BLMH_RABIT
ID BLMH_RABIT Reviewed; 277 AA.
AC P13019;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bleomycin hydrolase;
DE Short=BH;
DE Short=BLM hydrolase;
DE Short=BMH;
DE EC=3.4.22.40;
DE Flags: Fragment;
GN Name=BLMH;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-48.
RC TISSUE=Lung;
RX PubMed=2477059; DOI=10.1021/bi00442a003;
RA Sebti S.M., Mignano J.E., Jani J.P., Srimatkandada S., Lazo J.S.;
RT "Bleomycin hydrolase: molecular cloning, sequencing, and biochemical
RT studies reveal membership in the cysteine proteinase family.";
RL Biochemistry 28:6544-6548(1989).
CC -!- FUNCTION: The normal physiological role of BLM hydrolase is unknown,
CC but it catalyzes the inactivation of the antitumor drug BLM (a
CC glycopeptide) by hydrolyzing the carboxamide bond of its B-
CC aminoalaninamide moiety thus protecting normal and malignant cells from
CC BLM toxicity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
CC hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
CC shows general aminopeptidase activity. The specificity varies
CC somewhat with source, but amino acid arylamides of Met, Leu and Ala
CC are preferred.; EC=3.4.22.40;
CC -!- ACTIVITY REGULATION: Strongly inhibited by leupeptin, puromycin, NEM,
CC and divalent cations.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with NUDT12 (via ANK
CC repeats) (By similarity). {ECO:0000250|UniProtKB:Q13867}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13867}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q13867}. Note=Co-localizes
CC with NUDT12 in the cytoplasmic granules.
CC {ECO:0000250|UniProtKB:Q13867}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; J02866; AAA31171.1; -; mRNA.
DR PIR; A32972; A32972.
DR AlphaFoldDB; P13019; -.
DR SMR; P13019; -.
DR STRING; 9986.ENSOCUP00000003162; -.
DR MEROPS; C01.084; -.
DR PRIDE; P13019; -.
DR eggNOG; KOG4128; Eukaryota.
DR InParanoid; P13019; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR004134; Peptidase_C1B.
DR PANTHER; PTHR10363; PTHR10363; 1.
DR Pfam; PF03051; Peptidase_C1_2; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome; Thiol protease.
FT CHAIN <1..>277
FT /note="Bleomycin hydrolase"
FT /id="PRO_0000050552"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088,
FT ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000255|PROSITE-
FT ProRule:PRU10090"
FT NON_TER 1
FT NON_TER 277
SQ SEQUENCE 277 AA; 32579 MW; F22745EC44EA5CE3 CRC64;
DPQFVLAQNV GTHHDLLDIC LRRATVQGAQ HVFQHVVPQE GKPVTNQKSS GRCWIFSCLN
VMRLPFMKKL NIEEFEFSQS YVFFWDKVER CYFFLNAFVD TAQKKEPEDG RLVQYLLMNP
TNDGGQWDML VNIIEKYGVV PKKCFPESHT TEASRRMNDI LNHKMREFCI RLRNMVHSGA
TKAEISATED TMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP LEFYRQHVKP
LFNMEDKICF VNDPRPQHKY NRLYTVDYLS NMVGGRK
