The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.

Catalysis of the release of a N-terminal glutamate (and to a lesser extent aspartate) from a peptide.

A fine reticular network of membrane-limited elements that pervades the sarcoplasm of a muscle fiber; continuous over large portions of the cell and with the nuclear envelope; an endoplasmic reticulum specialized for the sequestration of calcium ions.

Any process by which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner.

Catalysis of the degradation of insulin, glucagon and other polypeptides. No action on proteins.

Catalysis of the preferential cleavage of one bond in native collagen. Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-Ile776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Enables the directed movement of prostaglandins into, out of, within or between cells. A prostaglandin is any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities.

Catalysis of the hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at Ala14-Leu15 and Tyr16-Leu17 in the B chain of insulin.

Catalysis of the cleavage of Ala14-Leu15 and Tyr16-Leu17 in B chain of insulin. No action on collagen types I, II, IV and V. Cleaves gelatin chain alpha-2(I)

Enables the directed movement of sialic acid into, out of, within or between cells.

Catalysis of the hydrolysis of dipeptides.

Enables the directed movement of citrate, 2-hydroxy-1,2,3-propanetricarboyxlate, into, out of, within or between cells.

Catalysis of the hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.

Catalysis of the release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.