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IMP dehydrogenase
inosine-5'-monophosphate dehydrogenase catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the rate-limiting step in the de novo synthesis of guanine nucleotides
ligand-gated ion channel
ligand-gated ion channel (LIC or LGIC) is a member of a family of neurotransmitter receptors vital for communication throughout the nervous system
Dimerisation domain of Ca+-activated chloride-channel, anoctamin
This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins. (from Pfam)
Bartter syndrome, infantile, with sensorineural deafness (Barttin)
Barttin is a family of mammalian proteins that are chloride ion channel beta-subunits crucial for renal Cl-re-absorption and inner ear K+ secretion. Bartter syndrome is a term covering a heterogeneous group of autosomal recessive salt-losing nephropathies that are caused by disturbed transepithelial sodium chloride re-absorption in the distal nephron. Mutations in the BCD proteins lead to sensorial deafness. (from Pfam)
Calcium-activated chloride channel N terminal
The CLCA family of calcium-activated chloride channels has been identified in many epithelial and endothelial cell types as well as in smooth muscle cells [1] and has four or five putative transmembrane regions. Additionally to their role as chloride channels some CLCA proteins function as adhesion molecules and may also have roles as tumour suppressors [2]. This protein cleaves itself into an N-terminal portion and a C-terminal portion. The N-terminus contains an HEXXHXXXGXXDE motif which is essential for proteolytic cleavage [3-4]. (from Pfam)
Mid-1-related chloride channel (MCLC)
This family consists of several mid-1-related chloride channels. mid-1-related chloride channel (MCLC) proteins function as a chloride channel when incorporated in the planar lipid bilayer [1]. (from Pfam)
anoctamin
The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes [1]. (from Pfam)
chloride channel protein
This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 (Swiss:P35523) is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney [3]. These proteins contain two Pfam:PF00571 domains. (from Pfam)
CBS domain-containing protein
CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5]. (from Pfam)
bestrophin family ion channel
Human bestrophin is a chloride channel, while the Klebsiella pneumoniae homolog KpBest1 is a sodium channel.
ClC family voltage-gated chloride channel protein containing a C-terminal CBS pair domain, catalyzes the selective flow of Cl(-) ions across the cellular membrane
choice-of-anchor X domain-containing protein
Members of this domain family are highly variable in architecture, and found in both prokaryotes and eukaryotes. Prokaryotic members include proteins with C-terminal sorting signals for processing by rhombosortases and myxosortases and eventual surface attachment. Eukaryotic member proteins include human calcium-activated chloride channel regulator 4.
CLCA_X family protein
CLCAs, named for calcium-activated chloride channel bCLCA1, are proteins that resemble certain zinc-dependent metalloproteases in fold by lacking the signature HEXXH motifs. The CLCA_X family, described by this model, was identified based on weak similarities by Lenart, et al. as a notable CLCA-like family with a consistent architecture. The C-terminal half of the CLCA_X family was later described as the LPD1 domain (Large polyvalent protein-associated domain 1 - see PF18796) in a study of domains found within a variety of different architectures in larger proteins of phage and conjugative elements.
voltage-gated chloride channel family protein
voltage-gated chloride channel family protein similar to Salmonella enterica ion-transport protein YfeO
ClcB-like voltage-gated chloride channel protein
ClcB-like voltage-gated chloride channel protein is a ClC family voltage-gated chloride channel protein that catalyzes the selective flow of Cl(-) ions across the cellular membrane
anoctamin family protein
anoctamin family protein similar to anoctamin (anion channel with 8 transmembrane domains), which is a calcium-activated protein and may mediate the calcium-dependent exposure of phospholipids to the extracellular surface, a process called phospholipid scrambling
Voldacs domain-containing protein
Voldacs (volume decrease after cellular swelling) domain-containing protein similar to Homo sapiens methylosome subunit pICln that is involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins
CBS (cystathione beta synthase) domain-containing protein; CBS domains may act as regulatory units
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