ID   ALKB7_BOVIN             Reviewed;         221 AA.
AC   Q2M2S8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial;
DE            EC=1.14.11.-;
DE   AltName: Full=Alkylated DNA repair protein alkB homolog 7;
DE   Flags: Precursor;
GN   Name=ALKBH7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as protein hydroxylase; can catalyze auto-
CC       hydroxylation at Leu-110 (in vitro), but this activity may be due to
CC       the absence of the true substrate. Required to induce programmed
CC       necrosis in response to DNA damage caused by cytotoxic alkylating
CC       agents. Acts by triggering the collapse of mitochondrial membrane
CC       potential and loss of mitochondrial function that leads to energy
CC       depletion and cell death. ALKBH7-mediated necrosis is probably required
CC       to prevent the accumulation of cells with DNA damage. Does not display
CC       DNA demethylase activity (By similarity). Involved in fatty acid
CC       metabolism (By similarity). {ECO:0000250|UniProtKB:Q9BT30,
CC       ECO:0000250|UniProtKB:Q9D6Z0}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9BT30};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9BT30};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9BT30}.
CC   -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR   EMBL; BC111665; AAI11666.1; -; mRNA.
DR   RefSeq; NP_001039867.1; NM_001046402.2.
DR   AlphaFoldDB; Q2M2S8; -.
DR   SMR; Q2M2S8; -.
DR   STRING; 9913.ENSBTAP00000035795; -.
DR   PaxDb; Q2M2S8; -.
DR   PRIDE; Q2M2S8; -.
DR   Ensembl; ENSBTAT00000035929; ENSBTAP00000035795; ENSBTAG00000025540.
DR   GeneID; 535305; -.
DR   KEGG; bta:535305; -.
DR   CTD; 84266; -.
DR   VEuPathDB; HostDB:ENSBTAG00000025540; -.
DR   VGNC; VGNC:25838; ALKBH7.
DR   eggNOG; KOG4176; Eukaryota.
DR   GeneTree; ENSGT00390000014585; -.
DR   HOGENOM; CLU_092162_1_0_1; -.
DR   InParanoid; Q2M2S8; -.
DR   OMA; VEPHMKR; -.
DR   OrthoDB; 1181737at2759; -.
DR   TreeFam; TF314197; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000025540; Expressed in tongue muscle and 105 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0010883; P:regulation of lipid storage; ISS:UniProtKB.
DR   GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; ISS:UniProtKB.
DR   Gene3D; 2.60.120.590; -; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032870; ALKBH7.
DR   PANTHER; PTHR21052; PTHR21052; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Mitochondrion; Necrosis; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..221
FT                   /note="Alpha-ketoglutarate-dependent dioxygenase alkB
FT                   homolog 7, mitochondrial"
FT                   /id="PRO_0000239287"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
FT   BINDING         165
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
FT   BINDING         197..199
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
FT   BINDING         203
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT30"
SQ   SEQUENCE   221 AA;  24589 MW;  E55590CB6B5D30D5 CRC64;
     MAGGGQVVLR TLSQQGWVRG SGAAVLSRLQ DAAVVRPGFL STAEEETLSR ELEPELRRRR
     YEYDHWDAAI HGFRETEKSR WSEASRAILR RVQAAAFGPG QTLLSSVHVL DLEPQGYIKP
     HVDSIKFCGS TIAGLSLLSP SVMRLVHTQE PGEWLELLLE PGSLYILRGS ARYDFSHEIL
     RDEESFFGER RIPRGRRISV ICRSLPEGMG PGEPGQLPPA C