ID ABCC9_HUMAN Reviewed; 1549 AA. AC O60706; O60707; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 24-JAN-2024, entry version 206. DE RecName: Full=ATP-binding cassette sub-family C member 9; DE AltName: Full=Sulfonylurea receptor 2; GN Name=ABCC9; Synonyms=SUR2 {ECO:0000303|PubMed:31575858}; 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 [GENOMIC DNA] (ISOFORMS SUR2A AND SUR2B), AND REVIEW. RX PubMed=9457174; DOI=10.1152/physrev.1998.78.1.227; RA Aguilar-Bryan L., Clement J.P. IV, Gonzalez G., Kunjilwar K., Babenko A., RA Bryan J.; RT "Toward understanding the assembly and structure of KATP channels."; RL Physiol. Rev. 78:227-245(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP FUNCTION, AND SUBUNIT. RX PubMed=9831708; DOI=10.1161/01.res.83.11.1132; RA Babenko A.P., Gonzalez G., Aguilar-Bryan L., Bryan J.; RT "Reconstituted human cardiac KATP channels: functional identity with the RT native channels from the sarcolemma of human ventricular cells."; RL Circ. Res. 83:1132-1143(1998). RN [4] RP POSSIBLE FUNCTION IN REGULATION OF SLEEP DURATION. RX PubMed=22105623; DOI=10.1038/mp.2011.142; RA Allebrandt K.V., Amin N., Muller-Myhsok B., Esko T., Teder-Laving M., RA Azevedo R.V., Hayward C., van Mill J., Vogelzangs N., Green E.W., RA Melville S.A., Lichtner P., Wichmann H.E., Oostra B.A., Janssens A.C., RA Campbell H., Wilson J.F., Hicks A.A., Pramstaller P.P., Dogas Z., Rudan I., RA Merrow M., Penninx B., Kyriacou C.P., Metspalu A., van Duijn C.M., RA Meitinger T., Roenneberg T.; RT "A K(ATP) channel gene effect on sleep duration: from genome-wide RT association studies to function in Drosophila."; RL Mol. Psychiatry 18:122-132(2013). RN [5] RP VARIANT CMD1O THR-1513. RX PubMed=15034580; DOI=10.1038/ng1329; RA Bienengraeber M., Olson T.M., Selivanov V.A., Kathmann E.C., O'Cochlain F., RA Gao F., Karger A.B., Ballew J.D., Hodgson D.M., Zingman L.V., Pang Y.-P., RA Alekseev A.E., Terzic A.; RT "ABCC9 mutations identified in human dilated cardiomyopathy disrupt RT catalytic KATP channel gating."; RL Nat. Genet. 36:382-387(2004). RN [6] RP VARIANT ATFB12 ILE-1547, AND CHARACTERIZATION OF VARIANT ATFB12 ILE-1547. RX PubMed=17245405; DOI=10.1038/ncpcardio0792; RA Olson T.M., Alekseev A.E., Moreau C., Liu X.K., Zingman L.V., Miki T., RA Seino S., Asirvatham S.J., Jahangir A., Terzic A.; RT "KATP channel mutation confers risk for vein of Marshall adrenergic atrial RT fibrillation."; RL Nat. Clin. Pract. Cardiovasc. Med. 4:110-116(2007). RN [7] RP VARIANTS HTOCD VAL-478; TYR-1043; GLN-1154 AND TRP-1154. RX PubMed=22608503; DOI=10.1016/j.ajhg.2012.04.014; RA van Bon B.W., Gilissen C., Grange D.K., Hennekam R.C., Kayserili H., RA Engels H., Reutter H., Ostergaard J.R., Morava E., Tsiakas K., Isidor B., RA Le Merrer M., Eser M., Wieskamp N., de Vries P., Steehouwer M., RA Veltman J.A., Robertson S.P., Brunner H.G., de Vries B.B., Hoischen A.; RT "Cantu syndrome is caused by mutations in ABCC9."; RL Am. J. Hum. Genet. 90:1094-1101(2012). RN [8] RP VARIANTS HTOCD TYR-60; GLU-207; CYS-380; LEU-432; PRO-1020; SER-1039; RP TYR-1054; HIS-1116; CYS-1116; GLN-1154 AND TRP-1154, AND CHARACTERIZATION RP OF VARIANTS HTOCD LEU-432; HIS-1116 AND GLN-1154. RX PubMed=22610116; DOI=10.1038/ng.2324; RA Harakalova M., van Harssel J.J., Terhal P.A., van Lieshout S., Duran K., RA Renkens I., Amor D.J., Wilson L.C., Kirk E.P., Turner C.L., Shears D., RA Garcia-Minaur S., Lees M.M., Ross A., Venselaar H., Vriend G., Takanari H., RA Rook M.B., van der Heyden M.A., Asselbergs F.W., Breur H.M., Swinkels M.E., RA Scurr I.J., Smithson S.F., Knoers N.V., van der Smagt J.J., Nijman I.J., RA Kloosterman W.P., van Haelst M.M., van Haaften G., Cuppen E.; RT "Dominant missense mutations in ABCC9 cause Cantu syndrome."; RL Nat. Genet. 