ID MITOS_HUMAN Reviewed; 735 AA. AC Q9NUT2; A5D8W3; B2RBL8; B3KND2; B4DG02; G3XAP3; O95787; Q53GM0; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 3. DT 24-JUL-2024, entry version 208. 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:25944712}; DE Short=ABCB8 {ECO:0000303|PubMed:25944712}; DE AltName: Full=Mitochondrial ATP-binding cassette 1 {ECO:0000303|PubMed:9878413}; DE Short=M-ABC1 {ECO:0000303|PubMed:9878413}; DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000303|PubMed:31435016}; DE Short=MITOSUR {ECO:0000303|PubMed:31435016}; DE Flags: Precursor; GN Name=ABCB8 {ECO:0000303|PubMed:25944712, ECO:0000312|HGNC:HGNC:49}; GN Synonyms=MABC1 {ECO:0000303|PubMed:9878413}, GN MITOSUR {ECO:0000303|PubMed:31435016}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS. RX PubMed=9878413; DOI=10.1006/jmbi.1998.2259; RA Hogue D.L., Liu L., Ling V.; RT "Identification and characterization of a mammalian mitochondrial ATP- RT binding cassette membrane protein."; RL J. Mol. Biol. 285:379-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5). RC TISSUE=Amygdala, Placenta, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). 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 [7] RP SUBCELLULAR LOCATION, AND TRANSIT PEPTIDE CLEAVAGE SITE. RX PubMed=16259955; DOI=10.1016/j.bbrc.2005.10.070; RA Ardehali H., Xue T., Dong P., Machamer C.; RT "Targeting of the mitochondrial membrane proteins to the cell surface for RT functional studies."; RL Biochem. Biophys. Res. Commun. 338:1143-1151(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] RP VARIANT ILE-152. RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6; RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., RA Nakamura Y.; RT "Three hundred twenty-six genetic variations in genes encoding nine members RT of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese RT population."; RL J. Hum. Genet. 47:38-50(2002). RN [10] RP VARIANTS [LARGE SCALE ANALYSIS] THR-165 AND GLY-690. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [11] RP INDUCTION BY SP1. RX PubMed=21046154; DOI=10.1007/s00438-010-0586-8; RA Sachrajda I., Ratajewski M.; RT "Mithramycin A suppresses expression of the human melanoma-associated gene RT ABCB8."; RL Mol. Genet. Genomics 285:57-65(2011). RN [12] RP INTERACTION WITH C10ORF88. RX PubMed=25063848; DOI=10.1096/fj.14-254045; RA Yang X., Yang J., Li L., Sun L., Yi X., Han X., Si W., Yan R., Chen Z., RA Xie G., Li W., Shang Y., Liang J.; RT "PAAT, a novel ATPase and trans-regulator of mitochondrial ABC RT transporters, is critically involved in the maintenance of mitochondrial RT homeostasis."; RL FASEB J. 28:4821-4834(2014). RN [13] RP FUNCTION, AND INTERACTION WITH NRP1. RX PubMed=30623799; DOI=10.1016/j.isci.2018.12.005; RA Issitt T., Bosseboeuf E., De Winter N., Dufton N., Gestri G., Senatore V., RA Chikh A., Randi A.M., Raimondi C.; RT "Neuropilin-1 Controls Endothelial Homeostasis by Regulating Mitochondrial RT Function and Iron-Dependent Oxidative Stress."; RL IScience 11:205-223(2019). RN [14] RP MUTAGENESIS OF LYS-513, FUNCTION, SUBUNIT, TOPOLOGY, ACTIVITY REGULATION, RP AND SUBCELLULAR LOCATION. RX PubMed=31435016; DOI=10.1038/s41586-019-1498-3; RA Paggio A., Checchetto V., Campo A., Menabo R., Di Marco G., Di Lisa F., RA Szabo I., Rizzuto R., De Stefani D.; RT "Identification of an ATP-sensitive potassium channel in mitochondria."; RL Nature 572:609-613(2019). RN [15] {ECO:0007744|PDB:5OCH} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 110-714 IN COMPLEX WITH ADP. RA Faust B., Pike A.C.W., Shintre C.A., Quiqley A.M., Chu A., Barr A., RA Shrestha L., Mukhopadhyay S., Borkowska O., Chalk R., Burgess-Brown N.A., RA Arrowsmith C.H., Edwards A.M., Bountra C., Carpenter E.P.; RT "The crystal structure of human ABCB8 in an outward-facing state."; RL Submitted (JUN-2017) to the PDB data bank. CC -!