ABCC8_RAT
ID ABCC8_RAT Reviewed; 1582 AA.
AC Q09429; O54989; P70532; Q9EQT0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP-binding cassette sub-family C member 8;
DE AltName: Full=Sulfonylurea receptor 1;
GN Name=Abcc8; Synonyms=Sur, Sur1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RC TISSUE=Pancreatic islet;
RX PubMed=7716547; DOI=10.1126/science.7716547;
RA Aguilar-Bryan L., Nichols C.G., Wechsler S.W., Clement J.P. IV,
RA Boyd A.E. III, Gonzalez G., Herrera-Sosa H., Nguy K., Bryan J.,
RA Nelson D.A.;
RT "Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator
RT of insulin secretion.";
RL Science 268:423-426(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Pancreatic islet;
RA Faure C., Partiseti M., Gouhier C., Graham D.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Pancreatic islet;
RA Blache P., Peyrollier K., Gros L., Bataille D.;
RT "Identification of two forms of sulfonylurea receptors (SUR 1A and SUR 1B)
RT by means of polymerase chain reaction, subcloning, DNA sequencing and
RT tissue distribution.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Vascular smooth muscle;
RA Cao K., Wang R.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GLYCOSYLATION AT ASN-10.
RX PubMed=8942641; DOI=10.1021/bi960777y;
RA Nelson D.A., Bryan J., Wechsler S., Clement J.P. IV, Aguilar-Bryan L.;
RT "The high-affinity sulfonylurea receptor: distribution, glycosylation,
RT purification, and immunoprecipitation of two forms from endocrine and
RT neuroendocrine cell lines.";
RL Biochemistry 35:14793-14799(1996).
CC -!- FUNCTION: Subunit of the beta-cell ATP-sensitive potassium channel
CC (KATP). Regulator of ATP-sensitive K(+) channels and insulin release.
CC {ECO:0000250|UniProtKB:Q09428}.
CC -!- SUBUNIT: Interacts with KCNJ11. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q09428};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=A;
CC IsoId=Q09429-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q09429-2; Sequence=VSP_000057;
CC Name=C;
CC IsoId=Q09429-3; Sequence=VSP_000056;
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; L40624; AAA99237.1; -; mRNA.
DR EMBL; X97279; CAA65934.1; -; mRNA.
DR EMBL; AF039595; AAB96684.1; -; mRNA.
DR EMBL; AB052294; BAB19011.1; -; mRNA.
DR RefSeq; NP_037171.2; NM_013039.2. [Q09429-1]
DR RefSeq; XP_008757542.1; XM_008759320.2. [Q09429-3]
DR AlphaFoldDB; Q09429; -.
DR SMR; Q09429; -.
DR ComplexPortal; CPX-186; Inward rectifying potassium channel complex, Kir6.2-SUR1.
DR CORUM; Q09429; -.
DR STRING; 10116.ENSRNOP00000028696; -.
DR BindingDB; Q09429; -.
DR ChEMBL; CHEMBL1944490; -.
DR GlyGen; Q09429; 2 sites.
DR iPTMnet; Q09429; -.
DR PaxDb; Q09429; -.
DR PRIDE; Q09429; -.
DR ABCD; Q09429; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000028696; ENSRNOP00000028696; ENSRNOG00000021130. [Q09429-1]
DR Ensembl; ENSRNOT00000038798; ENSRNOP00000035010; ENSRNOG00000021130. [Q09429-2]
DR GeneID; 25559; -.
DR KEGG; rno:25559; -.
DR UCSC; RGD:3786; rat. [Q09429-1]
DR CTD; 6833; -.
DR RGD; 3786; Abcc8.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000156626; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q09429; -.
DR OMA; ANTVVLW; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q09429; -.
DR Reactome; R-RNO-1296025; ATP sensitive Potassium channels.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR PRO; PR:Q09429; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021130; Expressed in cerebellum and 13 other tissues.
DR Genevisible; Q09429; RN.
DR GO; GO:0008282; C:inward rectifying potassium channel; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
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:RGD.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; IMP:RGD.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:RGD.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IMP:RGD.
DR GO; GO:0061855; P:negative regulation of neuroblast migration; IMP:RGD.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:RGD.