44:793-796(2012). RN [9] RP VARIANTS HTOCD LEU-432; VAL-478 AND TYR-1043, AND CHARACTERIZATION OF RP VARIANTS HTOCD LEU-432; VAL-478 AND TYR-1043. RX PubMed=26621776; DOI=10.1085/jgp.201511495; RA Cooper P.E., Sala-Rabanal M., Lee S.J., Nichols C.G.; RT "Differential mechanisms of Cantu syndrome-associated gain of function RT mutations in the ABCC9 (SUR2) subunit of the KATP channel."; RL J. Gen. Physiol. 146:527-540(2015). RN [10] RP VARIANT ARG-1160. RX PubMed=31303265; DOI=10.1016/j.ajhg.2019.06.007; RG DDD Study; RA Snijders Blok L., Kleefstra T., Venselaar H., Maas S., Kroes H.Y., RA Lachmeijer A.M.A., van Gassen K.L.I., Firth H.V., Tomkins S., Bodek S., RA Ounap K., Wojcik M.H., Cunniff C., Bergstrom K., Powis Z., Tang S., RA Shinde D.N., Au C., Iglesias A.D., Izumi K., Leonard J., Abou Tayoun A., RA Baker S.W., Tartaglia M., Niceta M., Dentici M.L., Okamoto N., Miyake N., RA Matsumoto N., Vitobello A., Faivre L., Philippe C., Gilissen C., Wiel L., RA Pfundt R., Deriziotis P., Brunner H.G., Fisher S.E.; RT "De Novo Variants Disturbing the Transactivation Capacity of POU3F3 Cause a RT Characteristic Neurodevelopmental Disorder."; RL Am. J. Hum. Genet. 105:403-412(2019). RN [11] RP INVOLVEMENT IN IDMYS. RX PubMed=31575858; DOI=10.1038/s41467-019-12428-7; RA Smeland M.F., McClenaghan C., Roessler H.I., Savelberg S., Hansen G.A.M., RA Hjellnes H., Arntzen K.A., Mueller K.I., Dybesland A.R., Harter T., RA Sala-Rabanal M., Emfinger C.H., Huang Y., Singareddy S.S., Gunn J., RA Wozniak D.F., Kovacs A., Massink M., Tessadori F., Kamel S.M., Bakkers J., RA Remedi M.S., Van Ghelue M., Nichols C.G., van Haaften G.; RT "ABCC9-related Intellectual disability Myopathy Syndrome is a KATP RT channelopathy with loss-of-function mutations in ABCC9."; RL Nat. Commun. 10:4457-4457(2019). CC -!- FUNCTION: Subunit of ATP-sensitive potassium channels (KATP). Can form CC cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms CC the channel pore while ABCC9 is required for activation and regulation. CC {ECO:0000269|PubMed:9831708}. CC -!- SUBUNIT: Interacts with KCNJ11. {ECO:0000269|PubMed:9831708}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=SUR2A; CC IsoId=O60706-1; Sequence=Displayed; CC Name=SUR2B; CC IsoId=O60706-2; Sequence=VSP_000058; CC -!- DISEASE: Cardiomyopathy, dilated, 1O (CMD1O) [MIM:608569]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:15034580}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Atrial fibrillation, familial, 12 (ATFB12) [MIM:614050]: A CC familial form of atrial fibrillation, a common sustained cardiac rhythm CC disturbance. Atrial fibrillation is characterized by disorganized CC atrial electrical activity and ineffective atrial contraction promoting CC blood stasis in the atria and reduces ventricular filling. It can CC result in palpitations, syncope, thromboembolic stroke, and congestive CC heart failure. {ECO:0000269|PubMed:17245405}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Hypertrichotic osteochondrodysplasia (HTOCD) [MIM:239850]: A CC rare disorder characterized by congenital hypertrichosis, neonatal CC macrosomia, a distinct osteochondrodysplasia, and cardiomegaly. The CC hypertrichosis leads to thick scalp hair, which extends onto the CC forehead, and a general increase in body hair. In addition, CC macrocephaly and coarse facial features, including a broad nasal CC bridge, epicanthal folds, a wide mouth, and full lips, can be CC suggestive of a storage disorder. About half of affected individuals CC are macrosomic and edematous at birth, whereas in childhood they CC usually have a muscular appearance with little subcutaneous fat. CC Thickened calvarium, narrow thorax, wide ribs, flattened or ovoid CC vertebral bodies, coxa valga, osteopenia, enlarged medullary canals, CC and metaphyseal widening of long bones have been reported. Cardiac CC manifestations such as patent ductus arteriosus, ventricular CC hypertrophy, pulmonary hypertension, and pericardial effusions are CC present in approximately 80% of cases. Motor development is usually