- FUNCTION: ATP-binding subunit of the mitochondrial ATP-gated potassium CC channel (mitoK(ATP)) (PubMed:31435016). Together with pore-forming CC subunit CCDC51/MITOK of the mitoK(ATP) channel, mediates ATP-dependent CC potassium currents across the mitochondrial inner membrane CC (PubMed:31435016). An increase in ATP intracellular levels closes the CC channel, inhibiting K(+) transport, whereas a decrease in ATP levels CC enhances K(+) uptake in the mitochondrial matrix (PubMed:31435016). CC Plays a role in mitochondrial iron transport (PubMed:30623799). CC Required for maintenance of normal cardiac function, possibly by CC influencing mitochondrial iron export and regulating the maturation of CC cytosolic iron sulfur cluster-containing enzymes (By similarity). CC {ECO:0000250|UniProtKB:Q9CXJ4, ECO:0000269|PubMed:30623799, CC ECO:0000269|PubMed:31435016}. CC -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via CC ABCB8/MITOSUR subunit. {ECO:0000269|PubMed:31435016}. CC -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) is composed CC of 4 subunits of CCDC51/MITOK and 4 subunits of ABCB8/MITOSUR CC (Probable). Interacts with C10orf88/PAAT (PubMed:25063848). Interacts CC with NRP1; NRP1 regulates ABCB8/MITOSUR protein levels in mitochondria CC (PubMed:30623799). {ECO:0000269|PubMed:25063848, CC ECO:0000269|PubMed:30623799, ECO:0000305|PubMed:31435016}. CC -!- INTERACTION: CC Q9NUT2; Q96ER9: CCDC51; NbExp=2; IntAct=EBI-722515, EBI-11926384; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:16259955, ECO:0000269|PubMed:31435016}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Long; CC IsoId=Q9NUT2-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q9NUT2-2; Sequence=VSP_000026; CC Name=3; CC IsoId=Q9NUT2-3; Sequence=VSP_000026, VSP_055297; CC Name=4; CC IsoId=Q9NUT2-4; Sequence=VSP_056745; CC Name=5; CC IsoId=Q9NUT2-5; Sequence=VSP_056744; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: SP1 transcription factor binds to the ABCB8 core promoter CC region, possibly regulating its transcription. CC {ECO:0000269|PubMed:21046154, ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; 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; AF047690; AAD15748.1; -; mRNA. DR EMBL; AK002018; BAA92038.1; -; mRNA. DR EMBL; AK024401; BAG51294.1; -; mRNA. DR EMBL; AK222911; BAD96631.1; -; mRNA. DR EMBL; AK294344; BAG57613.1; -; mRNA. DR EMBL; AK314721; BAG37265.1; -; mRNA. DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471173; EAW54057.1; -; Genomic_DNA. DR EMBL; CH471173; EAW54061.1; -; Genomic_DNA. DR EMBL; CH471173; EAW54062.1; -; Genomic_DNA. DR EMBL; BC141814; AAI41815.1; -; mRNA. DR EMBL; BC141836; AAI41837.1; -; mRNA. DR EMBL; BC151235; AAI51236.1; -; mRNA. DR CCDS; CCDS5913.1; -. [Q9NUT2-2] DR CCDS; CCDS64798.1; -. [Q9NUT2-4] DR CCDS; CCDS64799.1; -. [Q9NUT2-1] DR CCDS; CCDS64800.1; -. [Q9NUT2-3] DR RefSeq; NP_001269220.1; NM_001282291.1. [Q9NUT2-1] DR RefSeq; NP_001269221.1; NM_001282292.1. [Q9NUT2-3] DR RefSeq; NP_001269222.1; NM_001282293.1. [Q9NUT2-4] DR RefSeq; NP_009119.2; NM_007188.4. [Q9NUT2-2] DR PDB; 5OCH; X-ray; 3.40 A; A/B/C/D/E/F/G/H=110-714. DR PDB; 7EHL; EM; -; A/B=58-735. DR PDBsum; 5OCH; -. DR PDBsum; 7EHL; -. DR AlphaFoldDB; Q9NUT2; -. DR EMDB; EMD-31142; -. DR SMR; Q9NUT2; -. DR BioGRID; 116364; 66. DR ComplexPortal; CPX-6083; MITOK-MITOSUR mitochondrial potassium channel complex. DR IntAct; Q9NUT2; 23. DR MINT; Q9NUT2; -. DR STRING; 9606.ENSP00000297504; -. DR DrugBank; DB00997; Doxorubicin. DR TCDB; 3.A.1.201.22; the atp-binding cassette (abc) superfamily. DR GlyGen; Q9NUT2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NUT2; -. DR PhosphoSitePlus; Q9NUT2; -. DR SwissPalm; Q9NUT2; -. DR BioMuta; ABCB8; -. DR DMDM; 143811358; -. DR jPOST; Q9NUT2; -. DR MassIVE; Q9NUT2; -. DR PaxDb; 9606-ENSP00000297504; -. DR PeptideAtlas; Q9NUT2; -. DR ProteomicsDB; 33804; -. DR ProteomicsDB; 719; -. DR ProteomicsDB; 82718; -. [Q9NUT2-1] DR ProteomicsDB; 82719; -. [Q9NUT2-2] DR Pumba; Q9NUT2; -. DR Antibodypedia; 32942; 193 antibodies from 28 providers. DR DNASU; 11194; -. DR Ensembl; ENST00000297504.10; ENSP00000297504.6; ENSG00000197150.13. [Q9NUT2-1] DR Ensembl; ENST00000358849.9; ENSP00000351717.4; ENSG00000197150.13. [Q9NUT2-2] DR Ensembl; ENST00000498578.5; ENSP00000418271.1; ENSG00000197150.13. [Q9NUT2-3] DR