DEFA5
entrez
1670
canonical
uniprot
Q01523
canonical
ensembl
ENSG00000164816
resolver
ensembl
ENSG00000285251
resolver
ensp
ENSP00000329890
resolver
ensp
ENSP00000494799
resolver
enst
ENST00000330590
resolver
enst
ENST00000647159
resolver
genesymbol
DEFA5
resolver
genesymbol_syn
DEF5
resolver
hgnc
HGNC:2764
resolver
uniprot
A0JDY6
resolver
uniprot
Q3KNV2
resolver
uniprot_entry
DEF5_HUMAN
resolver
uniprot_sec
A0JDY6
resolver
uniprot_sec
Q3KNV2
resolver
amino_acid_sequence
MRTIAILAAILLVALQAQAESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRTGRCATRESLSGVCEISGRLYRLCCR
uniprot
proteins
function
FUNCTION: Host-defense peptide that maintains sterility in the urogenital system (PubMed:12021776, PubMed:12660734, PubMed:15616305, PubMed:19589339, PubMed:22359618, PubMed:22573326, PubMed:25354318, PubMed:25782105, PubMed:30808760). Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes (PubMed:12021776, PubMed:15616305, PubMed:19589339, PubMed:22359618, PubMed:22573326, PubMed:25354318, PubMed:30808760). Confers resistance to intestinal infection by S.typhimurium (PubMed:12660734). Exhibits antimicrobial activity against enteric commensal bacteria such as B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and S.thermophilus (PubMed:25354318). Binds to bacterial membranes and causes membrane disintegration (PubMed:25782105). Induces the secretion of the chemokine IL-8 by intestinal epithelial cells (PubMed:19589339). Binds to B.antracis lef/lethal factor, a major virulence factor from B.anthracis, and neutralizes its enzymatic activity (PubMed:22573326). {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:12660734, ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:19589339, ECO:0000269|PubMed:22359618, ECO:0000269|PubMed:22573326, ECO:0000269|PubMed:25354318, ECO:0000269|PubMed:25782105, ECO:0000269|PubMed:30808760}.; FUNCTION: (Microbial infection) Acts as a target for S.flexneri infection by binding to the bacterium, possibly via bacterial surface proteins, and thereby augmenting infectivity via enhanced bacterial adhesion and invasion of epithelial cells and tissues. {ECO:0000269|PubMed:29858013}.
uniprot
proteins
mass_dalton
10071
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="C->S: Prohibits tetramer formation; when associated with S-93."; /evidence="ECO:0000269|PubMed:23163963"; MUTAGEN 69; /note="T->R: Enhanced antibacterial activity against both E.coli and S.aureus. Enhanced membrane binding and membrane disintegration abilities, as well as further increased antibacterial activity; when associated with R-83."; /evidence="ECO:0000269|PubMed:25782105"; MUTAGEN 71; /note="R->A: Reduced killing of S.aureus and E.coli. Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-90. Reduced induction of IL-8 secretion; when associated with A-90."; /evidence="ECO:0000269|PubMed:19589339, ECO:0000269|PubMed:22573326"; MUTAGEN 71; /note="R->K: Impairs antimicrobial activity against S. aureus; when associated with K-90. Reduced induction of IL-8 secretion; when associated with K-90."; /evidence="ECO:0000269|PubMed:19589339"; MUTAGEN 72; /note="C->S: Prohibits tetramer formation; when associated with S-92."; /evidence="ECO:0000269|PubMed:23163963"; MUTAGEN 75; /note="R->A: Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-94. Reduced induction of IL-8 secretion; when associated with A-94."; /evidence="ECO:0000269|PubMed:19589339"; MUTAGEN 75; /note="R->K: Does not impair antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with K-94. Reduced induction of IL-8 secretion; when associated with K-90."; /evidence="ECO:0000269|PubMed:19589339"; MUTAGEN 77; /note="S->A: Increased interaction with B.antracis lef/lethal factor."; /evidence="ECO:0000269|PubMed:22573326"; MUTAGEN 83; /note="E->R: Enhanced antibacterial activity against both E.coli and S.aureus. Disrupts homodimerization. Enhanced membrane binding and membrane disintegration abilities, as well further increased antibacterial activity; when associated with R-69."; /evidence="ECO:0000269|PubMed:25782105"; MUTAGEN 