CYNT_HALAU
ID CYNT_HALAU Reviewed; 30 AA.
AC P0C007;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Dicynthaurin;
OS Halocynthia aurantium (Sea peach).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=254849;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, CIRCULAR DICHROISM ANALYSIS, AMIDATION AT
RP THR-30, AND MASS SPECTROMETRY.
RC TISSUE=Hemocyte;
RX PubMed=11479030; DOI=10.1016/s0304-4165(01)00156-8;
RA Lee I.H., Lee Y.S., Kim C.H., Kim C.R., Hong T., Menzel L., Boo L.M.,
RA Pohl J., Sherman M.A., Waring A., Lehrer R.I.;
RT "Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary
RT tunicate, Halocynthia aurantium.";
RL Biochim. Biophys. Acta 1527:141-148(2001).
CC -!- FUNCTION: Shows antibacterial activity against both Gram-positive and
CC Gram-negative bacteria. Its antimicrobial activity is optimal at NaCl
CC concentrations below 100 mM, suggesting that the antimicrobial actions
CC of this peptide may take place intracellularly rather than
CC extracellularly. Has no activity against the fungus C.albicans. Has
CC modest hemolytic activity.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=3104.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11479030};
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DR AlphaFoldDB; P0C007; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Secreted.
FT PEPTIDE 1..30
FT /note="Dicynthaurin"
FT /id="PRO_0000044129"
FT MOD_RES 30
FT /note="Threonine amide"
FT /evidence="ECO:0000269|PubMed:11479030"
FT DISULFID 9
FT /note="Interchain"
SQ SEQUENCE 30 AA; 3106 MW; F94A4BD57917FFDF CRC64;
ILQKAVLDCL KAAGSSLSKA AITAIYNKIT