DFB4A_PANTR
ID DFB4A_PANTR Reviewed; 64 AA.
AC Q9TT12;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Flags: Precursor;
GN Name=DEFB4A; Synonyms=DEFB102, DEFB2, DEFB4;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Duits L.A., Langermans J.A.M., van der Straaten T., Vervenne R.A.W.,
RA Paltansing S., Frost P.A., Hiemstra P.S., Thomas A.W., Nibbering P.H.;
RT "Expression of beta-defensin-2 in chimpanzee (Pan troglodytes).";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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; AF209855; AAF20154.1; -; mRNA.
DR RefSeq; NP_001009076.1; NM_001009076.1.
DR AlphaFoldDB; Q9TT12; -.
DR SMR; Q9TT12; -.
DR STRING; 9598.ENSPTRP00000034201; -.
DR PaxDb; Q9TT12; -.
DR Ensembl; ENSPTRT00000101613; ENSPTRP00000072908; ENSPTRG00000050168.
DR GeneID; 450193; -.
DR KEGG; ptr:450193; -.
DR CTD; 1673; -.
DR eggNOG; ENOG502SYUI; Eukaryota.
DR GeneTree; ENSGT00940000160995; -.
DR HOGENOM; CLU_189296_4_1_1; -.
DR InParanoid; Q9TT12; -.
DR OMA; IRSGAIC; -.
DR OrthoDB; 1584343at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR Bgee; ENSPTRG00000050168; Expressed in thymus and 1 other tissue.
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_0000006970"
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; 7068 MW; B0D2454CE7ACCD13 CRC64;
MRVLYLLFSF LFIFLMPLPG VFGGISDPVT CLKSGAICHP VFCPRRYKQI GTCGLPGTKC
CKKP
