MITOS_MOUSE
ID MITOS_MOUSE Reviewed; 717 AA.
AC Q9CXJ4; Q8C695; Q8C7W4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitochondrial potassium channel ATP-binding subunit {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 8, mitochondrial {ECO:0000303|PubMed:22375032};
DE Short=ABCB8 {ECO:0000303|PubMed:22375032};
DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000250|UniProtKB:Q9NUT2};
DE Short=MITOSUR {ECO:0000250|UniProtKB:Q9NUT2};
DE Flags: Precursor;
GN Name=Abcb8 {ECO:0000303|PubMed:22375032, ECO:0000312|MGI:MGI:1351667};
GN Synonyms=Mitosur {ECO:0000250|UniProtKB:Q9NUT2};
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; TISSUE=Head, Pituitary, and Skin;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22375032; DOI=10.1073/pnas.1119338109;
RA Ichikawa Y., Bayeva M., Ghanefar M., Potini V., Sun L., Mutharasan R.K.,
RA Wu R., Khechaduri A., Jairaj Naik T., Ardehali H.;
RT "Disruption of ATP-binding cassette B8 in mice leads to cardiomyopathy
RT through a decrease in mitochondrial iron export.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4152-4157(2012).
CC -!- FUNCTION: ATP-binding subunit of the mitochondrial potassium channel
CC located in the mitochondrial inner membrane (By similarity). Together
CC with CCDC51/MITOK, forms a protein complex localized in the
CC mitochondria that mediates ATP-dependent potassium currents across the
CC inner membrane (that is, mitoK(ATP) channel) (By similarity). Plays a
CC role in mitochondrial iron transport (PubMed:22375032). Required for
CC maintenance of normal cardiac function, possibly by influencing
CC mitochondrial iron export and regulating the maturation of cytosolic
CC iron sulfur cluster-containing enzymes (PubMed:22375032).
CC {ECO:0000250|UniProtKB:Q9NUT2, ECO:0000269|PubMed:22375032}.
CC -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via
CC ABCB8/MITOSUR subunit. {ECO:0000250|UniProtKB:Q9NUT2}.
CC -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) is composed
CC of 4 subunits of CCDC51/MITOK and 4 subunits of ABCB8/MITOSUR (By
CC similarity). Interacts with PAAT (By similarity). Interacts with NRP1;
CC NRP1 regulates ABCB8/MITOSUR protein levels in mitochondria (By
CC similarity). {ECO:0000250|UniProtKB:Q9NUT2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9NUT2}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in heart results in a severe
CC cardiomyopathy and mitochondrial iron accumulation.
CC {ECO:0000269|PubMed:22375032}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; AK014319; BAB29270.1; -; mRNA.
DR EMBL; AK030624; BAC27052.1; -; mRNA.
DR EMBL; AK049152; BAC33571.1; -; mRNA.
DR EMBL; AK076315; BAC36297.1; -; mRNA.
DR EMBL; AK166704; BAE38958.1; -; mRNA.
DR EMBL; BC015301; AAH15301.1; -; mRNA.
DR CCDS; CCDS19118.1; -.
DR RefSeq; NP_083296.2; NM_029020.2.
DR RefSeq; XP_006535875.1; XM_006535812.1.
DR AlphaFoldDB; Q9CXJ4; -.
DR SMR; Q9CXJ4; -.
DR ComplexPortal; CPX-6084; MITOK-MITOSUR mitochondrial potassium channel complex.
DR IntAct; Q9CXJ4; 1.
DR STRING; 10090.ENSMUSP00000110729; -.
DR iPTMnet; Q9CXJ4; -.
DR PhosphoSitePlus; Q9CXJ4; -.
DR SwissPalm; Q9CXJ4; -.
DR EPD; Q9CXJ4; -.
DR jPOST; Q9CXJ4; -.
DR MaxQB; Q9CXJ4; -.
DR PaxDb; Q9CXJ4; -.
DR PeptideAtlas; Q9CXJ4; -.
DR PRIDE; Q9CXJ4; -.
DR ProteomicsDB; 285953; -.
DR Antibodypedia; 32942; 194 antibodies from 28 providers.
DR DNASU; 74610; -.
DR Ensembl; ENSMUST00000073076; ENSMUSP00000072826; ENSMUSG00000028973.
DR Ensembl; ENSMUST00000115077; ENSMUSP00000110729; ENSMUSG00000028973.
DR GeneID; 74610; -.
DR KEGG; mmu:74610; -.
DR UCSC; uc008wrh.1; mouse.
DR CTD; 11194; -.
DR MGI; MGI:1351667; Abcb8.
DR VEuPathDB; HostDB:ENSMUSG00000028973; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159126; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q9CXJ4; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q9CXJ4; -.
DR TreeFam; TF105196; -.
DR Reactome; R-MMU-1369007; Mitochondrial ABC transporters.
DR BioGRID-ORCS; 74610; 1 hit in 56 CRISPR screens.
DR ChiTaRS; Abcb8; mouse.
DR PRO; PR:Q9CXJ4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXJ4; protein.
DR Bgee; ENSMUSG00000028973; Expressed in spermatocyte and 241 other tissues.
DR ExpressionAtlas; Q9CXJ4; baseline and differential.
DR Genevisible; Q9CXJ4; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; IPI:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; ISO:MGI.
DR GO; GO:0140141; P:mitochondrial potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Potassium;
KW Potassium transport; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..717
FT /note="Mitochondrial potassium channel ATP-binding subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000356233"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 132..419
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 454..691
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 695..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 101
FT /note="S -> Y (in Ref. 1; BAC33571)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="I -> M (in Ref. 1; BAC36297)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> L (in Ref. 1; BAC36297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 78000 MW; E573D4276B9658EB CRC64;
MLVHLFRFGI RGGPVPGWSL QSLRFQTFSA ARSSDDRLSS HLLRTVAQLR VQLRAHLPRA
PPASHWSPSA WCWVGGTLVV PAVLWQHPRL CLIALCEAKE SPPAQPTRAP ELRFNWKLFW
HFLHPHLLAL GAAIVLALGA ALVNVQIPLL LGQLVEIVAK YTRDHMGSFV SESRKLSVQL
LLLYGVQGLL TFGYLVLLSH IGERMAMDMR KALFSSLLRQ DIAFFDAKKT GQLVSRLTTD
VQEFKSSFKL VISQGLRSCT QVIGSLVSLS MLSPRLTLML AVVTPALMGV GTLMGSGLRK
LSRQCQEQIA RATGVADEAL GNVRTVRAFA MEKREEERYQ AELESCCCKA EELGRGIALF
QGLSNIAFNC MVLGTLFIGG SLVAGQQLKG GDLMSFLVAS QTVQRSMASL SVLFGQVVRG
LSAGARVFEY MALSPVIPLT GGYCIPNKDI RGSITFQNVT FSYPCRPGFN VLKDFTLKLP
SGKIVALVGQ SGGGKTTVAS LLERFYDPEA GSVTLDGHDL RTLNPSWLRG QVIGFISQEP
VLFATTIMEN IRFGKLDASD EEVYTAAREA NAHEFISSFP DGYSTVVGER GTTLSGGQKQ
RLAIARALIK QPTVLILDEA TSALDAESER VVQEALDRAS AGRTVLVIAH RLSTVRAAHS
IIVMANGQVC EAGTHEELLK KGGLYSELIR RQTLDASLTS TPPAEKPEDP KSCQSKA
