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Q3ZC89 (AMPM2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine aminopeptidase 2
Short name=MAP 2
Short name=MetAP 2
EC=3.4.11.18
Alternative name(s):
Peptidase M 2
Gene names
Name:METAP2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins By similarity.

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 By similarity.

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.

Subunit structure

Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3 By similarity.

Subcellular location

Cytoplasm. Note: About 30% of expressed METAP2 associates with polysomes By similarity.

Post-translational modification

Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCobalt
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 477476Methionine aminopeptidase 2
PRO_0000246091

Regions

Compositional bias36 – 4611Arg/Lys-rich (basic)
Compositional bias81 – 9212Asp/Glu-rich (acidic)
Compositional bias97 – 1059Poly-Lys

Sites

Metal binding2501Cobalt 1 By similarity
Metal binding2611Cobalt 1 By similarity
Metal binding2611Cobalt 2 By similarity
Metal binding3301Cobalt 2 By similarity
Metal binding3631Cobalt 2 By similarity
Metal binding4581Cobalt 1 By similarity
Metal binding4581Cobalt 2 By similarity
Binding site2301Substrate By similarity
Binding site3381Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue451Phosphoserine By similarity
Modified residue621Phosphoserine By similarity
Modified residue4261N6-acetyllysine By similarity
Glycosylation621O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ZC89 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 4D10309613D2F0F1

FASTA47752,812
        10         20         30         40         50         60 
MAGVEEAASC GSHLNGDLDP DEREEGAAST AEEAAKKKKR KKKKSKGAAT GQQEPDKEAG 

        70         80         90        100        110        120 
ASVDEVTRQL ERQALEEKEK DDDDEDGDGD GDGATGKKKK KKKKKRGPKV QTDPPSVPIC 

       130        140        150        160        170        180 
DLYPNGVFPK GQECEYPPTQ DGRTAAWRTT SEEKKALDQA SEEIWNDFRE AAEAHRQVRK 

       190        200        210        220        230        240 
YVMSWIKPGM TMIEICEKME DCSRKLIKEN GLNAGLAFPT GCSLNNCAAH YTPNAGDTTV 

       250        260        270        280        290        300 
LQYDDICKID FGTHISGRII DCAFTVTFNP KYDTLLKAVK DATNTGIKCA GIDVRLCDVG 

       310        320        330        340        350        360 
EAIQEVMESY EVEIDGKTYQ VKPIRNLNGH SIGPYRIHAG KTVPIVKGGE ATRMEEGEVY 

       370        380        390        400        410        420 
AIETFGSTGK GVVHDDMECS HYMKNFDVGH VPIRLPRTKH LLNVINENFG TLAFCRRWLD 

       430        440        450        460        470 
RLGESKYLMA LKNLCDLGIV DPYPPLCDIK GSYTAQFEHT ILLRPTCKEV VSRGDDY

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC102824 mRNA. Translation: AAI02825.1.
IPIIPI00707569.
RefSeqNP_001035583.1. NM_001040493.1.
UniGeneBt.49424.

3D structure databases

ProteinModelPortalQ3ZC89.
SMRQ3ZC89. Positions 109-477.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ZC89.

Protein family/group databases

MEROPSM24.002.

Proteomic databases

PRIDEQ3ZC89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID404150.
KEGGbta:404150.

Organism-specific databases

CTD10988.

Phylogenomic databases

eggNOGmaNOG05636.
HOVERGENHBG050495.
InParanoidQ3ZC89.
OrthoDBEOG46T31M.
PhylomeDBQ3ZC89.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK01265.
PANTHERPTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMsTIGR00501. Met_pdase_II. 1 hit.
PROSITEPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM2_BOVIN
AccessionPrimary (citable) accession number: Q3ZC89
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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