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Reviewed, UniProtKB/Swiss-Prot P70645 (BLMH_RAT)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bleomycin hydrolase
      Short name=BLM hydrolase
      Short name=BMH
      Short name=BH
    EC=3.4.22.40
Gene names
Name: Blmh
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

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.

Sequence similarities

Belongs to the peptidase C1 family.

biophysicochemical properties

pH dependence:

Optimum pH is 7.5.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Bleomycin hydrolase
PRO_0000050553

Sites

Active site731 By similarity
Active site3721 By similarity
Active site3961 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70645-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 30BAC4A1A89DC1DC

FASTA45452,323
        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 

« Hide

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

D87336 mRNA. Translation: BAA13333.1.
IPIIPI00231419.
PIRJC4886.
UniGeneRn.100672

3D structure databases

HSSPHSSP built from PDB template 2CB5 based on UniProtKB Q13867.
SMRP70645. Positions 2-454.
ModBaseSearch...

Protein family/group databases

MEROPSC01.084.

Genome annotation databases

EnsemblENSRNOG00000003563. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD1304668. Blmh.

Phylogenomic databases

HOVERGENP70645.

Enzyme and pathway databases

BRENDA3.4.22.40. 248.

Gene expression databases

ArrayExpressP70645.
GermOnlineENSRNOG00000003563. Rattus norvegicus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERPTHR10363. Peptidase_C1B. 1 hit.
PfamPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFPIRSF005700. PepC. 1 hit.
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLMH_RAT
AccessionPrimary (citable) accession number: P70645
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents