Eosinophil major basic protein, C-type lectin-like domain (IPR033816)

Short name: EMBP_CTLD

Overlapping homologous superfamilies

Domain relationships

  • C-type lectin-like (IPR001304)
    • Eosinophil major basic protein, C-type lectin-like domain (IPR033816)


This is a C-type lectin-like domain (CTLD) of the type found in the human proteins eosinophil major basic protein (EMBP) and prepro major basic protein homologue (MBPH) [PMID: 11292023]. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins [PMID: 16336259].

Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. The proform inhibits the metallopeptidase pregnancy-associated plasma protein A [PMID: 12421832,PMID: 10913121] and is considered to be a peptidase inhibitor (MEROPS identifier I63.001). EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites [PMID: 3171483]. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production [PMID: 10318872]. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent [PMID: 16245931]. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP [PMID: 11292023,PMID: 7531438].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.