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HAMAP rule MF_03175

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General rule information [?]

Accession MF_03175
Dates 5-JUN-2013 (Created)
7-DEC-2023 (Last updated, Version 12)
Name MetAP_2_euk
Scope(s) Eukaryota
Template(s) P50579 (MAP2_HUMAN); P38062 (MAP2_RAT); P38174 (MAP2_YEAST); Q8SR45 (MAP2_ENCCU); [ Recover all ]
Triggered by HAMAP; MF_03175 (Get profile general information and statistics)

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 + AltName: Full=Initiation factor 2-associated 67 kDa glycoprotein;
                 Short=p67eIF2;
                 Short=p67;
end case
case <OC:Vertebrata>
Gene name Name=METAP2;
else case <OC:Saccharomycotina>
Gene name Name=MAP2;
end case

Comments [?]

FUNCTIONCotranslationally 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>
FUNCTIONProtects 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.
SUBUNITBinds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3.
PTMContains 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 Name=Co(2+); Xref=ChEBI:CHEBI:48828; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; 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 LOCATIONCytoplasm. Note=About 30% of expressed @gn(METAP2) associates with polysomes.
else
SUBCELLULAR LOCATIONCytoplasm.
end case
SIMILARITYBelongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0046872; Molecular function:metal ion binding
GO:0070006; Molecular function:metalloaminopeptidase activity
GO:0004239; Molecular function:initiator methionyl aminopeptidase activity

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
NCBIfam TIGR00501; met_pdase_II; 1;
PROSITE PS01202; MAP_2; 1;
PROSITE PS50318; LYS_RICH; 0-unlimited;
General POLY_LYS; PolyAA; 0-unlimited;

Features [?]

From: MAP2_HUMAN (P50579)
Key From To Description Tag Condition FTGroup
BINDING 251 251 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="1"
D
BINDING 262 262 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="1"
D
BINDING 262 262 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="2"
/ligand_note="catalytic"
D
BINDING 331 331 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="2"
/ligand_note="catalytic"
H
BINDING 364 364 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="2"
/ligand_note="catalytic"
E
BINDING 459 459 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="1"
E
BINDING 459 459 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="2"
/ligand_note="catalytic"
E
BINDING 231 231 /ligand="substrate" H
BINDING 339 339 /ligand="substrate" H

Additional information [?]

Size range 357-486 amino acids
Related rules None
Fusion Nter: None Cter: None



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