ALKB7_MOUSE
ID ALKB7_MOUSE Reviewed; 221 AA.
AC Q9D6Z0; Q8K1H3; Q9CY41; Q9D942;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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; Synonyms=Spata11;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, Pancreas, and Tongue;
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] OF 4-221 (ISOFORM 1).
RC TISSUE=Eye;
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, Heart, Kidney, Liver, 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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=23572141; DOI=10.1093/jmcb/mjt012;
RA Solberg A., Robertson A.B., Aronsen J.M., Rognmo O., Sjaastad I.,
RA Wisloff U., Klungland A.;
RT "Deletion of mouse Alkbh7 leads to obesity.";
RL J. Mol. Cell Biol. 5:194-203(2013).
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. {ECO:0000250|UniProtKB:Q9BT30,
CC ECO:0000269|PubMed:23572141}.
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:0000269|PubMed:23572141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6Z0-2; Sequence=VSP_019132;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23572141}.
CC -!- DISRUPTION PHENOTYPE: Increased body weight and body fat, a phenotype
CC amplified under high-fat diet. {ECO:0000269|PubMed:23572141}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK007380; BAB24999.1; -; mRNA.
DR EMBL; AK009812; BAB26517.1; -; mRNA.
DR EMBL; AK010930; BAB27274.1; -; mRNA.
DR EMBL; GL456179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029677; AAH29677.1; ALT_INIT; mRNA.
DR CCDS; CCDS28921.1; -. [Q9D6Z0-1]
DR CCDS; CCDS57105.1; -. [Q9D6Z0-2]
DR RefSeq; NP_079814.1; NM_025538.3. [Q9D6Z0-1]
DR RefSeq; NP_081648.1; NM_027372.1. [Q9D6Z0-2]
DR AlphaFoldDB; Q9D6Z0; -.
DR SMR; Q9D6Z0; -.
DR STRING; 10090.ENSMUSP00000002737; -.
DR EPD; Q9D6Z0; -.
DR MaxQB; Q9D6Z0; -.
DR PaxDb; Q9D6Z0; -.
DR PeptideAtlas; Q9D6Z0; -.
DR PRIDE; Q9D6Z0; -.
DR ProteomicsDB; 296097; -. [Q9D6Z0-1]
DR ProteomicsDB; 296098; -. [Q9D6Z0-2]
DR Antibodypedia; 42538; 81 antibodies from 22 providers.
DR Ensembl; ENSMUST00000002737; ENSMUSP00000002737; ENSMUSG00000002661. [Q9D6Z0-1]
DR Ensembl; ENSMUST00000074141; ENSMUSP00000073775; ENSMUSG00000002661. [Q9D6Z0-2]
DR GeneID; 66400; -.
DR KEGG; mmu:66400; -.
DR UCSC; uc008ddn.2; mouse. [Q9D6Z0-1]
DR UCSC; uc012avz.1; mouse. [Q9D6Z0-2]
DR CTD; 84266; -.
DR MGI; MGI:1913650; Alkbh7.
DR VEuPathDB; HostDB:ENSMUSG00000002661; -.
DR eggNOG; KOG4176; Eukaryota.
DR GeneTree; ENSGT00390000014585; -.
DR HOGENOM; CLU_092162_1_0_1; -.
DR InParanoid; Q9D6Z0; -.
DR OMA; VEPHMKR; -.
DR OrthoDB; 1181737at2759; -.
DR PhylomeDB; Q9D6Z0; -.
DR TreeFam; TF314197; -.
DR BioGRID-ORCS; 66400; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Alkbh7; mouse.
DR PRO; PR:Q9D6Z0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D6Z0; protein.
DR Bgee; ENSMUSG00000002661; Expressed in interventricular septum and 226 other tissues.
DR Genevisible; Q9D6Z0; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0010883; P:regulation of lipid storage; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Iron; Metal-binding; Mitochondrion;
KW Necrosis; Oxidoreductase; 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_0000239289"
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"
FT VAR_SEQ 69..126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019132"
FT CONFLICT 191
FT /note="R -> L (in Ref. 1; BAB24999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24970 MW; 7961509733692740 CRC64;
MAGSRRLAMR LLSGCAWVRG SDSAVLGRLR DEAVVHPGFL SQEEEDTLTR ELEPQLRRRR
YEYDHWDAAI HGFRETEKSC WSDASQVILQ RVRAAAFGPD QSLLSPVHVL DLEPRGYIKP
HVDSVKFCGS TIAGLSLLSP SVMKLVHTQE PEQWLELLLE PGSLYILRGS ARYDFSHEIL
RDEESFFGEH RVPRGRRISV ICRSLPEGMG PGRPEEPPPA C
