AC   MF_03175;
DC   Protein; auto
TR   HAMAP; MF_03175; -; 1; level=0
XX
Names: MetAP_2_euk
XX
ID   MAP2
DE   RecName: Full=Methionine aminopeptidase 2;
DE            Short=MAP 2;
DE            Short=MetAP 2;
DE            EC=3.4.11.18;
DE   AltName: Full=Peptidase M;
case <OC:Vertebrata>
DE   + AltName: Full=Initiation factor 2-associated 67 kDa glycoprotein;
DE            Short=p67eIF2;
DE            Short=p67;
end case
case <OC:Vertebrata>
GN   Name=METAP2;
else case <OC:Saccharomycotina>
GN   Name=MAP2;
end case
XX
CC   -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC       nascent proteins. The N-terminal methionine is often cleaved when the
CC       second residue in the primary sequence is small and uncharged (Met-
CC       Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
case <OC:Vertebrata>
CC   -!- FUNCTION: Protects eukaryotic initiation factor EIF2S1 from
CC       translation-inhibiting phosphorylation by inhibitory kinases such as
CC       EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of
CC       protein synthesis.
CC   -!- SUBUNIT: Binds EIF2S1 at low magnesium concentrations. Interacts
CC       strongly with the eIF-2 gamma-subunit EIF2S3.
CC   -!- PTM: Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc)
CC       residues. O-glycosylation is required for EIF2S1 binding.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC       and a low affinity metal-binding site. The true nature of the
CC       physiological cofactor is under debate. The enzyme is active with
CC       cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC       aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC       physiological conditions, and the catalytically relevant metal-binding
CC       site has been assigned to the histidine-containing high-affinity site.;
case <OC:Vertebrata>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About 30% of expressed
CC       @gn(METAP2) associates with polysomes.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase eukaryotic type 2 subfamily.
XX
DR   Pfam; PF00557; Peptidase_M24; 1; trigger=no
DR   PRINTS; PR00599; MAPEPTIDASE; 1; trigger=no
DR   NCBIfam; TIGR00501; met_pdase_II; 1; trigger=no
DR   PROSITE; PS01202; MAP_2; 1; trigger=no
DR   PROSITE; PS50318; LYS_RICH; 0-unlimited; trigger=strict
DR   General; POLY_LYS; PolyAA; 0-unlimited; trigger=strict
XX
KW   Aminopeptidase
KW   Cytoplasm
KW   Hydrolase
KW   Metal-binding
KW   Protease
case <OC:Vertebrata>
KW   Glycoprotein
end case
XX
GO   GO:0046872; F:metal ion binding
GO   GO:0070006; F:metalloaminopeptidase activity
GO   GO:0004239; F:initiator methionyl aminopeptidase activity
XX
FT   From: MAP2_HUMAN (P50579)
FT   BINDING         251
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         262
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         262
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Condition: D
FT   BINDING         331
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Condition: H
FT   BINDING         364
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Condition: E
FT   BINDING         459
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         459
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Condition: E
FT   BINDING         231
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         339
FT                   /ligand="substrate"
FT   Condition: H
XX
Size: 357-486;
Related: None;
Template: P50579; P38062; P38174; Q8SR45;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in AJECG, AJEDR, AJEDS, ARATH, ARTGP, ARTOC, ASPCL, ASPFC, ASPFN,
 ASPFU, ASPNC, ASPTN, CHAGB, COLGM, EMENI, LEPMJ, FUSV7, NEOFI, PENCW, PENMQ,
 PYRTR, PYRTT, TALSN
Plasmid: None
Comments: None
XX
# Revision 1.12 2023/12/07
//