ID   CHY1_PAGMA              Reviewed;          25 AA.
AC   P83545;
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-1;
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, TISSUE SPECIFICITY, AMIDATION AT HIS-25, MASS
RP   SPECTROMETRY, 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. Localized in certain epithelial cells lining
CC       the surface of secondary lamellae and eosinophilic granule cell-like
CC       cells at the base of secondary lamellae. {ECO:0000269|PubMed:12581207}.
CC   -!- MASS SPECTROMETRY: Mass=2891.2; 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; P83545; -.
DR   TCDB; 1.C.88.1.1; 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-1"
FT                   /id="PRO_0000043414"
FT   MOD_RES         25
FT                   /note="Histidine amide"
FT                   /evidence="ECO:0000269|PubMed:12581207"
SQ   SEQUENCE   25 AA;  2892 MW;  5B00990A42DF51E4 CRC64;
     FFGWLIKGAI HAGKAIHGLI HRRRH