMed:22791717).
CC       {ECO:0000305|PubMed:21876042, ECO:0000305|PubMed:22791717}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Short antimicrobial peptide (group 4) family.
CC       {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; JN172934; AEK32596.1; -; mRNA.
DR   AlphaFoldDB; G1FE62; -.
DR   BMRB; G1FE62; -.
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:0019835; P:cytolysis; 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   2: Evidence at transcript level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Fungicide; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane; Transmembrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..41
FT                   /note="Antimicrobial peptide ctriporin"
FT                   /id="PRO_0000418800"
FT   PROPEP          47..75
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418801"
FT   MOD_RES         41
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   75 AA;  8821 MW;  16C2BB6F74AFD213 CRC64;
     MDSKYLFVFL IFNVIVIDLC QGFLWGLIPG AISAVTSLIK KGRRRRELGS QYDYLQDFRK
     RELDLDDLLS KFPDY