ID   AMP_POCDA               Reviewed;         107 AA.
AC   F1DFM9; A0A3M6U162;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Antimicrobial peptide damicornin {ECO:0000303|PubMed:21536670};
DE   Flags: Precursor;
OS   Pocillopora damicornis (Cauliflower coral) (Millepora damicornis).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Pocillopora.
OX   NCBI_TaxID=46731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 68-106, AMIDATION AT
RP   ARG-106, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RX   PubMed=21536670; DOI=10.1074/jbc.m110.216358;
RA   Vidal-Dupiol J., Ladriere O., Destoumieux-Garzon D., Sautiere P.E.,
RA   Meistertzheim A.L., Tambutte E., Tambutte S., Duval D., Foure L.,
RA   Adjeroud M., Mitta G.;
RT   "Innate immune responses of a scleractinian coral to vibriosis.";
RL   J. Biol. Chem. 286:22688-22698(2011).
RN   [2] {ECO:0000312|EMBL:RMX47400.1, ECO:0000312|Proteomes:UP000275408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSMAS {ECO:0000312|EMBL:RMX47400.1};
RX   PubMed=30382153; DOI=10.1038/s41598-018-34459-8;
RA   Cunning R., Bay R.A., Gillette P., Baker A.C., Traylor-Knowles N.;
RT   "Comparative analysis of the Pocillopora damicornis genome highlights role
RT   of immune system in coral evolution.";
RL   Sci. Rep. 8:16134-16134(2018).
CC   -!- FUNCTION: Cationic peptide with probable antimicrobial activity against
CC       coral pathogens. Shows in vitro activity against Gram-positive bacteria
CC       and the filamentous fungus F.oxysporum (MIC=1.25 uM). Gram-positive
CC       bacteria tested are B.megaterium (MIC=20 uM), S.aureus (MIC=5 uM), M.
CC       luteus (MIC=1.25 uM), B.stationis (MIC=10 uM), M.maritypicum (MIC=20
CC       uM). Has no or little effect against Gram-negative bacteria (the coral
CC       pathogen V.coralliilyticus (MIC>20 uM), V.aesturianus (MIC>20 uM),
CC       V.shiloi (MIC>20 uM), and E.coli (MIC=10 uM)). Has no hemolytic
CC       activity against sheep erythrocytes. {ECO:0000269|PubMed:21536670}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC       {ECO:0000305|PubMed:21536670}. Secreted {ECO:0000305|PubMed:21536670}.
CC   -!- TISSUE SPECIFICITY: Is specifically expressed in the granular cells of
CC       the ectoderm. {ECO:0000269|PubMed:21536670}.
CC   -!- INDUCTION: Transiently up-regulated (6-fold) after challenge with the
CC       coral pathogen V.coralliilyticus and dramatically repressed (50-fold)
CC       thereafter. {ECO:0000269|PubMed:21536670}.
CC   -!- MASS SPECTROMETRY: Mass=4492.74; Method=MALDI; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:21536670};
CC   -!- SIMILARITY: Belongs to the coral AMP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=RMX47400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; HQ825099; ADV51532.1; -; mRNA.
DR   EMBL; RCHS01002422; RMX47400.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; F1DFM9; -.
DR   Proteomes; UP000275408; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytoplasm; Disulfide bond; Fungicide; Immunity; Innate immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..67
FT                   /evidence="ECO:0000305|PubMed:21536670"
FT                   /id="PRO_0000452121"
FT   CHAIN           68..106
FT                   /note="Antimicrobial peptide damicornin"
FT                   /evidence="ECO:0000269|PubMed:21536670"
FT                   /id="PRO_5003264075"
FT   REGION          37..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:21536670"
FT   DISULFID        69..105
FT                   /evidence="ECO:0000269|PubMed:21536670"
FT   DISULFID        78..99
FT                   /evidence="ECO:0000269|PubMed:21536670"
FT   DISULFID        85..103
FT                   /evidence="ECO:0000269|PubMed:21536670"
FT   CONFLICT        15
FT                   /note="M -> I (in Ref. 2; RMX47400)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   107 AA;  11775 MW;  3C9DF23E68A5B46E CRC64;
     MKVLVILFGA MLVLMEFQKA SAATLLEDFD DDDDLLDDGG DFDLEANSDA SSGNGNDSND
     AVPEKRRACA DLRGKTFCRL FKSYCDKKGI RGRLMRDKCS YSCGCRG