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This gene is a member of the receptors of complement activation (RCA) family and is located in the 'cluster RCA' region of chromosome 1. The genome is polymorphic at this locus with allele-specific splice variants encoding different isoforms, based on the presence/absence of long homologous repeats (LHRs). The gene encodes a monomeric single-pass type I membrane glycoprotein found on erythrocytes, leukocytes, glomerular podocytes, and splenic follicular dendritic cells. The Knops blood grou

Prostaglandins are produced by the metabolism of arachidonic acid. Prostaglandin E2 is one of the five physiologically significant prostanoids known. Its wide spectrum of physiologic and pharmacologic effects in various tissues is mediated through binding to the Prostaglandin E2 receptors (EP1, EP2, EP3 & EP4). These include effects on the immune, endocrine, cardiovascular, renal and reproductive systems as well as smooth muscle. It is also one of the most abundant of the prostanoid f

The four human glycoprotein hormones chorionic gonadotropin (CG), luteinizing hormone (LH), follicle stimulating hormone (FSH), and thyroid stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits of these hormones are identical, however, their beta chains are unique and confer biological specificity. Thyroid stimulating hormone functions in the control of thyroid structure and metabolism. The protein encoded by this ge

The protein encoded by this gene is a 36-kD water-soluble protein which carries 11-cis-retinaldehyde or 11-cis-retinal as physiologic ligands. It may be a functional component of the visual cycle. Mutations of this gene have been associated with severe rod-cone dystrophy, Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa) and retinitis punctata albescens. [provided by RefSeq, Jul 2008]

PTBP-2 is a member of the polypyrimidine tract binding family of proteins. Predominantly expressed in brain, but also found in heart and skeletal muscle, PTBP-2 localizes to the nucleus and contains four RRM (RNA recognition motif) domains. PTBP-2 functions as an RNA-binding protein associated in a complex that is involved in the regulation of exon splicing and the stabilization of mRNAs in the cytoplasm. Six isoforms exist for PTBP-2 due to alternative splicing events. Isoforms 1 and 2 (al