ABCC9_HUMAN
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 03-AUG-2022, entry version 198.
DE RecName: Full=ATP-binding cassette sub-family C member 9;
DE AltName: Full=Sulfonylurea receptor 2;
GN Name=ABCC9; Synonyms=SUR2;
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).
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 -!- 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";
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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; 5.
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 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; O60706; -.
DR PeptideAtlas; O60706; -.
DR PRIDE; O60706; -.
DR ProteomicsDB; 49533; -. [O60706-1]
DR ProteomicsDB; 49534; -. [O60706-2]
DR ABCD; O60706; 3 sequenced antibodies.
DR Antibodypedia; 12381; 238 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 CTD; 10060; -.
DR DisGeNET; 10060; -.
DR GeneCards; ABCC9; -.
DR GeneReviews; ABCC9; -.
DR HGNC; HGNC:60; ABCC9.
DR HPA; ENSG00000069431; Tissue enhanced (liver).
DR MalaCards; ABCC9; -.
DR MIM; 239850; phenotype.
DR MIM; 601439; gene.
DR MIM; 608569; phenotype.
DR MIM; 614050; 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; PMETRRY; -.
DR OrthoDB; 801938at2759; -.
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; 9 hits in 1078 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 126 other tissues.
DR ExpressionAtlas; O60706; baseline and differential.
DR Genevisible; O60706; HS.
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:0019829; F:ATPase-coupled cation transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome.
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:0061337; P:cardiac conduction; IMP:ARUK-UCL.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0098655; P:cation transmembrane transport; ISS:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0098662; P:inorganic 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:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IMP:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR DisProt; DP02381; -. [O60706-2]
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; IPR001475; ABCC9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000388; Sulphorea_rcpt.
DR PANTHER; PTHR24223:SF173; PTHR24223:SF173; 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Atrial fibrillation; Cardiomyopathy;
KW Disease variant; Glycoprotein; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Transmembrane; 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 (unknown pathological significance;
FT 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 nucleotide-
FT dependent induction of KATP current; mutant ABCC9 that is
FT co-expressed with KCNJ11 pore generates an aberrant channel
FT that retains ATP-induced inhibition of potassium current,
FT but shows a blunted response to ADP; 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
