ID   DEFL1_CENLI             Reviewed;          56 AA.
AC   Q6GU94; P83738;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Defensin-1;
DE   AltName: Full=Cll-dlp;
DE   Flags: Precursor;
OS   Centruroides limpidus (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 25-56, FUNCTION, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Hemolymph;
RX   PubMed=15197474; DOI=10.1007/s00018-004-4096-x;
RA   Rodriguez De La Vega R.C., Garcia B.I., D'Ambrosio C., Diego-Garcia E.,
RA   Scaloni A., Possani L.D.;
RT   "Antimicrobial peptide induction in the haemolymph of the Mexican scorpion
RT   Centruroides limpidus limpidus in response to septic injury.";
RL   Cell. Mol. Life Sci. 61:1507-1519(2004).
CC   -!- FUNCTION: Antibacterial protein involved in the immune response to
CC       septic injury. When combined with 14.026 kDa and 14.059 kDa hemolymph
CC       antimicrobial peptides, it has a strong cooperative activity against
CC       the Gram-positive bacteria B.subtilis and S.aureus, and against the
CC       Gram-negative bacteria E.coli DH5-alpha and K.pneumoniae ATCC 138833.
CC       Does not show detectable antibacterial activity when present alone. Has
CC       no hemolytic activity in human erythrocytes.
CC       {ECO:0000269|PubMed:15197474}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15197474}.
CC   -!- INDUCTION: By septic injury. {ECO:0000269|PubMed:15197474}.
CC   -!- MASS SPECTROMETRY: Mass=3816.9; Mass_error=1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15197474};
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; AY656081; AAT57643.1; -; Genomic_DNA.
DR   EMBL; AY520534; AAS90630.1; -; mRNA.
DR   PDB; 6B9W; NMR; -; A=25-56.
DR   PDB; 6BAM; NMR; -; A=25-56.
DR   PDB; 6BB6; NMR; -; A=25-56.
DR   PDB; 6BI5; NMR; -; A=25-56.
DR   PDBsum; 6B9W; -.
DR   PDBsum; 6BAM; -.
DR   PDBsum; 6BB6; -.
DR   PDBsum; 6BI5; -.
DR   AlphaFoldDB; Q6GU94; -.
DR   SMR; Q6GU94; -.
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   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Defensin;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:15197474"
FT   CHAIN           25..56
FT                   /note="Defensin-1"
FT                   /evidence="ECO:0000269|PubMed:15197474"
FT                   /id="PRO_0000006764"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:15197474"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:15197474"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:15197474"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:6B9W"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:6B9W"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:6BAM"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:6BAM"
SQ   SEQUENCE   56 AA;  6396 MW;  4669FC4DF80D6CBF CRC64;
     MKAIVVLLIL ALILCLYAMT TVEGACQFWS CNSSCISRGY RQGYCWGIQY KYCQCQ