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UniProtKB/Swiss-Prot entry P70645


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BLMH_RAT
Primary accession number P70645
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Bleomycin hydrolase
Synonyms BLM hydrolase
BMH
BH
EC 3.4.22.40
Gene name
Name: Blmh
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 44-62; 165-175 AND 283-296.
TISSUE=Spleen;
PubMed=8889821 [NCBI, ExPASy, EBI, Israel, Japan]
Takeda A., Masuda Y., Yamamoto T., Hirabayashi T., Nakamura Y., Nakaya K.;
"Cloning and analysis of cDNA encoding rat bleomycin hydrolase, a DNA-binding cysteine protease.";
J. Biochem. 120:353-359(1996).
[2]
PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1, AND CHARACTERIZATION.
TISSUE=Skin;
PubMed=8907172 [NCBI, ExPASy, EBI, Israel, Japan]
Takeda A., Higuchi D., Yamamoto T., Nakamura Y., Masuda Y., Hirabayashi T., Nakaya K.;
"Purification and characterization of bleomycin hydrolase, which represents a new family of cysteine proteases, from rat skin.";
J. Biochem. 119:29-36(1996).
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.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    pH dependence:   Optimum pH is 7.5;
  • SUBUNIT: Homohexamer.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • 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.
  • SIMILARITY: Belongs to the peptidase C1 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D87336; BAA13333.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4886; JC4886.
UniGene Rn.100672
3D structure databases
HSSP Q13867; 2CB5. [HSSP ENTRY / PDB]
SMR P70645; 2-454.
ModBase P70645.
Protein family/group databases
MEROPS C01.084; -.
Organism-specific databases
RGD 1304668; Blmh.
Gene expression databases
ArrayExpress P70645; -.
GermOnline ENSRNOG00000003563; Rattus norvegicus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR004134; Peptidase_C1B.
Graphical view of domain structure.
PANTHER PTHR10363; Peptidase_C1B; 1.
Pfam PF03051; Peptidase_C1_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005700; PepC; 1.
PROSITE PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; FALSE_NEG.
ProtoNet P70645.
Genome annotation databases
Ensembl ENSRNOG00000003563; Rattus norvegicus. [Contig view]
Phylogenomic databases
HOVERGEN P70645; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Thiol protease.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   454  454     Bleomycin hydrolase. PRO_0000050553
ACT_SITE   73    73        By similarity. 
ACT_SITE   372   372        By similarity. 
ACT_SITE   396   396        By similarity. 
MOD_RES   1     1        N-acetylmethionine. 
Sequence information
Length: 454 AA [This is the length of the unprocessed precursor] Molecular weight: 52323 Da [This is the MW of the unprocessed precursor] CRC64: 30BAC4A1A89DC1DC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNNAGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQGAQ HVFQHVVPQE 

        70         80         90        100        110        120 
GKPVTNQKSS GRCWIFSCLN VMRLPFMKKF NIEEFEFSQS YLFFWDKVER CYFFLNAFVD 

       130        140        150        160        170        180 
TAQKKEPEDG RLVQYLLMNP TNDGGQWDML VNIVEKYGVV PKKCFPESHT TEATRRMNDI 

       190        200        210        220        230        240 
LNHKMREFCI RLRNLVHSGA TKGEISSTQD AMMEEIFRVV CICLGNPPET FTWEYRDKDK 

       250        260        270        280        290        300 
NYHKVGPITP LQFYKEHVKP LFNMEDKICF VNDPRPQHKY NKLYTVDYLS NMVGGRKTLY 

       310        320        330        340        350        360 
NNQPIDFLKK MVAASIRDGE AVWFGCDVGK HFNGKLGLSD MNVYDHELVF GVSLKNMNKA 

       370        380        390        400        410        420 
ERLAFGESLM THAMTFTAVS EKDDQEGAFV KWRVENSWGE DHGHKGYLCM TDEWFSEYVY 

       430        440        450 
EVVVDKKHVP EEVLAVLEQE PIVLPAWDPM GALA 

P70645 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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