Home  |  Contact
Annotation rule MF_03175
Send feedback

General rule information [?]

Accession MF_03175
Dates 5-JUN-2013 (Created)
20-NOV-2019 (Last updated, Version 7)
Name MetAP_2_euk
Scope
Eukaryota
Templates P50579 (MAP2_HUMAN); P38062 (MAP2_RAT); P38174 (MAP2_YEAST); Q8SR45 (MAP2_ENCCU): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
MAP2
Protein name
RecName: Full=Methionine aminopeptidase 2;
Short=MAP 2;
Short=MetAP 2;
EC 3.4.11.18;
AltName: Full=Peptidase M;
case <OC:Vertebrata>
Protein name
Full=Initiation factor 2-associated 67 kDa glycoprotein;
Short=p67eIF2;
Short=p67;
end case
case <OC:Vertebrata>
Gene name
METAP2
else case <OC:Saccharomycotina>
Gene name
MAP2
end case

Comments [?]

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).
case <OC:Vertebrata>
Function Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
Subunit Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3.
Ptm Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.
end case
Catalytic activity Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18;
Cofactor Co(2+)
Zn(2+)
Mn(2+)
Fe(2+)
Note: 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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
case <OC:Vertebrata>
Subcellular location Cytoplasm. Note=About 30% of expressed @gn(METAP2) associates with polysomes.
else
Subcellular location Cytoplasm.
end case
Similarity Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.

Keywords [?]

case <OC:Vertebrata>
end case

Gene Ontology [?]

GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0070084; Biological process: protein initiator methionine removal.

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
TIGRFAMs TIGR00501; met_pdase_II; 1;
PROSITE PS01202; MAP_2; 1;
PS50318; LYS_RICH; 0-unlimited;

Computed features [?]

General POLY_LYS; PolyAA; 0-unlimited;

Features [?]

From: MAP2_HUMAN (P50579)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     251     251       Divalent metal cation 1     D  
METAL     262     262       Divalent metal cation 1     D  
METAL     262     262       Divalent metal cation 2; catalytic     D  
METAL     331     331       Divalent metal cation 2; catalytic; via tele nitrogen     H  
METAL     364     364       Divalent metal cation 2; catalytic     E  
METAL     459     459       Divalent metal cation 1     E  
METAL     459     459       Divalent metal cation 2; catalytic     E  
BINDING     231     231       Substrate     H  
BINDING     339     339       Substrate     H  

Additional information [?]

Size range 357-486 amino acids
Related rules None
Fusion None