ID   DB118_PONPY             Reviewed;         123 AA.
AC   A4H221;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Defensin beta 118 {ECO:0000250|UniProtKB:Q96PH6};
DE   AltName: Full=Beta-defensin 118 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=DEFB118;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hollox E.J., Armour J.A.L.;
RT   "Evolution and sequence variation of human beta-defensin genes.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Host defense peptide that exhibits antimicrobial activity
CC       against both Gram-negative bacteria, such as E.coli and S.typhimurium,
CC       and Gram-positive bacteria, such as S.aureus and B.subtilis (By
CC       similarity). Inhibits cell adhesion of E.coli on intestinal epithelial
CC       enterocytes (By similarity). Causes rapid permeabilization of both the
CC       outer and inner membrane of E.coli, leading to morphological
CC       alterations on the bacterial surface (By similarity). Binds to
CC       bacterial lipopolysaccharides (LPS) with high affinity, and may thereby
CC       be involved in immunoregulation through LPS neutralization (By
CC       similarity). May contribute to epididymal innate immunity and protect
CC       the sperm against attack by microorganisms (By similarity).
CC       {ECO:0000250|UniProtKB:Q96PH6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96PH6}.
CC   -!- PTM: The three-dimensional structure formed by the three intramolecular
CC       disulfide bridges is indispensable for antimicrobial activity.
CC       {ECO:0000250|UniProtKB:Q96PH6}.
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; AM410126; CAL68941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4H221; -.
DR   SMR; A4H221; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; ISS:UniProtKB.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR025933; Beta_defensin.
DR   Pfam; PF13841; Defensin_beta_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         20..62
FT                   /note="Defensin beta 118"
FT                   /id="PRO_0000289828"
FT   PROPEP          65..123
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000289829"
FT   REGION          100..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        27..54
FT                   /evidence="ECO:0000250|UniProtKB:Q91V82"
FT   DISULFID        34..48
FT                   /evidence="ECO:0000250|UniProtKB:Q91V82"
FT   DISULFID        38..55
FT                   /evidence="ECO:0000250|UniProtKB:Q91V82"
SQ   SEQUENCE   123 AA;  13673 MW;  6F1FECEA11767AD1 CRC64;
     MKLLLLALPM LVLLPQVIPA YSGEKKCWNR SGHCRKQCKD GEAVKDTCKN LRACCVPSNE
     DHRRVPTTSP TPLSDSTRGV IDDILTVRFT TDYFEVSSKK NMVEESEVGQ GTQTSLPNVH
     HSS