NDB4T_OPICY
ID NDB4T_OPICY Reviewed; 69 AA.
AC C5J887;
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 OcyC2 {ECO:0000303|PubMed:19379768};
DE AltName: Full=Non-disulfide-bridged peptide 5.8 {ECO:0000303|PubMed:19379768};
DE Short=NDBP-5.8 {ECO:0000303|PubMed:19379768};
DE Contains:
DE RecName: Full=OcyC2f {ECO:0000303|PubMed:19379768};
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], PROTEIN SEQUENCE OF 24-35, MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND NOMENCLATURE.
RC TISSUE=Venom, and 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 FUNCTION, AND SYNTHESIS OF 27-37.
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 with antimicrobial activity
CC (PubMed:27917162). Shows antifungal activity with MIC values ranging
CC from 25 to 200 uM (PubMed:27917162). {ECO:0000269|PubMed:27917162}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19379768}. 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.
CC {ECO:0000305|PubMed:19379768}.
CC -!- MASS SPECTROMETRY: [Amphipathic peptide OcyC2]: Mass=1511.91;
CC Method=Unknown; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:19379768};
CC -!- MASS SPECTROMETRY: [OcyC2f]: Mass=1286.84; Method=Unknown;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:19379768};
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; FM998744; CAX51391.1; -; mRNA.
DR AlphaFoldDB; C5J887; -.
DR SMR; C5J887; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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; Antimicrobial; Direct protein sequencing; Fungicide; Membrane;
KW Secreted; Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:19379768"
FT PEPTIDE 24..37
FT /note="Amphipathic peptide OcyC2"
FT /id="PRO_5000471232"
FT PEPTIDE 24..35
FT /note="OcyC2f"
FT /evidence="ECO:0000269|PubMed:19379768"
FT /id="PRO_5000471231"
FT PROPEP 41..69
FT /id="PRO_0000398605"
FT MOD_RES 37
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 69 AA; 7771 MW; E9DE9D182191E2F5 CRC64;
MKTQFAILMI AVVLMQMLVQ TEGGILGKIW EGVKSLIGKR GLKKLDQLDD TFDSDLSDAD
VKLLREMFK