Ensembl; ENST00000542328.5; ENSP00000438776.1; ENSG00000197150.13. [Q9NUT2-4] DR GeneID; 11194; -. DR KEGG; hsa:11194; -. DR MANE-Select; ENST00000358849.9; ENSP00000351717.4; NM_007188.5; NP_009119.2. [Q9NUT2-2] DR UCSC; uc003wik.6; human. [Q9NUT2-1] DR AGR; HGNC:49; -. DR CTD; 11194; -. DR DisGeNET; 11194; -. DR GeneCards; ABCB8; -. DR HGNC; HGNC:49; ABCB8. DR HPA; ENSG00000197150; Low tissue specificity. DR MIM; 605464; gene. DR neXtProt; NX_Q9NUT2; -. DR OpenTargets; ENSG00000197150; -. DR PharmGKB; PA24390; -. DR VEuPathDB; HostDB:ENSG00000197150; -. DR eggNOG; KOG0058; Eukaryota. DR GeneTree; ENSGT00940000159126; -. DR HOGENOM; CLU_000604_84_3_1; -. DR InParanoid; Q9NUT2; -. DR OMA; MTWLGER; -. DR OrthoDB; 5487044at2759; -. DR PhylomeDB; Q9NUT2; -. DR TreeFam; TF105196; -. DR BRENDA; 7.4.2.5; 2681. DR PathwayCommons; Q9NUT2; -. DR Reactome; R-HSA-1369007; Mitochondrial ABC transporters. DR SignaLink; Q9NUT2; -. DR BioGRID-ORCS; 11194; 13 hits in 1163 CRISPR screens. DR ChiTaRS; ABCB8; human. DR GeneWiki; ABCB8; -. DR GenomeRNAi; 11194; -. DR Pharos; Q9NUT2; Tbio. DR PRO; PR:Q9NUT2; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9NUT2; Protein. DR Bgee; ENSG00000197150; Expressed in pancreatic ductal cell and 127 other cell types or tissues. DR ExpressionAtlas; Q9NUT2; baseline and differential. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:ProtInc. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0031966; C:mitochondrial membrane; IDA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0006884; P:cell volume homeostasis; IDA:ComplexPortal. DR GO; GO:0140141; P:mitochondrial potassium ion transmembrane transport; IDA:ComplexPortal. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd18574; ABC_6TM_ABCB8_like; 1. DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1. DR PANTHER; PTHR24221:SF643; MITOCHONDRIAL POTASSIUM CHANNEL ATP-BINDING SUBUNIT; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3D-structure; Alternative splicing; ATP-binding; Ion transport; Membrane; KW Mitochondrion; 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..735 FT /note="Mitochondrial potassium channel ATP-binding subunit" FT /evidence="ECO:0000255" FT /id="PRO_0000000251" FT TOPO_DOM 26..144 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:31435016" FT TRANSMEM 145..165 FT /note="Helical" FT /evidence="ECO:0000255, ECO:0000255|PROSITE- FT ProRule:PRU00441" FT TOPO_DOM 166..195 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:31435016" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255, ECO:0000255|PROSITE- FT ProRule:PRU00441" FT TOPO_DOM 217..295 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:31435016" FT TRANSMEM 296..316 FT /note="Helical" FT /evidence="ECO:0000255, ECO:0000255|PROSITE- FT ProRule:PRU00441" FT TOPO_DOM 317..735 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:31435016" FT DOMAIN 150..437 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 472..709 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 712..735 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 507..514 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434, FT ECO:0000269|Ref.15, ECO:0007744|PDB:5OCH" FT VAR_SEQ 1..187 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056744" FT VAR_SEQ 1..153 FT /note="MLVHLFRVGIRGGPFPGRLLPPLRFQTFSAVRNTWRNGKTGQLHKAEGEYSD FT GYRSSSLLRAVAHLRSQLWAHLPRAPLAPRWSPSAWCWVGGALLGPMVLSKHPHLCLVA FT LCEAEEAPPASSTPHVVGSRFNWKLFWQFLHPHLLVLGVAVV -> MRVKLLLPAAPVL FT PRQHAGAFISGRDSGWPIPRQAATAPPLPDILSCQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056745" FT VAR_SEQ 33..49 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9878413, FT ECO:0000303|Ref.3" FT /id="VSP_000026" FT VAR_SEQ 665..689 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055297" FT VARIANT 152 FT /note="V -> I (in dbSNP:rs4148844)" FT /evidence="ECO:0000269|PubMed:11829140" FT /id="VAR_013331" FT VARIANT 165 FT /note="I -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035733" FT VARIANT 690 FT /note="A -> G (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035734" FT MUTAGEN 