ID   NDB4S_OPICY             Reviewed;          68 AA.
AC   C5J886;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Amphipathic peptide OcyC1 {ECO:0000303|PubMed:19379768};
DE   AltName: Full=Non-disulfide-bridged peptide 5.7 {ECO:0000303|PubMed:19379768};
DE            Short=NDBP-5.7 {ECO:0000303|PubMed:19379768};
DE   Contains:
DE     RecName: Full=OcyC1f {ECO:0000250|UniProtKB:Q8MMJ7};
DE   Flags: Precursor;
OS   Opisthacanthus cayaporum (South American scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX   NCBI_TaxID=573324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=19379768; DOI=10.1016/j.toxicon.2009.04.010;
RA   Silva E.C., Camargos T.S., Maranhao A.Q., Silva-Pereira I., Silva L.P.,
RA   Possani L.D., Schwartz E.F.;
RT   "Cloning and characterization of cDNA sequences encoding for new venom
RT   peptides of the Brazilian scorpion Opisthacanthus cayaporum.";
RL   Toxicon 54:252-261(2009).
RN   [2]
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=18502464; DOI=10.1016/j.toxicon.2008.03.029;
RA   Schwartz E.F., Camargos T.S., Zamudio F.Z., Silva L.P., Bloch C. Jr.,
RA   Caixeta F., Schwartz C.A., Possani L.D.;
RT   "Mass spectrometry analysis, amino acid sequence and biological activity of
RT   venom components from the Brazilian scorpion Opisthacanthus cayaporum.";
RL   Toxicon 51:1499-1508(2008).
RN   [3]
RP   FUNCTION, AND SYNTHESIS OF 24-36.
RX   PubMed=27917162; DOI=10.3389/fmicb.2016.01844;
RA   Guilhelmelli F., Vilela N., Smidt K.S., de Oliveira M.A.,
RA   da Cunha Morales Alvares A., Rigonatto M.C., da Silva Costa P.H.,
RA   Tavares A.H., de Freitas S.M., Nicola A.M., Franco O.L., Derengowski L.D.,
RA   Schwartz E.F., Mortari M.R., Bocca A.L., Albuquerque P., Silva-Pereira I.;
RT   "Activity of scorpion venom-derived antifungal peptides against planktonic
RT   cells of Candida spp. and Cryptococcus neoformans and Candida albicans
RT   biofilms.";
RL   Front. Microbiol. 7:1844-1844(2016).
CC   -!- FUNCTION: [Amphipathic peptide OcyC1]: Antimicrobial peptide (By
CC       similarity) (PubMed:27917162). Inhibits the growth of Gram-positive and
CC       Gram-negative bacteria (By similarity). Shows antifungal activity with
CC       MIC values ranging from 12.5 to 25 uM (PubMed:27917162). Shows also an
CC       inhibitory activity on C.albicans biofilms at high concentrations
CC       (PubMed:27917162). Shows low cytotoxic activity and has weak hemolytic
CC       activity (PubMed:27917162). {ECO:0000250|UniProtKB:L0GCI6,
CC       ECO:0000269|PubMed:27917162}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18502464}. Target
CC       cell membrane {ECO:0000250}. Note=Forms an alpha-helical membrane
CC       channel in the prey. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: [Amphipathic peptide OcyC1]: Mass=1432.8;
CC       Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:18502464};
CC   -!- MASS SPECTROMETRY: [OcyC1f]: Mass=1174.6; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:18502464};
CC   -!- MISCELLANEOUS: Does not show antifungal activity against Candida
CC       glabrata (ATCC90030) and Candida parapsilosis (ATCC22019) (MIC>400 uM).
CC       {ECO:0000269|PubMed:27917162}.
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; FM998743; CAX51390.1; -; mRNA.
DR   AlphaFoldDB; C5J886; -.
DR   SMR; C5J886; -.
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; Fungicide; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250|UniProtKB:Q8MMJ7"
FT   PEPTIDE         24..36
FT                   /note="Amphipathic peptide OcyC1"
FT                   /id="PRO_5000471230"
FT   PEPTIDE         24..34
FT                   /note="OcyC1f"
FT                   /evidence="ECO:0000250|UniProtKB:Q8MMJ7"
FT                   /id="PRO_5000471229"
FT   PROPEP          38..68
FT                   /id="PRO_0000398604"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q8MMJ7"
SQ   SEQUENCE   68 AA;  7635 MW;  791912A2C43992D8 CRC64;
     MKAQLCILLI ALVLFQTFSQ SDAILSAIWS GIKSLFGRRG LNDLDDLDEL FDGEISQADV
     DFLNELMR