|CD158e2||KIR3DL1 (killer cell immunoglobulin-like receptor, 3 domains, long tail ,1), NKAT10|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|CD158e2 is expressed on subsets of NK cells, on subsets of cytotoxic cells and some T cells. Expression on individual NK cells is complex and several members of the KIR family. The repertoire of KIR molecules varies among NK cells and is not determined solely by the HLA hapotypes. There is no expression in B lymphoblastic cell lines or in a colon carcinoma cell line.|
|MOLECULAR FAMILY NAME: Belongs to the immunoglobulin gene superfamily.|
CD158e2 is a single-pass type-1 387 aa glycoprotein. It contains an extracellular domain containing 3 Ig-like C2-type domains (D0, D1 and D2) rather than the 2 Ig-like domains of other KIRs with a short cytoplasmic tail, a transmembrane domain which contains a charged lysine residue and the 27 aa long cytoplasmic domain which has 2 ITIMs.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
POST-TRANSLATIONAL MODIFICATION: No information.
|LIGANDS AND MOLECULES ASSOCIATED WITH CD158e2|
|CD158e2 is involved in the activation of NK cell cytotoxicity.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD158e2 IN INTACT ANIMAL
CD158e2, in combination with HLA-B alleles, is associated with the delayed progression of AIDS in individuals infected with HIV-1. In the absence of CD158e2, HLA-B was not associated with any AIDS outcomes, but in the absence of HLA-B, there is a more rapid progression to AIDS. It is suggested that the depletion of CD4+ T cells created a protective response of NK cells involving CD158e2 and HLA class I ligands which begins soon after HIV-1 infection.
Killer cell immunoglobulin (Ig)-like receptors (KIR), also called killer cell inhibitory receptors, are glycoproteins expressed in natural killer (NK) cells and some T cells. The KIR family is estimated to include about 11 genes. Some members of the KIR family bind to certain HLA class I deficient cell lines. Ligation of such KIR by HLA class I molecules on target cells results in inhibition of the NK or T cell cytotoxic activity. The inhibition could be disrupted by antibodies against membrane glycoproteins on NK cells that recognized HLA- and HLA-C. Inhibitory KIRs are found in 3 distinct isoforms. KIRs that recognize HLA-C are usually monomeric glycoproteins of about 58 kDa with 2 Ig-like domains (KIR2D). KIRs that are reactive with HLA-B are approximately 70 kDa monomeric glycoproteins with 3 Ig-like domains (KIR3D). The KIR family is further subdivided into forms with short and long intracytoplasmic tails. The 1st and 2nd Ig domains in KIR2D are closely related in aa sequence to the 2nd and 3rd Ig domains in KIR3D. These 2 related Ig domains are called D1 and D2, respectively. D0 is the 1st Ig domain in KIR3D. KIR members vary in the length of the cytoplasmic tails. Most of the long cytoplasmic tails, KIR2DL and KIR3DL, deliver an inhibitory signal and carry 2 immunoreceptor tyrosine-based inhibition motifs (ITIM) which recruit and activate protein tyrosine phosphates, SHP-1 and or SHP-2. Other receptors, of about 50 kDa, with short cytoplasmic regions (KIR2DS and KIR3DS) are truncated before the 1st ITIM causing them to have no ITIMs. They are are connected to a transmembrane region which includes a lysine residue and can activate NK or T cell responses. The short tail associates with a disulfide dimer of 14 kDa. phosphoproteins called DAP12 which is also known as killer activating protein (KARAP).
Database accession numbers
Revised June 25, 2008