ID   DFB4A_MACMU             Reviewed;          64 AA.
AC   Q9BDS9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Defensin beta 4A {ECO:0000250|UniProtKB:O15263};
DE   AltName: Full=Beta-defensin 2;
DE            Short=BD-2;
DE   AltName: Full=Defensin, beta 2;
DE   AltName: Full=RhBD-2;
DE   Flags: Precursor;
GN   Name=DEFB4A; Synonyms=DEFB2, DEFB4;
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].
RX   PubMed=11238224; DOI=10.1128/cdli.8.2.370-375.2001;
RA   Bals R., Lang C., Weiner D.J., Vogelmeier C., Welsch U., Wilson J.M.;
RT   "Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close
RT   homologues of human molecules.";
RL   Clin. Diagn. Lab. Immunol. 8:370-375(2001).
CC   -!- FUNCTION: Exhibits antimicrobial activity against Gram-negative
CC       bacteria and Gram-positive bacteria, with highest activity against
CC       Gram-negative bacteria (By similarity). Antimicrobial activity against
CC       P.aruginosa seems to be salt-sensitive and is reduced with high salt
CC       concentrations greater than 25 mM (By similarity). Also exhibits
CC       antimicrobial activity against the yeast C.albicans (By similarity).
CC       Permeabilizes C.albicans cell membranes via targeting plasma membrane
CC       lipid phosphatidylinositol 4,5-bisphosphate (PIP2), thereby leading to
CC       cell fragmentation and cell death (By similarity). Acts as a ligand for
CC       C-C chemokine receptor CCR6 (By similarity). Binds to CCR6 and induces
CC       chemotactic activity of CCR6-expressing cells, such as immature
CC       dendritic cells and memory T cells (By similarity).
CC       {ECO:0000250|UniProtKB:O15263}.
CC   -!- SUBUNIT: Monomer (By similarity). Homodimer (By similarity).
CC       {ECO:0000250|UniProtKB:O15263}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15263}.
CC   -!- SIMILARITY: Belongs to the beta-defensin family. LAP/TAP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF288286; AAK26259.1; -; mRNA.
DR   RefSeq; NP_001027999.1; NM_001032827.1.
DR   AlphaFoldDB; Q9BDS9; -.
DR   SMR; Q9BDS9; -.
DR   PRIDE; Q9BDS9; -.
DR   InParanoid; Q9BDS9; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0031731; F:CCR6 chemokine receptor binding; ISS:UniProtKB.
DR   GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISS:UniProtKB.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; 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:0031640; P:killing of cells of another organism; ISS:UniProtKB.
DR   GO; GO:0051673; P:membrane disruption in another organism; ISS:UniProtKB.
DR   InterPro; IPR001855; Defensin_beta-typ.
DR   InterPro; IPR006080; Defensin_beta/alpha.
DR   Pfam; PF00711; Defensin_beta; 1.
DR   SMART; SM00048; DEFSN; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..64
FT                   /note="Defensin beta 4A"
FT                   /id="PRO_0000006969"
FT   REGION          33..48
FT                   /note="Phosphatidylinositol 4,5-bisphosphate (PIP2)
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:O15263"
FT   DISULFID        31..60
FT                   /evidence="ECO:0000250|UniProtKB:O15263"
FT   DISULFID        38..53
FT                   /evidence="ECO:0000250|UniProtKB:O15263"
FT   DISULFID        43..61
FT                   /evidence="ECO:0000250|UniProtKB:O15263"
SQ   SEQUENCE   64 AA;  7065 MW;  BB26454CE7ACCDDF CRC64;
     MRVLYLLFSF LFIFLMPLPG VFGGIGDPVT CLKNGAICHP VFCPRRYKQI GTCGLPGTKC
     CKKP