BLMH_MOUSE
ID BLMH_MOUSE Reviewed; 455 AA.
AC Q8R016; Q3TJR8; Q8BLZ4; Q8BZH9; Q8C111; Q8CID9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Bleomycin hydrolase;
DE Short=BH;
DE Short=BLM hydrolase;
DE Short=BMH;
DE EC=3.4.22.40;
GN Name=Blmh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Bone marrow, Embryonic spinal ganglion, Eye, Placenta, and
RC Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, Mammary gland, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. {ECO:0000250}.
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 -!- 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}.
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DR EMBL; AK035228; BAC28989.1; -; mRNA.
DR EMBL; AK040799; BAC30706.1; -; mRNA.
DR EMBL; AK051441; BAC34639.1; -; mRNA.
DR EMBL; AK053872; BAC35568.1; -; mRNA.
DR EMBL; AK150438; BAE29560.1; -; mRNA.
DR EMBL; AK167325; BAE39427.1; -; mRNA.
DR EMBL; AL603842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024090; AAH24090.1; -; mRNA.
DR EMBL; BC027037; AAH27037.1; -; mRNA.
DR EMBL; BC027362; AAH27362.1; -; mRNA.
DR EMBL; BC027403; AAH27403.1; -; mRNA.
DR CCDS; CCDS25073.1; -.
DR RefSeq; NP_848760.1; NM_178645.4.
DR AlphaFoldDB; Q8R016; -.
DR SMR; Q8R016; -.
DR BioGRID; 222434; 12.
DR STRING; 10090.ENSMUSP00000021197; -.
DR MEROPS; C01.084; -.
DR iPTMnet; Q8R016; -.
DR PhosphoSitePlus; Q8R016; -.
DR SwissPalm; Q8R016; -.
DR CPTAC; non-CPTAC-3322; -.
DR EPD; Q8R016; -.
DR jPOST; Q8R016; -.
DR MaxQB; Q8R016; -.
DR PaxDb; Q8R016; -.
DR PeptideAtlas; Q8R016; -.
DR PRIDE; Q8R016; -.
DR ProteomicsDB; 273499; -.
DR Antibodypedia; 15119; 271 antibodies from 32 providers.
DR DNASU; 104184; -.
DR Ensembl; ENSMUST00000021197; ENSMUSP00000021197; ENSMUSG00000020840.
DR GeneID; 104184; -.
DR KEGG; mmu:104184; -.
DR UCSC; uc007kge.2; mouse.
DR CTD; 642; -.
DR MGI; MGI:1345186; Blmh.
DR VEuPathDB; HostDB:ENSMUSG00000020840; -.
DR eggNOG; KOG4128; Eukaryota.
DR GeneTree; ENSGT00390000001735; -.
DR HOGENOM; CLU_038600_0_0_1; -.
DR InParanoid; Q8R016; -.
DR OMA; WDMIVNL; -.
DR OrthoDB; 649145at2759; -.
DR PhylomeDB; Q8R016; -.
DR TreeFam; TF323372; -.
DR BRENDA; 3.4.22.40; 3474.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 104184; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Blmh; mouse.
DR PRO; PR:Q8R016; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R016; protein.
DR Bgee; ENSMUSG00000020840; Expressed in bone fossa and 268 other tissues.
DR ExpressionAtlas; Q8R016; baseline and differential.
DR Genevisible; Q8R016; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR GO; GO:0043418; P:homocysteine catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR CDD; cd00585; Peptidase_C1B; 1.
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 PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Thiol protease.
FT CHAIN 1..455
FT /note="Bleomycin hydrolase"
FT /id="PRO_0000050551"
FT ACT_SITE 73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P70645"
FT MOD_RES 391
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 16
FT /note="Q -> K (in Ref. 1; BAC28989)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="V -> A (in Ref. 3; AAH24090)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="K -> R (in Ref. 1; BAC30706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 52511 MW; 032F3B1DA1AD5063 CRC64;
MNNAGLNSEK VSALIQKLNS DPQFVLAQNV GTTHDLLDIC LRRATVQGAQ HVFQHVVPQE
GKPVTNQKSS GRCWIFSCLN VMRLPFMKKF NIEEFEFSQS YLFFWDKVER CYFFLNAFVD
TAQKKEPEDG RLVQYLLMNP TNDGGQWDML VNIVEKYGVV PKKCFPESHT TEATRRMNDI
LNHKMREFCI RLRNLVHSGA TKGEISSTQD AMMEEIFRVV CICLGNPPET FTWEYRDKDK
NYHKIGPITP LQFYKEHVKP LFNMEDKICF VNDPRPQHKY NKLYTVDYLS NMVGGRKTLY
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNGKLGLSD MNVYDHELVF GVSLKNMNKA
ERLAFGESLM THAMTFTAVS EKDNQEGTFV KWRVENSWGE DHGHKGYLCM TDEWFSEYVY
EVVVDKKHVP EEVLAVLEQE PIVLPAWDPM GALAE
