METAP1 Antibody – Mouse Monoclonal

Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. Ref.7 Ref.9

Catalytic activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.9

Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site

By similarity. Ref.7Binds 1 sodium ion per subunit. The sodium ion has a structural role. Ref.7

Subunit structure: Associates with the 60S ribosomal subunit of the 80S translational complex

By similarity.

Subcellular location: Cytoplasm

By similarity HAMAP-Rule MF_03174.

Sequence similarities: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Sequence caution: The sequence AAH30054.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA07679.1 differs from that shown. Reason: Erroneous initiation.