DEFA1

Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. Several alpha defensin genes appear to be clustered on chromosome 8. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. It differs from defensin, alpha 3 by only one amino acid. [provided by RefSeq]

Full Name

defensin, alpha 1

Function

Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.

Biological Process

Antibacterial humoral response Source: UniProtKB
Antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
Antimicrobial humoral response Source: Reactome
Cellular response to lipopolysaccharide Source: GO_Central
Chemotaxis Source: ProtInc
Defense response to fungus Source: UniProtKB-KW
Defense response to Gram-negative bacterium Source: GO_Central
Defense response to Gram-positive bacterium Source: UniProtKB
Defense response to protozoan Source: UniProtKB
Defense response to virus Source: UniProtKB-KW
Immune response Source: ProtInc
Innate immune response in mucosa Source: UniProtKB
Intracellular estrogen receptor signaling pathway Source: UniProtKB
Killing by host of symbiont cells Source: UniProtKB
Killing of cells of other organism Source: UniProtKB
Membrane disruption in other organism Source: GO_Central
Neutrophil degranulation Source: Reactome
Pore formation in membrane of other organism during symbiotic interaction Source: UniProtKB
T cell chemotaxis Source: UniProtKB

Cellular Location

Secreted

PTM

ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production.
Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-ribosylation.