This gene encodes a type I cell-surface receptor for the TGF-beta superfamily of ligands. It shares with an other type I receptors a high degree of similarity in serine-threonine kinase subdomains, a glycine-and serine-rich region (called the GS domain) preceding the kinase domain, and a short C-terminal tail. The encoded protein, sometimes termed ALK1, shares similar domain structures with an other closely related ALK or activin receptor-like kinase proteins that form a subfamily of receptor serine/threonine kinases. Mutations in this gene are associated with an hemorrhagic telangiectasia type 2, also known as Rendu-Osler-Weber syndrome 2.
Aminoacylase 1 (ACY1), a metalloenzyme that removes amide-linked ACY1 groups from amino acids and may play a role in regulating responses to oxidative stress. Both the C-terminal fragment found in the two-hybrid screen and full-length ACY1 co-immunoprecipitate with SphK1. Though both C-terminal and full-length proteins slightly reduce SphK1 activity measured in vitro, the C-terminal fragment inhibits while full-length ACY1 potentiates the effects of SphK1 on proliferation and apoptosis. It suggested that ACY1 physically interacts with SphK1 and may influence its physiological functions. As a homodimeric zinc-binding enzyme, Aminoacylase 1 catalyzes the hydrolysis of N alpha-acylated amino acids. Deficiency of Aminoacylase 1 due to mutations in the Aminoacylase 1 (ACY1) gene follows an autosomal-recessive trait of inheritance and is characterized by accumulation of N-acetyl amino acids in the urine.
Aspartoacylase 3, also known as ACY3, N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming), Acylase III, Aminoacylase-3, Aspartoacylase-2, Aspartoacylase-2, HCV core-binding protein 1 and ASPA2, is a member of the Aspartoacylase subfamily. ACY3 plays an important role in deacetylating mercapturic acids in kidney proximal tubules and acts on N-acetyl-aromatic amino acids.ACY3 is located in the cytoplasm of S2 and S3 proximal tubules and the apical domain of S1 proximal tubules. ACY3 protein is also expressed at low levels in stomach, testis, heart, brain, lung and liver, and may function as an HCV (Hepatitis C virus) core binding protein.
ACYP1; also known as Acylphosphatase-1; Acylphosphatase; erythrocyte isozyme; Acylphosphatase; organ-common type isozyme; Acylphosphate phosphohydrolase 1 and ACYPE; is a small cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates.ACYP1 is a protein which belongs to the acylphosphatase family and contains 1 fibrinogen C-terminal domain. Two isoenzymes have been isolated; called muscle acylphosphatase and erythrocyte acylphosphatase; on the basis of their tissue localization. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis. Recombinant human ACYP1 protein was expressed in E. coli fused with HIS-tag at N-terminus.
ACYP2; also known as Acylphosphatase-2; is a protein which belongs to the acylphosphatase family. ACYP2 contains one acylphosphatase-like domain. ACYP2 plays an important role in hydrolyzing the phosphoenzyme intermediate of different membrane pumps; particularly the Ca2+/Mg2+-ATPase from sarcoplasmic reticulum of skeletal muscle. Two isoenzymes have been isolated; called muscle acylphosphatase and erythrocyte acylphosphatase on the basis of their tissue localization. This gene encodes the muscle-type isoform (MT). An increase of the MT isoform is associated with muscle differentiation.
The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes.
ADAM15, also known as Metargidin, is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain) family of proteins and is widely expressed in different tissues and cell types. Members of this family contain an amino-terminal metalloprotease domain followed by a disintegrin domain, a cysteine-rich region and a membrane proximal EGF-like domain. The disintegrin domain of ADAM15/metargidin contains an RGD tripeptide sequence, suggesting that it may potentially interact with the integrin family of proteins. ADAM15 is a transmembrane multi-domain proteins implicated in proteolysis, cell-cell and cell-matrix interactions in various disease conditions. There is also evidence supporting a role for ADAM15 in angiogenesis and angioinvasion of tumor cells, which are critical for unrestrained tumor growth and metastatic spread. Given its diverse functions, ADAM15 may represent a pivotal regulatory component of tumor progression, an important target for therapeutic intervention, or emerge as a biomarker of disease progression.
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