CC delayed due to hypotonia. Most patients have a mild speech delay, and a CC small percentage have learning difficulties or intellectual disability. CC {ECO:0000269|PubMed:22608503, ECO:0000269|PubMed:22610116, CC ECO:0000269|PubMed:26621776}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Intellectual disability and myopathy syndrome (IDMYS) CC [MIM:619719]: An autosomal recessive disorder characterized by global CC developmental delay, mildly impaired intellectual development, CC hypotonia, muscle weakness and fatigue, and white matter abnormalities CC on brain imaging. Variable additional features may include CC sensorineural hearing loss, dysmorphic facies, and progressive heart CC disease. {ECO:0000269|PubMed:31575858}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: May contribute to the regulation of sleep duration. An CC intronic variant of this gene may account for about 5% of the variation CC of sleep duration between individuals (PubMed:22105623). Sleep duration CC is influenced both by environmental and genetic factors, with an CC estimated heritability of about 40%. Numerous genes are expected to CC contribute to the regulation of sleep duration. CC {ECO:0000305|PubMed:22105623}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family. CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On The Other Side - Issue CC 139 of June 2012; CC URL="https://web.expasy.org/spotlight/back_issues/139"; 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; AF061323; AAC16057.1; -; Genomic_DNA. DR EMBL; AF061289; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061290; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061291; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061292; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061293; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061294; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061295; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061296; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061297; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061298; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061299; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061300; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061301; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061302; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061303; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061304; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061305; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061306; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061307; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061308; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061309; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061310; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061311; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061312; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061313; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061314; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061315; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061316; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061317; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061318; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061319; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061320; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061321; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061322; AAC16057.1; JOINED; Genomic_DNA. DR EMBL; AF061324; AAC16058.1; -; Genomic_DNA. DR