ID   SCAB_ORYRH              Reviewed;          66 AA.
AC   Q86SC0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Scarabaecin;
DE   Contains:
DE     RecName: Full=Scarabaecin, minor form;
DE   Contains:
DE     RecName: Full=Scarabaecin, major form;
DE   Flags: Precursor;
GN   Name=scar {ECO:0000312|EMBL:BAC54897.1};
OS   Oryctes rhinoceros (Coconut rhinoceros beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=72550;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC54897.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-55 AND 62-64, FUNCTION,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Fat body {ECO:0000312|EMBL:BAC54897.1};
RX   PubMed=12859949; DOI=10.1016/s0006-291x(03)01162-8;
RA   Tomie T., Ishibashi J., Furukawa S., Kobayashi S., Sawahata R., Asaoka A.,
RA   Tagawa M., Yamakawa M.;
RT   "Scarabaecin, a novel cysteine-containing antifungal peptide from the
RT   rhinoceros beetle, Oryctes rhinoceros.";
RL   Biochem. Biophys. Res. Commun. 307:261-266(2003).
RN   [2] {ECO:0000312|PDB:1IYC}
RP   STRUCTURE BY NMR OF 29-64, AND FUNCTION.
RX   PubMed=12676931; DOI=10.1074/jbc.m301025200;
RA   Hemmi H., Ishibashi J., Tomie T., Yamakawa M.;
RT   "Structural basis for new pattern of conserved amino acid residues related
RT   to chitin-binding in the antifungal peptide from the coconut rhinoceros
RT   beetle Oryctes rhinoceros.";
RL   J. Biol. Chem. 278:22820-22827(2003).
CC   -!- FUNCTION: Possesses antifungal activity against phytopathogenic fungi
CC       such as P.oryzae, R.solani and B.cinerea but not against
CC       phytopathogenic bacteria. Shows weak activity against the insect
CC       pathogenic fungus B.bassiana and against S.aureus. Binds chitin.
CC       {ECO:0000269|PubMed:12676931, ECO:0000269|PubMed:12859949}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12859949}.
CC   -!- MASS SPECTROMETRY: [Scarabaecin, minor form]: Mass=4080; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12859949};
CC   -!- MASS SPECTROMETRY: [Scarabaecin, major form]: Mass=4266; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12859949};
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DR   EMBL; AB081620; BAC54897.1; -; mRNA.
DR   PDB; 1IYC; NMR; -; A=29-64.
DR   PDBsum; 1IYC; -.
DR   AlphaFoldDB; Q86SC0; -.
DR   SMR; Q86SC0; -.
DR   EvolutionaryTrace; Q86SC0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   SUPFAM; SSF57625; SSF57625; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:12859949"
FT   PEPTIDE         27..64
FT                   /note="Scarabaecin, minor form"
FT                   /evidence="ECO:0000269|PubMed:12859949"
FT                   /id="PRO_0000259619"
FT   PEPTIDE         29..64
FT                   /note="Scarabaecin, major form"
FT                   /evidence="ECO:0000269|PubMed:12859949"
FT                   /id="PRO_0000259620"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000269|PubMed:12676931"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1IYC"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1IYC"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1IYC"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1IYC"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1IYC"
SQ   SEQUENCE   66 AA;  7454 MW;  EE900BCCD79CFE29 CRC64;
     MKTLTFYTLL LCAALYSNFF DCKAVADAEL PKLPDDKVLI RSRSNCPKGK VWNGFDCKSP
     FAFSKK