Q5RBF3 (AMPM1_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 47.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methionine aminopeptidase 1 Short name=MAP 1 Short name=MetAP 1 EC=3.4.11.18 Alternative name(s): Peptidase M 1 | ||
| Gene names |
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| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 386 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins 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. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity. |
| Sequence similarities | Belongs to the peptidase M24A family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Cobalt Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | cellular process Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 386 | 385 | Methionine aminopeptidase 1 | PRO_0000323735 | |||||
Sites | |||||||||
| Metal binding | 220 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 231 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 231 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 294 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 327 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 358 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 358 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 203 | 1 | Substrate By similarity | ||||||
| Binding site | 301 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 253 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR858696 mRNA. Translation: CAH90907.1. |
| RefSeq | NP_001125517.1. NM_001132045.1. |
| UniGene | Pab.13560. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2B3H based on UniProtKB P53582. |
| ProteinModelPortal | Q5RBF3. |
| SMR | Q5RBF3. Positions 81-384. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M24.001. |
Proteomic databases | |
| PRIDE | Q5RBF3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSPPYT00000017366; ENSPPYP00000016687; ENSPPYG00000014945. |
| GeneID | 100172428. |
| KEGG | pon:100172428. |
Organism-specific databases | |
| CTD | 23173. |
Phylogenomic databases | |
| HOVERGEN | HBG067178. |
| InParanoid | Q5RBF3. |
| OMA | IEPMISE. |
| OrthoDB | EOG40S0FP. |
Family and domain databases | |
| InterPro | IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view] |
| Gene3D | G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit. |
| KO | K01265. |
| Pfam | PF00557. Peptidase_M24. 1 hit. [Graphical view] |
| PRINTS | PR00599. MAPEPTIDASE. |
| SUPFAM | SSF55920. Peptidase_M24_cat_core. 1 hit. |
| TIGRFAMs | TIGR00500. Met_pdase_I. 1 hit. |
| PROSITE | PS00680. MAP_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPM1_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RBF3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with