EMBL; AF061289; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061290; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061291; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061292; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061293; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061294; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061295; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061296; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061297; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061298; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061299; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061300; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061301; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061302; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061303; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061304; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061305; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061306; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061307; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061308; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061309; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061310; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061311; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061312; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061313; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061314; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061315; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061316; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061317; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061318; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061319; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061320; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061321; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AF061322; AAC16058.1; JOINED; Genomic_DNA. DR EMBL; AC008250; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084806; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS8693.1; -. [O60706-2] DR CCDS; CCDS8694.1; -. [O60706-1] DR RefSeq; NP_005682.2; NM_005691.3. [O60706-1] DR RefSeq; NP_064693.2; NM_020297.3. [O60706-2] DR RefSeq; XP_005253341.1; XM_005253284.3. DR RefSeq; XP_005253343.1; XM_005253286.3. DR RefSeq; XP_005253344.1; XM_005253287.4. DR RefSeq; XP_005253345.1; XM_005253288.3. [O60706-2] DR RefSeq; XP_011518847.1; XM_011520545.2. [O60706-2] DR AlphaFoldDB; O60706; -. DR SMR; O60706; -. DR BioGRID; 115371; 6. DR ComplexPortal; CPX-197; Inward rectifying potassium channel complex, Kir6.2-SUR2A. [O60706-1] DR ComplexPortal; CPX-199; Inward rectifying potassium channel complex, Kir6.2-SUR2B. [O60706-2] DR CORUM; O60706; -. DR IntAct; O60706; 3. DR STRING; 9606.ENSP00000261200; -. DR BindingDB; O60706; -. DR ChEMBL; CHEMBL1971; -. DR DrugBank; DB00171; ATP. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB09220; Nicorandil. DR DrugCentral; O60706; -. DR GuidetoPHARMACOLOGY; 2746; -. DR TCDB; 3.A.1.208.23; the atp-binding cassette (abc) superfamily. DR CarbonylDB; O60706; -. DR GlyCosmos; O60706; 6 sites, 1 glycan. DR GlyGen; O60706; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; O60706; -. DR PhosphoSitePlus; O60706; -. DR BioMuta; ABCC9; -. DR EPD; O60706; -. DR jPOST; O60706; -. DR MassIVE; O60706; -. DR PaxDb; 9606-ENSP00000261200; -. DR PeptideAtlas; O60706; -. DR ProteomicsDB; 49533; -. [O60706-1] DR ProteomicsDB; 49534; -. [O60706-2] DR ABCD; O60706; 3 sequenced antibodies. DR Antibodypedia; 12381; 261 antibodies from 31 providers. DR DNASU; 10060; -. DR Ensembl; ENST00000261200.9; ENSP00000261200.4; ENSG00000069431.14. [O60706-2] DR Ensembl; ENST00000261201.10; ENSP00000261201.4; ENSG00000069431.14. [O60706-1] DR GeneID; 10060; -. DR KEGG; hsa:10060; -. DR MANE-Select; ENST00000261200.9; ENSP00000261200.4; NM_020297.4; NP_064693.2. [O60706-2] DR UCSC; uc001rfh.4; human. [O60706-1] DR AGR; HGNC:60; -. DR CTD; 10060; -. DR DisGeNET; 10060; -. DR GeneCards; ABCC9; -. DR GeneReviews; ABCC9; -. DR HGNC; HGNC:60; ABCC9. DR HPA; ENSG00000069431; Tissue enhanced (skeletal). DR MalaCards; ABCC9; -. DR MIM; 239850; phenotype. DR MIM; 601439; gene. DR MIM; 608569; phenotype. DR MIM; 614050; phenotype. DR MIM; 619719; phenotype. DR neXtProt; NX_O60706; -. DR OpenTargets; ENSG00000069431; -. DR Orphanet; 130; Brugada syndrome. DR Orphanet; 1517; Cantu syndrome. DR Orphanet; 334; Familial atrial fibrillation. