ID   DEFI_MYTGA              Reviewed;          60 AA.
AC   P80571; Q9Y0B0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Defensin MGD-1 {ECO:0000303|PubMed:10564642};
DE   AltName: Full=Defensin-like peptide {ECO:0000305};
DE            Short=DLP {ECO:0000305};
DE   AltName: Full=Mytilus galloprovincialis defensin 1 {ECO:0000303|PubMed:8925841};
DE            Short=MGD1 {ECO:0000303|PubMed:8925841};
DE   Flags: Precursor; Fragment;
GN   Name=FH3;
OS   Mytilus galloprovincialis (Mediterranean mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=29158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-60, PROTEIN SEQUENCE OF 1-9, TISSUE
RP   SPECIFICITY, INDUCTION BY BACTERIA, AND MASS SPECTROMETRY.
RC   TISSUE=Hemocyte;
RX   PubMed=10564642; DOI=10.1242/jcs.112.23.4233;
RA   Mitta G., Vandenbulcke F., Hubert F., Roch P.;
RT   "Mussel defensins are synthesised and processed in granulocytes then
RT   released into the plasma after bacterial challenge.";
RL   J. Cell Sci. 112:4233-4242(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-38, FUNCTION, HYDROXYLATION AT TRP-28, AND AMIDATION
RP   AT CYS-38.
RC   TISSUE=Hemolymph;
RX   PubMed=8925841; DOI=10.1111/j.1432-1033.1996.0302h.x;
RA   Hubert F., Noeel T., Roch P.;
RT   "A member of the arthropod defensin family from edible Mediterranean
RT   mussels (Mytilus galloprovincialis).";
RL   Eur. J. Biochem. 240:302-306(1996).
RN   [3]
RP   ERRATUM OF PUBMED:8925841.
RA   Hubert F., Noeel T., Roch P.;
RL   Eur. J. Biochem. 240:815-815(1996).
RN   [4]
RP   STRUCTURE BY NMR OF 1-38.
RX   PubMed=11087396; DOI=10.1021/bi0011835;
RA   Yang Y.S., Mitta G., Chavanieu A., Calas B., Sanchez J.F., Roch P.,
RA   Aumelas A.;
RT   "Solution structure and activity of the synthetic four-disulfide bond
RT   Mediterranean mussel defensin (MGD-1).";
RL   Biochemistry 39:14436-14447(2000).
CC   -!- FUNCTION: Active against both Gram-positive and Gram-negative bacteria
CC       but is not cytotoxic towards human erythrocytes or protozoa
CC       (PubMed:8925841). {ECO:0000269|PubMed:8925841}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in hemocytes.
CC       {ECO:0000269|PubMed:10564642}.
CC   -!- INDUCTION: Its expression is increased by bacterial challenge.
CC       {ECO:0000269|PubMed:10564642}.
CC   -!- PTM: The hydroxylation of the Trp-28 is not important for the
CC       antibacterial activity. {ECO:0000269|PubMed:11087396}.
CC   -!- MASS SPECTROMETRY: Mass=4414.90; Mass_error=2.63; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10564642};
CC   -!- MISCELLANEOUS: The Cys-4-Pro-5 bond is in cis conformation.
CC       {ECO:0000269|PubMed:11087396}.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00438";
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DR   EMBL; AF162337; AAD45117.1; -; mRNA.
DR   PIR; S74088; S74088.
DR   PDB; 1FJN; NMR; -; A=1-38.
DR   PDBsum; 1FJN; -.
DR   AlphaFoldDB; P80571; -.
DR   SMR; P80571; -.
DR   EvolutionaryTrace; P80571; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial; Defensin;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation; Immunity;
KW   Innate immunity; Secreted.
FT   PEPTIDE         1..38
FT                   /note="Defensin MGD-1"
FT                   /evidence="ECO:0000269|PubMed:8925841"
FT                   /id="PRO_0000006762"
FT   PROPEP          39..60
FT                   /id="PRO_0000006763"
FT   MOD_RES         28
FT                   /note="3-hydroxytryptophan"
FT                   /evidence="ECO:0000269|PubMed:8925841"
FT   MOD_RES         38
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:8925841"
FT   DISULFID        4..25
FT                   /evidence="ECO:0000269|PubMed:11087396,
FT                   ECO:0007744|PDB:1FJN"
FT   DISULFID        10..33
FT                   /evidence="ECO:0000269|PubMed:11087396,
FT                   ECO:0007744|PDB:1FJN"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000269|PubMed:11087396,
FT                   ECO:0007744|PDB:1FJN"
FT   DISULFID        21..38
FT                   /evidence="ECO:0000269|PubMed:11087396,
FT                   ECO:0007744|PDB:1FJN"
FT   NON_TER         1
FT   HELIX           7..16
FT                   /evidence="ECO:0007829|PDB:1FJN"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1FJN"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:1FJN"
SQ   SEQUENCE   60 AA;  6920 MW;  7BC1B9633C969261 CRC64;
     GFGCPNNYQC HRHCKSIPGR CGGYCGGWHR LRCTCYRCGG RREDVEDIFD IFDNEAADRF