ID   CHY3_PAGMA              Reviewed;          20 AA.
AC   P83547;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Chrysophsin-3;
OS   Pagrus major (Red sea bream) (Chrysophrys major).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Pagrus.
OX   NCBI_TaxID=143350 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AMIDATION AT HIS-20, MASS SPECTROMETRY,
RP   CIRCULAR DICHROISM ANALYSIS, AND SYNTHESIS.
RC   TISSUE=Gill;
RX   PubMed=12581207; DOI=10.1046/j.1432-1033.2003.03419.x;
RA   Iijima N., Tanimoto N., Emoto Y., Morita Y., Uematsu K., Murakami T.,
RA   Nakai T.;
RT   "Purification and characterization of three isoforms of chrysophsin, a
RT   novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys
RT   major.";
RL   Eur. J. Biochem. 270:675-686(2003).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacteria
CC       B.subtilis ATCC 6633, L.garvieae ATCC 49156 and S.iniae F-8502, and
CC       Gram-negative bacteria E.coli WT-2, V.anguillarum ATCC 19264,
CC       V.penaeicida KHA, V.harveyi ATCC 14126, V.vulnificus ATCC 33148,
CC       A.salmonicida NCMB 1102 and P.putida ATCC 12633. Has hemolytic activity
CC       against human red blood cells. Seems to disrupt the membranes by
CC       adopting an alpha helical conformation. May play a significant role in
CC       innate host defense. {ECO:0000269|PubMed:12581207,
CC       ECO:0000303|PubMed:12581207}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Gill.
CC   -!- MASS SPECTROMETRY: Mass=2285.7; Mass_error=0.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12581207};
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   AlphaFoldDB; P83547; -.
DR   TCDB; 1.C.88.1.3; the chrysophsin (chrysophsin) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Secreted.
FT   PEPTIDE         1..20
FT                   /note="Chrysophsin-3"
FT                   /id="PRO_0000043416"
FT   MOD_RES         20
FT                   /note="Histidine amide"
FT                   /evidence="ECO:0000269|PubMed:12581207"
SQ   SEQUENCE   20 AA;  2287 MW;  D6D0AC1A3C34AFD2 CRC64;
     FIGLLISAGK AIHDLIRRRH