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR PharmGKB; PA396; -. DR VEuPathDB; HostDB:ENSG00000069431; -. DR eggNOG; KOG0054; Eukaryota. DR GeneTree; ENSGT00940000156680; -. DR HOGENOM; CLU_000604_27_6_1; -. DR InParanoid; O60706; -. DR OMA; WLSFWPR; -. DR OrthoDB; 3384185at2759; -. DR PhylomeDB; O60706; -. DR TreeFam; TF105201; -. DR PathwayCommons; O60706; -. DR Reactome; R-HSA-1296025; ATP sensitive Potassium channels. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-5578775; Ion homeostasis. DR Reactome; R-HSA-5678420; Defective ABCC9 causes CMD10, ATFB12 and Cantu syndrome. DR SignaLink; O60706; -. DR SIGNOR; O60706; -. DR BioGRID-ORCS; 10060; 10 hits in 1157 CRISPR screens. DR ChiTaRS; ABCC9; human. DR GeneWiki; ABCC9; -. DR GenomeRNAi; 10060; -. DR Pharos; O60706; Tclin. DR PRO; PR:O60706; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; O60706; Protein. DR Bgee; ENSG00000069431; Expressed in gastrocnemius and 128 other cell types or tissues. DR ExpressionAtlas; O60706; baseline and differential. DR GO; GO:0008282; C:inward rectifying potassium channel; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; ISS:ARUK-UCL. DR GO; GO:0030017; C:sarcomere; IEA:Ensembl. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome. DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0005267; F:potassium channel activity; IEA:Ensembl. DR GO; GO:0015459; F:potassium channel regulator activity; ISS:BHF-UCL. DR GO; GO:0008281; F:sulfonylurea receptor activity; ISS:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0001508; P:action potential; IEA:Ensembl. DR GO; GO:0061337; P:cardiac conduction; IMP:ARUK-UCL. DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl. DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IMP:MGI. DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:ARUK-UCL. DR GO; GO:0098655; P:monoatomic cation transmembrane transport; ISS:ARUK-UCL. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:BHF-UCL. DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:ARUK-UCL. DR GO; GO:0033198; P:response to ATP; IMP:ARUK-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR CDD; cd18591; ABC_6TM_SUR1_D1_like; 1. DR CDD; cd18602; ABC_6TM_SUR1_D2_like; 1. DR CDD; cd03290; ABCC_SUR1_N; 1. DR CDD; cd03288; ABCC_SUR2; 1. DR DisProt; DP02381; -. [O60706-2] DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. 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; IPR000388; ABCC8/9. DR InterPro; IPR001475; ABCC9. DR InterPro; IPR047080; ABCC9_ATP-bd_dom1. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1. DR PANTHER; PTHR24223:SF173; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 9; 1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR PRINTS; PR01094; SULFNYLUR2. DR PRINTS; PR01092; SULFNYLUREAR. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS50929; ABC_TM1F; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; O60706; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Atrial fibrillation; Cardiomyopathy; KW Disease variant; Glycoprotein; Intellectual disability; Membrane; KW Nucleotide-binding; Receptor; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1549 FT /note="ATP-binding cassette sub-family C member 9" FT /id="PRO_0000093402" FT TOPO_DOM 1..30 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 31..51 FT /note="Helical; Name=1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 52..72 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 73..93 FT /note="Helical; Name=2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 94..101 