Reviewed,
UniProtKB/Swiss-Prot P24155 (THOP1_RAT)
Last modified
June 16, 2009.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thimet oligopeptidase EC=3.4.24.15 Alternative name(s): Endo-oligopeptidase A Endopeptidase 24.15 PZ-peptidase Soluble metallo-endopeptidase | ||
| Gene names |
| ||
| 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 | 687 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. |
| Catalytic activity | Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Expressed abundantly in the testis. It is also found in the liver, lung and kidney. |
| Sequence similarities | Belongs to the peptidase M3 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Traceable author statement. Source: RGD |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | metalloendopeptidase activity Traceable author statement. Source: RGD peptide bindingInferred from direct assay. Source: RGD 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 687 | 686 | Thimet oligopeptidase | PRO_0000078155 | |||||
Sites | |||||||||
| Active site | 474 | 1 | By similarity | ||||||
| Metal binding | 473 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 477 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 480 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 278 | 1 | Phosphotyrosine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 321 | 1 | C → S in AAA41586. Ref.1 | ||||||
| Sequence conflict | 347 – 348 | 2 | TR → DS in AAA41586. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15." Pierotti A., Dong K.-W., Glucksman M.J., Orlowski M., Roberts J.L. Biochemistry 29:10323-10329(1990) [PubMed: 2261476] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Testis. |
| [2] | "Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzyme." McKie N., Dando P.M., Rawlings N.D., Barrett A.J. Biochem. J. 295:57-60(1993) [PubMed: 8216239] [Abstract] Cited for: SEQUENCE REVISION. |
| [3] | "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]. Tissue: Testis. |
| [4] | Lubec G., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 35-45; 267-273; 311-317; 351-357; 411-418 AND 560-578, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M61142 mRNA. Translation: AAA41586.1. BC081706 mRNA. Translation: AAH81706.1. | |
| IPI | IPI00211777. |
| PIR | HYRTTH. S38760. |
| RefSeq | NP_742072.2. |
| UniGene | Rn.9490 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I1I based on UniProtKB P42676. |
| SMR | P24155. Positions 24-677. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M03.001. |
PTM databases | |
| PhosphoSite | P24155. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000019924. Rattus norvegicus. [Contig view] |
| GeneID | 64517. |
| KEGG | rno:64517. |
Organism-specific databases | |
| RGD | 68330. Thop1. |
Phylogenomic databases | |
| HOVERGEN | P24155. |
| OMA | P24155. EQTKCVY. |
Enzyme and pathway databases | |
| BRENDA | 3.4.24.15. 248. |
Gene expression databases | |
| ArrayExpress | P24155. |
| GermOnline | ENSRNOG00000019924. Rattus norvegicus. |
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 | 613318. |
Entry information
| Entry name | THOP1_RAT | ||||||||
| Accession | Primary (citable) accession number: P24155 Secondary accession number(s): Q66HS4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


