ID   DB118_MACMU             Reviewed;         123 AA.
AC   Q95LI0;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Defensin beta 118 {ECO:0000250|UniProtKB:Q96PH6};
DE   AltName: Full=Beta-defensin 118 {ECO:0000305};
DE   AltName: Full=Epididymal secretory protein 13.6;
DE            Short=ESP13.6;
DE   Flags: Precursor;
GN   Name=DEFB118; Synonyms=ESC42;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=11564719; DOI=10.1210/endo.142.10.8422;
RA   Liu Q., Hamil K.G., Sivashanmugam P., Grossman G., Soundararajan R.,
RA   Rao A.J., Richardson R.T., Zhang Y.-L., O'Rand M.G., Petrusz P.,
RA   French F.S., Hall S.H.;
RT   "Primate epididymis-specific proteins: characterization of ESC42, a novel
RT   protein containing a trefoil-like motif in monkey and human.";
RL   Endocrinology 142:4529-4539(2001).
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:0000269|PubMed:11564719}.
CC   -!- TISSUE SPECIFICITY: High-level and epididymis-specific expression. Most
CC       abundant in the epithelium of the caput and is also present in the
CC       lumen and bound to sperm. {ECO:0000269|PubMed:11564719}.
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; AF207834; AAL26779.1; -; mRNA.
DR   RefSeq; NP_001032421.1; NM_001037344.1.
DR   AlphaFoldDB; Q95LI0; -.
DR   SMR; Q95LI0; -.
DR   STRING; 9544.ENSMMUP00000011538; -.
DR   Ensembl; ENSMMUT00000096383; ENSMMUP00000067470; ENSMMUG00000063307.
DR   GeneID; 641438; -.
DR   KEGG; mcc:641438; -.
DR   CTD; 117285; -.
DR   VEuPathDB; HostDB:ENSMMUG00000063307; -.
DR   eggNOG; ENOG502TM86; Eukaryota.
DR   GeneTree; ENSGT00530000064565; -.
DR   HOGENOM; CLU_164142_0_0_1; -.
DR   InParanoid; Q95LI0; -.
DR   OMA; CWNKSGH; -.
DR   OrthoDB; 1618767at2759; -.
DR   TreeFam; TF336381; -.
DR   Proteomes; UP000006718; Chromosome 10.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; TAS: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:0051673; P:membrane disruption in another organism; IEA:Ensembl.
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   GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR   InterPro; IPR025933; Beta_defensin.
DR   Pfam; PF13841; Defensin_beta_2; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         20..62
FT                   /note="Defensin beta 118"
FT                   /id="PRO_0000006985"
FT   PROPEP          65..123
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000006986"
FT   REGION          100..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Polar residues"
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;  13630 MW;  EB0EF33715FF94E1 CRC64;
     MKLLLLALPI LVLLPQVIPA YGGEKKCWNR SGHCRKQCKD GEAVKETCKN HRACCVPSNE
     DHRRLPTTSP TPLSDSTPGI IDNILTIRFT TDYFEISSKK DMVEESEAGQ GTQTSPPNVH
     HTS