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 102..122 FT /note="Helical; Name=3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 123..132 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 133..153 FT /note="Helical; Name=4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 154..167 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 168..188 FT /note="Helical; Name=5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 189..301 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 302..322 FT /note="Helical; Name=6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 323..350 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 351..371 FT /note="Helical; Name=7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 372..423 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 424..444 FT /note="Helical; Name=8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 445..455 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 456..476 FT /note="Helical; Name=9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 477..531 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 532..552 FT /note="Helical; Name=10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 553..571 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 572..592 FT /note="Helical; Name=11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 593..990 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 991..1011 FT /note="Helical; Name=12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1012..1034 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1035..1055 FT /note="Helical; Name=13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1056..1127 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1128..1148 FT /note="Helical; Name=14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1149..1245 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1246..1266 FT /note="Helical; Name=15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1267..1549 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 297..597 FT /note="ABC transmembrane type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 672..912 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 994..1274 FT /note="ABC transmembrane type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 1312..1546 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 944..967 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 950..966 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 705..712 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 1346..1353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CARBOHYD 9 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 326 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 333 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 334 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1508..1549 FT /note="SSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK -> HTILTA FT DLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM (in isoform SUR2B)" FT /evidence="ECO:0000305" FT /id="VSP_000058" FT VARIANT 60 FT /note="H -> Y (in HTOCD; dbSNP:rs387907230)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068485" FT VARIANT 207 FT /note="D -> E (in HTOCD)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068486" FT VARIANT 380 FT /note="G -> C (in HTOCD; dbSNP:rs1165205076)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068487" FT VARIANT 432 FT /note="P -> L (in HTOCD; mutant channels show reduced ATP FT sensitivity; rat ABCC9 construct containing this mutation FT shows gain of function)" FT /evidence="ECO:0000269|PubMed:22610116, FT ECO:0000269|PubMed:26621776" FT /id="VAR_068488" FT VARIANT 478 FT /note="A -> V (in HTOCD; rat ABCC9 construct containing FT this mutation shows gain of function; dbSNP:rs387907211)" FT /evidence="ECO:0000269|PubMed:22608503, FT ECO:0000269|PubMed:26621776" FT /id="VAR_068489" FT VARIANT 1020 FT /note="S -> P (in