ID   CHY2_PAGMA              Reviewed;          25 AA.
AC   P83546;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Chrysophsin-2;
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-25, 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 and
CC       A.salmonicida NCMB 1102. Has hemolytic activity against human red blood
CC       cells. Seems to disrupt the membranes by adopting an alpha helical
CC       conformation. May play a significant role in innate host defense.
CC       {ECO:0000269|PubMed:12581207, ECO:0000303|PubMed:12581207}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Gill.
CC   -!- MASS SPECTROMETRY: Mass=2919.3; Mass_error=0.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12581207};
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   AlphaFoldDB; P83546; -.
DR   TCDB; 1.C.88.1.2; 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.
DR   InterPro; IPR012515; Antimicrobial12.
DR   Pfam; PF08107; Antimicrobial12; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Chrysophsin-2"
FT                   /id="PRO_0000043415"
FT   MOD_RES         25
FT                   /note="Histidine amide"
FT                   /evidence="ECO:0000269|PubMed:12581207"
SQ   SEQUENCE   25 AA;  2920 MW;  5B008BBDB2DF51E4 CRC64;
     FFGWLIRGAI HAGKAIHGLI HRRRH