Reviewed,
UniProtKB/Swiss-Prot Q91YP2 (NEUL_MOUSE)
Last modified
June 16, 2009.
Version 60.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Neurolysin, mitochondrial EC=3.4.24.16 Alternative name(s): Neurotensin endopeptidase Mitochondrial oligopeptidase M Microsomal endopeptidase Short name=MEP | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 704 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 | Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A By similarity. |
| Catalytic activity | Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subcellular location | Mitochondrion intermembrane space By similarity. Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase M3 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion |
| Domain | Transit peptide |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 37 | 37 | Mitochondrion | ||||||
| Chain | 38 – 704 | 667 | Neurolysin, mitochondrial | PRO_0000319046 | |||||
Sites | |||||||||
| Active site | 498 | 1 | By similarity | ||||||
| Metal binding | 497 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 501 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 504 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 32 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 44 | 1 | G → V in BAE27114. Ref.1 | ||||||
| Sequence conflict | 329 – 331 | 3 | LGE → HAS in AAH25520. Ref.2 | ||||||
Sequences
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References
| [1] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.  Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c and C57BL/6J. Tissue: Diencephalon. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AK079090 mRNA. Translation: BAC37533.1. AK146364 mRNA. Translation: BAE27114.1. BC016224 mRNA. Translation: AAH16224.1. BC025520 mRNA. Translation: AAH25520.1. | |
| IPI | IPI00314829. |
| RefSeq | NP_083723.1. |
| UniGene | Mm.127692 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I1I based on UniProtKB P42676. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M03.002. |
PTM databases | |
| PhosphoSite | Q91YP2. |
Proteomic databases | |
| PRIDE | Q91YP2. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000021710. Mus musculus. [Contig view] |
| GeneID | 75805. |
| KEGG | mmu:75805. |
| NMPDR | fig|10090.3.peg.28361. |
Organism-specific databases | |
| MGI | MGI:1923055. Nln. |
Phylogenomic databases | |
| HOGENOM | Q91YP2. |
| HOVERGEN | Q91YP2. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.16. 244. |
Gene expression databases | |
| ArrayExpress | Q91YP2. |
| Bgee | Q91YP2. |
| CleanEx | MM_NLN. |
Family and domain databases | |
| InterPro | IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view] |
| Pfam | PF01432. Peptidase_M3. 1 hit. [Graphical view] |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 344006. |
| SOURCE | Search... |
Entry information
| Entry name | NEUL_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q91YP2 Secondary accession number(s): Q3UJP1, Q8R3F4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
