ABCC9_MOUSE
ID ABCC9_MOUSE Reviewed; 1546 AA.
AC P70170; O08902; O08920; P70171;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=ATP-binding cassette sub-family C member 9;
DE AltName: Full=Sulfonylurea receptor 2;
GN Name=Abcc9; Synonyms=Sur2;
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 [MRNA] (ISOFORMS SUR2A AND SUR2B).
RC TISSUE=Heart;
RX PubMed=8798681; DOI=10.1074/jbc.271.40.24321;
RA Isomoto S., Kondo C., Yamada M., Matsumoto S., Higashiguchi O., Horio Y.,
RA Matsuzawa Y., Kurachi Y.;
RT "A novel sulfonylurea receptor forms with BIR (Kir6.2) a smooth muscle type
RT ATP-sensitive K+ channel.";
RL J. Biol. Chem. 271:24321-24324(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SUR2A AND SUR2C).
RX PubMed=8826984; DOI=10.2337/diab.45.10.1439;
RA Chutkow W.A., Simon M.C., Le Beau M.M., Burant C.F.;
RT "Cloning, tissue expression, and chromosomal localization of SUR2, the
RT putative drug-binding subunit of cardiac, skeletal muscle, and vascular
RT KATP channels.";
RL Diabetes 45:1439-1445(1996).
RN [3]
RP PROTEIN SEQUENCE OF 493-498, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Spleen;
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).
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 -!- SUBUNIT: Interacts with KCNJ11.
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=3;
CC Name=SUR2A;
CC IsoId=P70170-1; Sequence=Displayed;
CC Name=SUR2B;
CC IsoId=P70170-2; Sequence=VSP_000060;
CC Name=SUR2C;
CC IsoId=P70170-3; Sequence=VSP_000059;
CC -!- TISSUE SPECIFICITY: Isoforms SUR2A and SUR2B are found in cerebellum,
CC eye, atrium, ventricle, urinary bladder and skeletal muscle. Isoform
CC SUR2B is also found in forebrain, liver, lung, pancreas, kidney,
CC spleen, stomach, small intestine, colon, uterus, ovary and fat tissue.
CC Isoform SUR2C is expressed exclusively in the heart.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; D86037; BAA12969.2; -; mRNA.
DR EMBL; D86038; BAA12970.2; -; mRNA.
DR EMBL; AF003531; AAB58753.1; -; mRNA.
DR EMBL; U97066; AAB58701.1; -; mRNA.
DR CCDS; CCDS39696.1; -. [P70170-2]
DR CCDS; CCDS39697.1; -. [P70170-3]
DR CCDS; CCDS39699.1; -. [P70170-1]
DR PIR; T42711; T42711.
DR PIR; T42728; T42728.
DR RefSeq; NP_001038185.1; NM_001044720.1.
DR RefSeq; NP_035641.1; NM_011511.2. [P70170-2]
DR RefSeq; NP_066378.1; NM_021041.2. [P70170-1]
DR RefSeq; NP_066379.2; NM_021042.2. [P70170-3]
DR RefSeq; XP_006507011.1; XM_006506948.3. [P70170-2]
DR RefSeq; XP_006507012.1; XM_006506949.3. [P70170-2]
DR RefSeq; XP_006507013.1; XM_006506950.3. [P70170-2]
DR RefSeq; XP_006507014.1; XM_006506951.3. [P70170-2]
DR AlphaFoldDB; P70170; -.
DR SMR; P70170; -.
DR BioGRID; 203578; 5.
DR ComplexPortal; CPX-196; Inward rectifying potassium channel complex, Kir6.2-SUR2A. [P70170-1]
DR ComplexPortal; CPX-198; Inward rectifying potassium channel complex, Kir6.2-SUR2B. [P70170-2]
DR CORUM; P70170; -.
DR STRING; 10090.ENSMUSP00000084805; -.
DR GlyGen; P70170; 2 sites.
DR iPTMnet; P70170; -.
DR PhosphoSitePlus; P70170; -.
DR EPD; P70170; -.
DR jPOST; P70170; -.
DR MaxQB; P70170; -.
DR PaxDb; P70170; -.
DR PRIDE; P70170; -.
DR ProteomicsDB; 296471; -. [P70170-1]
DR ProteomicsDB; 297496; -. [P70170-2]
DR ProteomicsDB; 297497; -. [P70170-3]
DR ABCD; P70170; 5 sequenced antibodies.
DR Antibodypedia; 12381; 238 antibodies from 31 providers.
DR DNASU; 20928; -.
DR Ensembl; ENSMUST00000073173; ENSMUSP00000072914; ENSMUSG00000030249. [P70170-3]
DR Ensembl; ENSMUST00000087527; ENSMUSP00000084805; ENSMUSG00000030249. [P70170-1]
DR Ensembl; ENSMUST00000100827; ENSMUSP00000098390; ENSMUSG00000030249. [P70170-2]
DR Ensembl; ENSMUST00000205202; ENSMUSP00000144779; ENSMUSG00000030249. [P70170-3]
DR GeneID; 20928; -.
DR KEGG; mmu:20928; -.
DR UCSC; uc009epm.1; mouse. [P70170-1]
DR UCSC; uc009epo.1; mouse. [P70170-3]
DR UCSC; uc009epp.1; mouse. [P70170-2]
DR CTD; 10060; -.
DR MGI; MGI:1352630; Abcc9.
