Reviewed, UniProtKB/Swiss-Prot P38062 (AMPM2_RAT)

Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase 2
      Short name=MetAP 2
      Short name=MAP 2
    EC=3.4.11.18
Alternative name(s):
    Peptidase M 2
    Initiation factor 2-associated 67 kDa glycoprotein
    p67eIF2
      Short name=p67

Gene names

Name:	Metap2
Synonyms:	Mnpep, P67eif2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins. Protects eIF-2 alpha-subunit from inhibitory phosphorylation by eIF-2 kinases. Plays a critical role in the regulation of protein synthesis. It also interacts with the eIF-2 gamma-subunit.
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.
Post-translational modification	O-glycosylated; contains 12 O-linked GlcNAc.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Acetylation Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Inferred from sequence or structural similarity. Source: HGNC peptidyl-methionine modification Inferred from sequence or structural similarity. Source: HGNC protein processing Inferred from sequence or structural similarity. Source: HGNC proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: HGNC
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	Methionine aminopeptidase 2		PRO_0000148984
Regions
	Compositional bias	36 – 46	11	Arg/Lys-rich (basic)
	Compositional bias	82 – 93	12	Asp/Glu-rich (acidic)
	Compositional bias	98 – 106	9	Poly-Lys
Sites
	Metal binding	251	1	Cobalt 1 By similarity
	Metal binding	262	1	Cobalt 1 By similarity
	Metal binding	262	1	Cobalt 2 By similarity
	Metal binding	331	1	Cobalt 2 By similarity
	Metal binding	364	1	Cobalt 2 By similarity
	Metal binding	459	1	Cobalt 1 By similarity
	Metal binding	459	1	Cobalt 2 By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	339	1	Substrate By similarity
Amino acid modifications
	Modified residue	60	1	Phosphoserine By similarity
	Modified residue	63	1	Phosphoserine By similarity
	Modified residue	427	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	464 – 478	15	LRPTC…RGDDY → CAQPVKKLSAEEMTIKT in AAA41111. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38062-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: BE1C0E91E0CB3D74	FASTA	478	53,052
	10 20 30 40 50 60 MAGVEEASSF GGHLNRDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS AGQQELDKES 70 80 90 100 110 120 GTSVDEVAKQ LERQALEEKE KDDDDEDGDG DGDGAAGKKK KKKKKKRGPR VQTDPPSVPI 130 140 150 160 170 180 CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR 190 200 210 220 230 240 KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT 250 260 270 280 290 300 VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDILLKAV KDATNTGIKC AGIDVRLCDV 310 320 330 340 350 360 GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG EATRMEEGEV 370 380 390 400 410 420 YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL 430 440 450 460 470 DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY

References

[1]	"Cloning and characterization of complementary DNA encoding the eukaryotic initiation factor 2-associated 67-kDa protein (p67)." Wu S., Gupta S., Chatterjee N., Hileman R.E., Kinzy T.G., Denslow N.D., Merrick W.C., Chakrabarti D., Osterman J.C., Gupta N.K. J. Biol. Chem. 268:10796-10801(1993) [PubMed: 8496145] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Reuber H35. Tissue: Liver.
[2]	"Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes." Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A. Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995) [PubMed: 7644482] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L10652 mRNA. Translation: AAA41111.1.
IPI	IPI00480610.
PIR	A46702.
RefSeq	NP_071984.1.
UniGene	Rn.1984
3D structure databases
HSSP	HSSP built from PDB template 1B6A based on UniProtKB P50579.
SMR	P38062. Positions 110-478.
ModBase	Search...
Protein family/group databases
MEROPS	M24.002.
Genome annotation databases
Ensembl	ENSRNOT00000030056; ENSRNOP00000032680; ENSRNOG00000021881; Rattus norvegicus. [Genome view] ENSRNOT00000034664; ENSRNOP00000029380; ENSRNOG00000021881; Rattus norvegicus. [Genome view]
GeneID	64370.
KEGG	rno:64370.
UCSC	BC091150. rat.
Organism-specific databases
CTD	64370.
RGD	70995. Metap2.
Phylogenomic databases
HOVERGEN	P38062.
Enzyme and pathway databases
BRENDA	3.4.11.18. 248.
Gene expression databases
Genevestigator	P38062.
GermOnline	ENSRNOG00000021881. Rattus norvegicus.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002468. Pept_M24A_MAP2. IPR018349. Pept_M24A_MAP2_BS. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHER	PTHR10804:SF9. Pept_M24A_MAP2. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
TIGRFAMs	TIGR00501. met_pdase_II. 1 hit.
PROSITE	PS01202. MAP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	613106.

Entry information

Entry name

AMPM2_RAT

Accession

Primary (citable) accession number: P38062

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)