ID   BLMH_CHICK              Reviewed;         455 AA.
AC   P87362;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Bleomycin hydrolase;
DE            Short=BH;
DE            Short=BLM hydrolase;
DE            Short=BMH;
DE            EC=3.4.22.40;
DE   AltName: Full=Aminopeptidase H;
GN   Name=BLMH;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX   PubMed=9151954; DOI=10.1111/j.1432-1033.1997.t01-1-00283.x;
RA   Adachi H., Tsujimoto M., Fukasawa M., Sato Y., Arai H., Inoue K.,
RA   Nishimura T.;
RT   "cDNA cloning and expression of chicken aminopeptidase H, possessing
RT   endopeptidase as well as aminopeptidase activity.";
RL   Eur. J. Biochem. 245:283-288(1997).
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: Homooctamer. {ECO:0000269|PubMed:9151954}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13867}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB001322; BAA19236.1; -; mRNA.
DR   RefSeq; NP_990435.1; NM_205104.1.
DR   AlphaFoldDB; P87362; -.
DR   SMR; P87362; -.
DR   STRING; 9031.ENSGALP00000006762; -.
DR   MEROPS; C01.084; -.
DR   PaxDb; P87362; -.
DR   Ensembl; ENSGALT00000006773; ENSGALP00000006762; ENSGALG00000004259.
DR   GeneID; 395996; -.
DR   KEGG; gga:395996; -.
DR   CTD; 642; -.
DR   VEuPathDB; HostDB:geneid_395996; -.
DR   eggNOG; KOG4128; Eukaryota.
DR   GeneTree; ENSGT00390000001735; -.
DR   HOGENOM; CLU_038600_0_0_1; -.
DR   InParanoid; P87362; -.
DR   OMA; WDMIVNL; -.
DR   OrthoDB; 649145at2759; -.
DR   PhylomeDB; P87362; -.
DR   TreeFam; TF323372; -.
DR   Reactome; R-GGA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P87362; -.
DR   Proteomes; UP000000539; Chromosome 19.
DR   Bgee; ENSGALG00000004259; Expressed in muscle tissue and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
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   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Thiol protease.
FT   CHAIN           1..455
FT                   /note="Bleomycin hydrolase"
FT                   /id="PRO_0000050549"
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"
SQ   SEQUENCE   455 AA;  52690 MW;  0C79F43E40DFFE0F CRC64;
     MNAHGLSTEK AAAFTRRLRA EPQFLLAQNV ATCSDPLEVC LQRQVVQDTI QVFQHAVPAE
     GKPVTNQKNS GRCWIFSCLN AMRLPFMKKY NIEEFEFSQS YLFFWDKVER CYYFLNAFVE
     TAQKKEPIDG RLVQFLLTNP TNDGGQWDML VNIVEKYGVV PKKYFPESHT TEATRRMNEI
     LNHKMREYCL RLRNMVATGT NKEELCAAMD TMIEEVFRIV STCLGNPPET FCWEFRDKEK
     NYHKFGPMTP VQFYNEHVKP YFNMEDKVCL VNDPRPQNPY CQLYTVEYLG NMAGGRKTLY
     NNQPIEVLKK LAATSIKDGE AVWFGCDVAK HFYSKLGIND LNIFNHELVF GVSVKNMNKA
     ERLIFGDSLM THAMVLTAVS EKDGQEDCYE KWRVENSWGE DRGNKGYLIM TDDWFSEYVY
     EVVVDKKYVP EDVLAVMEQE PIVLPAWDPM GALAK