HTOCD; dbSNP:rs387907229)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068490" FT VARIANT 1039 FT /note="F -> S (in HTOCD)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068491" FT VARIANT 1043 FT /note="C -> Y (in HTOCD; rat ABCC9 construct containing FT this mutation shows gain of function; dbSNP:rs387907210)" FT /evidence="ECO:0000269|PubMed:22608503, FT ECO:0000269|PubMed:26621776" FT /id="VAR_068492" FT VARIANT 1054 FT /note="S -> Y (in HTOCD)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068493" FT VARIANT 1108 FT /note="P -> S (in dbSNP:rs35404804)" FT /id="VAR_048143" FT VARIANT 1116 FT /note="R -> C (in HTOCD; dbSNP:rs387907228)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068494" FT VARIANT 1116 FT /note="R -> H (in HTOCD; mutant channels show reduced ATP FT sensitivity; dbSNP:rs387907227)" FT /evidence="ECO:0000269|PubMed:22610116" FT /id="VAR_068495" FT VARIANT 1154 FT /note="R -> Q (in HTOCD; mutant channels show reduced ATP FT sensitivity; dbSNP:rs387907209)" FT /evidence="ECO:0000269|PubMed:22608503, FT ECO:0000269|PubMed:22610116" FT /id="VAR_068496" FT VARIANT 1154 FT /note="R -> W (in HTOCD; dbSNP:rs387907208)" FT /evidence="ECO:0000269|PubMed:22608503, FT ECO:0000269|PubMed:22610116" FT /id="VAR_068497" FT VARIANT 1160 FT /note="L -> R (in dbSNP:rs780799175)" FT /evidence="ECO:0000269|PubMed:31303265" FT /id="VAR_083082" FT VARIANT 1513 FT /note="A -> T (in CMD1O; dbSNP:rs72559751)" FT /evidence="ECO:0000269|PubMed:15034580" FT /id="VAR_018483" FT VARIANT 1547 FT /note="T -> I (in ATFB12; compromises adenine FT nucleotide-dependent induction of KATP current; mutant FT ABCC9 that is coexpressed with KCNJ11 pore generates an FT aberrant channel that retains ATP-induced inhibition of FT potassium current, but shows a blunted response to ADP; FT dbSNP:rs387906805)" FT /evidence="ECO:0000269|PubMed:17245405" FT /id="VAR_066210" FT CONFLICT 586 FT /note="F -> S (in Ref. 1; AAC16057/AAC16058)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="S -> F (in Ref. 1; AAC16057/AAC16058)" FT /evidence="ECO:0000305" FT CONFLICT 1503 FT /note="I -> M (in Ref. 1; AAC16057/AAC16058)" FT /evidence="ECO:0000305" SQ SEQUENCE 1549 AA; 174223 MW; 55508C9343AB1218 CRC64; MSLSFCGNNI SSYNINDGVL QNSCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSRRESR HLHLFMPAVM GFVATTTSIV YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYCQSGL DISNLRFCIT GMMVILNGLL MAVEINVIRV RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHK KPIDLKAIGK LPIAMRAVTN YVCLKDAYEE QKKKVADHPN RTPSIWLAMY RAFGRPILLS STFRYLADLL GFAGPLCISG IVQRVNETQN GTNNTTGISE TLSSKEFLEN AYVLAVLLFL ALILQRTFLQ ASYYVTIETG INLRGALLAM IYNKILRLST SNLSMGEMTL GQINNLVAIE TNQLMWFLFL CPNLWAMPVQ IIMGVILLYN LLGSSALVGA AVIVLLAPIQ YFIATKLAEA QKSTLDYSTE RLKKTNEILK GIKLLKLYAW EHIFCKSVEE TRMKELSSLK TFALYTSLSI FMNAAIPIAA VLATFVTHAY ASGNNLKPAE AFASLSLFHI LVTPLFLLST VVRFAVKAII SVQKLNEFLL SDEIGDDSWR TGESSLPFES CKKHTGVQPK TINRKQPGRY HLDSYEQSTR RLRPAETEDI AIKVTNGYFS WGSGLATLSN IDIRIPTGQL TMIVGQVGCG KSSLLLAILG EMQTLEGKVH WSNVNESEPS FEATRSRNRY SVAYAAQKPW LLNATVEENI TFGSPFNKQR YKAVTDACSL QPDIDLLPFG DQTEIGERGI NLSGGQRQRI CVARALYQNT NIVFLDDPFS ALDIHLSDHL MQEGILKFLQ DDKRTLVLVT HKLQYLTHAD WIIAMKDGSV LREGTLKDIQ TKDVELYEHW KTLMNRQDQE LEKDMEADQT TLERKTLRRA MYSREAKAQM EDEDEEEEEE EDEDDNMSTV MRLRTKMPWK TCWRYLTSGG FFLLILMIFS KLLKHSVIVA IDYWLATWTS EYSINNTGKA DQTYYVAGFS ILCGAGIFLC LVTSLTVEWM GLTAAKNLHH NLLNKIILGP IRFFDTTPLG LILNRFSADT NIIDQHIPPT LESLTRSTLL CLSAIGMISY ATPVFLVALL PLGVAFYFIQ KYFRVASKDL QELDDSTQLP LLCHFSETAE GLTTIRAFRH ETRFKQRMLE LTDTNNIAYL FLSAANRWLE VRTDYLGACI VLTASIASIS GSSNSGLVGL GLLYALTITN YLNWVVRNLA DLEVQMGAVK KVNSFLTMES ENYEGTMDPS QVPEHWPQEG EIKIHDLCVR YENNLKPVLK HVKAYIKPGQ KVGICGRTGS GKSSLSLAFF RMVDIFDGKI VIDGIDISKL PLHTLRSRLS IILQDPILFS GSIRFNLDPE CKCTDDRLWE ALEIAQLKNM VKSLPGGLDA VVTEGGENFS VGQRQLFCLA RAFVRKSSIL IMDEATASID MATENILQKV VMTAFADRTV VTIAHRVSSI MDAGLVLVFS EGILVECDTV PNLLAHKNGL FSTLVMTNK //