85; /note="S->R: Enhanced antibacterial activity against both E.coli and S.aureus."; /evidence="ECO:0000269|PubMed:25782105"; MUTAGEN 86; /note="G->R: Enhanced antibacterial activity against both E.coli and S.aureus."; /evidence="ECO:0000269|PubMed:25782105"; MUTAGEN 88; /note="L->A: Reduced interaction with B.antracis lef/lethal factor. Reduced enhancement of S.flexneri infection."; /evidence="ECO:0000269|PubMed:22573326, ECO:0000269|PubMed:29858013"; MUTAGEN 89; /note="Y->A: Disrupts homodimer-formation. Reduced interaction with B.antracis lef/lethal factor and reduced killing of S.aureus. Reduced enhancement of S.flexneri infection."; /evidence="ECO:0000269|PubMed:22573326, ECO:0000269|PubMed:29858013"; MUTAGEN 90; /note="R->A: Does not disrupt homodimer-formation. Reduced enhancement of S.flexneri infection. Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-71. Reduced induction of IL-8 secretion; when associated with A-71."; /evidence="ECO:0000269|PubMed:19589339, ECO:0000269|PubMed:29858013"; MUTAGEN 90; /note="R->K: Impairs antimicrobial activity against S. aureus; when associated with K-71. Reduced induction of IL-8 secretion; when associated with K-71."; /evidence="ECO:0000269|PubMed:19589339"; MUTAGEN 91; /note="L->A: Reduced interaction with B.antracis lef/lethal factor and decreased bactericidal activity against E.coli and S.aureus. Reduced enhancement of S.flexneri infection."; /evidence="ECO:0000269|PubMed:22573326, ECO:0000269|PubMed:29858013"; MUTAGEN 92; /note="C->S: Prohibits tetramer formation; when associated with S-72."; /evidence="ECO:0000269|PubMed:23163963"; MUTAGEN 93; /note="C->S: Prohibits tetramer formation; when associated with S-67."; /evidence="ECO:0000269|PubMed:23163963"; MUTAGEN 94; /note="R->A: Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-75. Reduced induction of IL-8 secretion; when associated with A-75."; /evidence="ECO:0000269|PubMed:19589339"; MUTAGEN 94; /note="R->K: Does not impair antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with K-75. Reduced induction of IL-8 secretion; when associated with K-75."; /evidence="ECO:0000269|PubMed:19589339
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:12021776}.; PTM: Proteolytically cleaved at Arg-62 by trypsin (PubMed:12021776). Both the propeptide form proHD5/HD5(20-94) and HD5(56-94) are cleaved into the lumenal peptide form HD5(63-94) by trypsin (PubMed:12021776). Unprocessed proHD5 exerts antimicrobial activities, but peptide potency is enhanced by peptide processing (PubMed:12021776). Proteolytically cleaved in duodenal fluid; derived fragments are antimicrobially active against commensal bacteria (in vitro) (PubMed:30808760). {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:30808760}.; PTM: (Microbial infection) The disulfide bridges and homodimerization are a prerequisite for the enhancement of S.flexneri adhesion and invasion. {ECO:0000269|PubMed:29858013}.
uniprot
proteins
protein_family
Alpha-defensin family
uniprot
proteins
pubmed
12021776
uniprot
proteins
pubmed
12660734
uniprot
proteins
pubmed
1429669
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616305
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17088326
uniprot
proteins
pubmed
19589339
uniprot
proteins
pubmed
22359618
uniprot
proteins
pubmed
22573326
uniprot
proteins
pubmed
23163963
uniprot
proteins
pubmed
25354318
uniprot
proteins
pubmed
25782105
uniprot
proteins
pubmed
29858013
uniprot
proteins
pubmed
30808760
uniprot
proteins
pubmed
9588893
uniprot
proteins
sequence_length
94
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}. Note=Stored as propeptide HD5(20-94) in secretory granules of small intestinal Paneth cells and found in the ileum lumen as processed mature peptides, predominantly in the HD5(63-94) form (PubMed:12021776). Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form (PubMed:12021776). Secreted into the female genital tract lumen (PubMed:9588893). {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}.
uniprot
proteins