Human Leukocyte Immunoglobulin-like Receptor Subfamily B Member 5 (LILRB5/CD85c/LIR-8) belongs to a family of transmembrane glycoproteins that negatively regulate immune cell activation. Mature human LIR-8 consists of a 435 amino acid (aa) extracellular domain with four Iglike domains, a 21 aa transmembrane segment, and a 111 aa cytoplasmic domain with two immunoreceptor tyrosine-based inhibitory motifs (ITIM). Alternative splicing of human LIR-8 generates an isoform that lacks the second Ig-like domain. LIR-8 is expressed on NK cells and in the tryptic granules of mast cells. Following cell activation and degranulation, it is present on the mast cell surface. Activated mast cells may also release soluble forms of LIR-8.
Lysosomal Integral Membrane Protein II (LIMPII), also known as SCARB2, LPG85, and CD36L2, is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. This protein may participate in membrane transportation and the reorganization of endosomal/lysosomal compartment. LIMPII is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Expression of human LIMPII enables normally unsusceptible cell lines to support the viruses’ propagation and develop cytopathic effects. In addition, LIMPII also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation. Deficiency of the protein in mice impairs cell membrane transport processes and causes pelvic junction obstruction, deafness, and peripheral neuropathy.
Scavenger Receptor Class B Member 2 (SCARB2) is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal/lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, SCARB2 also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.
Antimicrobial protein that is an integral component of the innate immune system. Binds to bacterial lipopolysaccharides (LPS). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin. The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro).
VIP36-like protein (LMAN2L) is a single-pass type I membrane protein and contains 1 L-type lectin-like domain. It is highly expressed in skeletal muscle and kidney, and its intermediate expression levels in heart, liver and placenta, low levels in brain, thymus, spleen, small intestine and lung. LMAN2L may be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. It also may function as a regulator of ERGIC-53.
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