DR VEuPathDB; HostDB:ENSMUSG00000030249; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000156680; -.
DR HOGENOM; CLU_000604_27_4_1; -.
DR InParanoid; P70170; -.
DR OMA; PMETRRY; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; P70170; -.
DR TreeFam; TF105201; -.
DR Reactome; R-MMU-1296025; ATP sensitive Potassium channels.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 20928; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Abcc9; mouse.
DR PRO; PR:P70170; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70170; protein.
DR Bgee; ENSMUSG00000030249; Expressed in triceps brachii and 218 other tissues.
DR ExpressionAtlas; P70170; baseline and differential.
DR Genevisible; P70170; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0008282; C:inward rectifying potassium channel; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; IMP:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:0008281; F:sulfonylurea receptor activity; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0061337; P:cardiac conduction; ISO:MGI.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IMP:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISO:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Direct protein sequencing; Glycoprotein;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1546
FT /note="ATP-binding cassette sub-family C member 9"
FT /id="PRO_0000093403"
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..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 370..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 443..453
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 475..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 551..569
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 591..987
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1009..1031
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1052
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1053..1124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1125..1145
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1146..1242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1243..1263
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1264..1546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 297..595
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 669..909
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 991..1271
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1309..1543
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 941..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..963
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 702..709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1343..1350
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 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 636..670
FT /note="Missing (in isoform SUR2C)"
FT /evidence="ECO:0000303|PubMed:8826984"
FT /id="VSP_000059"
FT VAR_SEQ 1505..1546
FT /note="SSIVDAGLVLVFSEGILVECDTGPNLLQHKNGLFSTLVMTNK -> HTILTA
FT DLVIVMKRGNILEYDTPESLLAQEDGVFASFVRADM (in isoform SUR2B)"
FT /evidence="ECO:0000303|PubMed:8798681"
FT /id="VSP_000060"
SQ SEQUENCE 1546 AA; 174239 MW; 91EEDFA2ECD9DBC2 CRC64;
MSLSFCGNNI SSYNIYYGVL QNPCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH
NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSHRASR HLHLFMPAVM GFVATTTSIV
YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYWQLGW GVSDLRFCIT GVMVILNGLL
MAVEINVIRV RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHR
KPIDLKAIGK LPIAMRAVTN YVCLKEAYEE QKKKAADHPN RTPSIWLAMY RAFGRPILLS
STFRYLADLL GFAGPLCISG IVQRVNEKTN TTREMFPETL SSKEFLENAH VLAVLLFLAL
ILQRTFLQAS YYVTIETGIN LRGALLAMIY NKILRLSTSN LSMGEMTLGQ INNLVAIETN
QLMWFLFLCP NLWAMPVQII MGVILLYNLL GSSALVGAAV IVLLAPIQYF IATKLAEAQK
STLDYSTERL KKTNEILKGI KLLKLYAWEH IFCKSVEETR MKELSSLKTF ALYTSLSIFM
NAAIPIAAVL ATFVTHAYAS GNNLKPAEAF ASLSLFHILV TPLFLLSTVV RFAVKAIISV
QKLNEFLLSD EIGEDSWRAG EGTLPFESCK KHTGVQSKPI NRKQPGRYHL DSYEQARRLR
PAETEDIAIK VTNGYFSWGS GLATLSNIDI RIPTGQLTMI VGQVGCGKSS LLLAILGEMQ
TLEGKVYWNN VNESEPSFEA TRSRSRYSVA YAAQKPWLLN ATVEENITFG SPFNRQRYKA
VTDACSLQPD IDLLPFGDQT EIGERGINLS GGQRQRICVA RALYQNTNIV FLDDPFSALD
IHLSDHLMQE GILKFLQDDK RTVVLVTHKL QYLTHADWII AMKDGSVLRE GTLKDIQTKD
VELYEHWKTL MNRQDQELEK DMEADQTTLE RKTLRRAMYS REAKAQMEDE DEEEEEEEDE
EDNMSTVMRL RTKMPWKTCW WYLTSGGFFL LFLMIFSKLL KHSVIVAIDY WLATWTSEYS
INHPGKADQT FYVAGFSILC GAGIFLCLVT SLTVEWMGLT AAKNLHHNLL NKIILGPIRF
FDTTPLGLIL NRFSADTNII DQHIPPTLES LTRSTLLCLS AIGMISYATP VFLVALAPLG
VAFYFIQKYF RVASKDLQEL DDSTQLPLLC HFSETAEGLT TIRAFRHETR FKQRMLELTD
TNNIAYLFLS AANRWLEVRT DYLGACIVLT ASIASISGSS NSGLVGLGLL YALTITNYLN
WVVRNLADLE VQMGAVKKVN SFLTMESENY EGTMDPSQVP EHWPQEGEIK IHDLCVRYEN
NLKPVLKHVK AYIKPGQKVG ICGRTGSGKS SLSLAFFRMV DIFDGKIVID GIDISKLPLH
TLRSRLSIIL QDPILFSGSI RFNLDPECKC TDDRLWEALE IAQLKNMVKS LPGGLDATVT
EGGENFSVGQ RQLFCLARAF VRKSSILIMD EATASIDMAT ENILQKVVMT AFADRTVVTI
AHRVSSIVDA GLVLVFSEGI LVECDTGPNL LQHKNGLFST LVMTNK
