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The protein encoded by this gene is a transformation and shape-change sensitive actin cross-linking/gelling protein found in fibroblasts and smooth muscle. Its expression is down-regulated in many cell lines, and this down-regulation may be an early and sensitive marker for the onset of transformation. A functional role of this protein is unclear. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibr

Band 3, also designated AE1, is an erythrocyte membrane glycoprotein that contributes to cell stuctural integrity and mediates exchange of chloride and bicarbonate across the phospholipid bilayer. The diverse functions of the approximately 900 amino acid protein are mediated by two distinct domains. The amino terminal domain, also known as cdb3 for cytoplasmic domain of erthrocyte membrane band 3, acts as an attachment site for the erythrocyte skeleton by binding ankyrin. The carboxy-terminal

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in

L1cam (L1 cell adhesion molecule isoform 1 precursor) is an axonal glycoprotein belonging to the immunoglobulin supergene family. The ectodomain, consisting of several immunoglobulin-like domains and fibronectin-like repeats (type III), is linked via a single transmembrane sequence to a conserved cytoplasmic domain. This cell adhesion molecule plays an important role in nervous system development, including neuronal migration and differentiation. Mutations in the gene cause three X-linked neu

C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages