P70645 (BLMH_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 85.
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: Bleomycin hydrolase Short name=BH Short name=BLM hydrolase Short name=BMH EC=3.4.22.40 | ||
| 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 | 454 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity By similarity. Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics. |
| Catalytic activity | Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred. |
| Subunit structure | Homohexamer. |
| Subcellular location | |
| Tissue specificity | Expressed at relatively higher levels in the stomach, esophagus, spleen, thymus and testis, and at lower levels in the skin, lung and skeletal muscle. |
| Sequence similarities | Belongs to the peptidase C1 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.5. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 454 | 454 | Bleomycin hydrolase | PRO_0000050553 | |||||
Sites | |||||||||
| Active site | 73 | 1 | By similarity | ||||||
| Active site | 372 | 1 | By similarity | ||||||
| Active site | 396 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.2 | ||||||
| Modified residue | 391 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Cloning and analysis of cDNA encoding rat bleomycin hydrolase, a DNA-binding cysteine protease." Takeda A., Masuda Y., Yamamoto T., Hirabayashi T., Nakamura Y., Nakaya K. J. Biochem. 120:353-359(1996) [PubMed: 8889821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-62; 165-175 AND 283-296. Tissue: Spleen. |
| [2] | "Purification and characterization of bleomycin hydrolase, which represents a new family of cysteine proteases, from rat skin." Takeda A., Higuchi D., Yamamoto T., Nakamura Y., Masuda Y., Hirabayashi T., Nakaya K. J. Biochem. 119:29-36(1996) [PubMed: 8907172] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1, CHARACTERIZATION. Tissue: Skin. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D87336 mRNA. Translation: BAA13333.1. |
| IPI | IPI00231419. |
| PIR | JC4886. |
| UniGene | Rn.100672. |
3D structure databases | |
| ProteinModelPortal | P70645. |
| SMR | P70645. Positions 2-454. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P70645. 1 interaction. |
| STRING | P70645. |
Protein family/group databases | |
| MEROPS | C01.084. |
Proteomic databases | |
| PRIDE | P70645. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | NM_001034163. rat. |
Organism-specific databases | |
| RGD | 1304668. Blmh. |
Phylogenomic databases | |
| GeneTree | ENSGT00390000001735. |
| HOVERGEN | HBG002388. |
| InParanoid | P70645. |
| OrthoDB | EOG4J3WGT. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.40. 5301. |
Gene expression databases | |
| ArrayExpress | P70645. |
| Genevestigator | P70645. |
| GermOnline | ENSRNOG00000003563. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR004134. Peptidase_C1B. [Graphical view] |
| PANTHER | PTHR10363. Peptidase_C1B. 1 hit. |
| Pfam | PF03051. Peptidase_C1_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF005700. PepC. 1 hit. |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BLMH_RAT | ||||||||
| Accession | Primary (citable) accession number: P70645 | ||||||||
| 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 |

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