Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD+ is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage.
Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. CLEC2 is a C-type lectin-like receptor expressed in myeloid cells and NK cells (Colonna et al., 2000 [PubMed 10671229]).
C-type lectin domain family 2 member D (CLEC2D), also known as lectin-like transcript 1 (LLT1) and osteoclast inhibitory lectin (OCIL), is a type II transmembrane C-type lectin receptor primarily expressed upon immune cell activation in T cells, B cells, NK cells, and plasmacytoid and monocyte-derived dendritic cells. CLEC2D interacts with NKR-P1A (KLRB1, CD161) on NK cells and some subsets of T cells, inhibiting NK cell cytotoxicity while alternatively inducing proliferation and IFNγ production in T cells. CLEC2D is also expressed by osteoblasts, inhibiting osteoclast formation and bone resorption.
Tetranectin binds to plasminogen and to isolated kringle 1. May be involved in the packaging of molecules destined for exocytosis.
Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion.
The protein encoded by this gene is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilizing an active conformation and considerably increasing the overall hydrophobic binding site. The gene product allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. This cofactor is only expressed in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Three transcript variants encoding different isoforms have been found for this gene.
Calsyntenins (calsyntenin-1, -2, -3) compose a family of neuronally expressed proteins that belong to the cadherin superfamily of cell adhesion molecules (PMID: 24966372; 12498782). Calsyntenin-1 (CLSTN1) is a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain. By binding Ca2+, calsyntenin-1 may modulate Ca2+-mediated postsynaptic signals (PMID: 11161476). Calsyntenin-1 is a transmembrane cargo-docking protein for Kinesin-1-mediated vesicular transport (PMID: 16760430). It can mediate axonal transport of the amyloid precursor protein and regulate Aβ production
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