512..513 FT /note="GK->AR: Renders the protein unstable." FT /evidence="ECO:0000269|PubMed:9878413" FT MUTAGEN 513 FT /note="K->A: Abolish binding to ATP." FT /evidence="ECO:0000269|PubMed:31435016" FT CONFLICT 174 FT /note="E -> K (in Ref. 1; AAD15748)" FT /evidence="ECO:0000305" FT CONFLICT 239 FT /note="D -> N (in Ref. 1; AAD15748)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="T -> S (in Ref. 1; AAD15748)" FT /evidence="ECO:0000305" FT CONFLICT 299 FT /note="M -> T (in Ref. 2; BAG57613)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="Q -> H (in Ref. 1; AAD15748)" FT /evidence="ECO:0000305" FT CONFLICT 347 FT /note="F -> L (in Ref. 1; AAD15748)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="R -> H (in Ref. 2; BAA92038)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="F -> Y (in Ref. 2; BAG57613)" FT /evidence="ECO:0000305" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 142..144 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 145..171 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 190..237 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 240..245 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 248..279 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 281..287 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 291..309 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 316..339 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 341..346 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 350..395 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 408..430 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 432..449 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 465..467 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 472..480 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 482..497 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 502..507 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 513..520 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 527..533 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 538..540 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 543..549 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 551..554 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 562..564 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 565..569 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 578..587 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 591..594 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 597..599 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 604..610 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 614..626 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 631..637 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 644..657 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 658..660 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:5OCH" FT TURN 670..672 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 673..675 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 676..683 FT /evidence="ECO:0007829|PDB:5OCH" FT STRAND 686..691 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 693..698 FT /evidence="ECO:0007829|PDB:5OCH" FT HELIX 702..714 FT /evidence="ECO:0007829|PDB:5OCH" SQ SEQUENCE 735 AA; 79989 MW; B7E02B063E6C6F3B CRC64; MLVHLFRVGI RGGPFPGRLL PPLRFQTFSA VRNTWRNGKT GQLHKAEGEY SDGYRSSSLL RAVAHLRSQL WAHLPRAPLA PRWSPSAWCW VGGALLGPMV LSKHPHLCLV ALCEAEEAPP ASSTPHVVGS RFNWKLFWQF LHPHLLVLGV AVVLALGAAL VNVQIPLLLG QLVEVVAKYT RDHVGSFMTE SQNLSTHLLI LYGVQGLLTF GYLVLLSHVG ERMAVDMRRA LFSSLLRQDI TFFDANKTGQ LVSRLTTDVQ EFKSSFKLVI SQGLRSCTQV AGCLVSLSML STRLTLLLMV ATPALMGVGT LMGSGLRKLS RQCQEQIARA MGVADEALGN VRTVRAFAME QREEERYGAE LEACRCRAEE LGRGIALFQG LSNIAFNCMV LGTLFIGGSL VAGQQLTGGD LMSFLVASQT VQRSMANLSV LFGQVVRGLS AGARVFEYMA LNPCIPLSGG CCVPKEQLRG SVTFQNVCFS YPCRPGFEVL KDFTLTLPPG KIVALVGQSG GGKTTVASLL ERFYDPTAGV VMLDGRDLRT LDPSWLRGQV VGFISQEPVL FGTTIMENIR FGKLEASDEE VYTAAREANA HEFITSFPEG YNTVVGERGT TLSGGQKQRL AIARALIKQP TVLILDEATS ALDAESERVV QEALDRASAG RTVLVIAHRL STVRGAHCIV VMADGRVWEA GTHEELLKKG GLYAELIRRQ ALDAPRTAAP PPKKPEGPRS HQHKS //