DR GO; GO:0061045; P:negative regulation of wound healing; IMP:RGD.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:RGD.
DR GO; GO:1905075; P:positive regulation of tight junction disassembly; IMP:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:1900721; P:positive regulation of uterine smooth muscle relaxation; IMP:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IMP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IDA:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; IMP:RGD.
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; IPR000844; ABCC8.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000388; Sulphorea_rcpt.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR PRINTS; PR01093; SULFNYLUR1.
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; Cell membrane; Glycoprotein; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1582
FT /note="ATP-binding cassette sub-family C member 8"
FT /id="PRO_0000093401"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 56..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 97..101
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 123..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..168
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..194
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 195..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..331
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 332..355
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 356..376
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 377..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 435..455
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 456..458
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 459..479
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 480..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 542..562
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 563..584
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 585..605
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 606..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1006..1026
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1027..1073
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1074..1094
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1095..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1139..1159
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1160
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1161..1181
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1182..1252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1253..1273
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1274..1277
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1278..1298
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1299..1582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 299..602
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 679..930
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1013..1307
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1345..1579
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 741..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 713..720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1379..1386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8942641"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 741
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:7716547"
FT /id="VSP_000056"
FT VAR_SEQ 1252..1289
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_000057"
FT CONFLICT 487
FT /note="S -> T (in Ref. 1; AAA99237)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="I -> T (in Ref. 4; BAB19011)"
FT /evidence="ECO:0000305"
FT CONFLICT 836..837
FT /note="QR -> PG (in Ref. 1; AAA99237)"
FT /evidence="ECO:0000305"
FT CONFLICT 1314
FT /note="R -> G (in Ref. 1; AAA99237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1582 AA; 177185 MW; 7C57A1CFC86B9214 CRC64;
MPLAFCGTEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI
HHSTWLHFPG HNLRWILTFI LLFVLVCEIA EGILSDGVTE SRHLHLYMPA GMAFMAAITS
VVYYHNIETS NFPKLLIALL IYWTLAFITK TIKFVKFYDH AIGFSQLRFC LTGLLVILYG
MLLLVEVNVI RVRRYVFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA
HKKPIDLRAI GKLPIAMRAL TNYQRLCLAF DAQARKDTQS QQGARAIWRA LCHAFGRRLV
LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NHVFQPKTQF LGVYFVSSQE FLGNAYVLAV
LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HLSTSNLSMG EMTAGQICNL
VAIDTNQLMW FFFLCPNLWA MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK
LSQAQRSTLE YSNERLKQTN EMLRGIKLLK LYAWENIFCS RVEKTRRKEM TSLRAFAVYT
SISIFMNTAI PIAAVLITFV GHVSFFKESD FSPSVAFASL SLFHILVTPL FLLSSVVRST
VKALVSVQKL SEFLSSAEIR EEQCAPREPA PQGQAGKYQA VPLKVVNRKR PAREEVRDLL
GPLQRLTPST DGDADNFCVQ IIGGFFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS
SLLLATLGEM QKVSGAVFWN SSLPDSEGED PSNPERETAA DSDARSRGPV AYASQKPWLL
NATVEENITF ESPFNKQRYK MVIEACSLQP DIDILPHGDQ TQIGERGINL SGGQRQRISV
ARALYQHTNV VFLDDPFSAL DVHLSDHLMQ AGILELLRDD KRTVVLVTHK LQYLPHADWI
IAMKDGTIQR EGTLKDFQRS ECQLFEHWKT LMNRQDQELE KETVMERKAP EPSQGLPRAM
SSRDGLLLDE DEEEEEAAES EEDDNLSSVL HQRAKIPWRA CTKYLSSAGI LLLSLLVFSQ
LLKHMVLVAI DYWLAKWTDS ALVLSPAARN CSLSQECALD QSVYAMVFTV LCSLGIALCL
VTSVTVEWTG LKVAKRLHRS LLNRIILAPM RFFETTPLGS ILNRFSSDCN TIDQHIPSTL
ECLSRSTLLC VSALAVISYV TPVFLVALLP LAVVCYFIQK YFRVASRDLQ QLDDTTQLPL
LSHFAETVEG LTTIRAFRYE ARFQQKLLEY TDSNNIASLF LTAANRWLEV RMEYIGACVV
LIAAATSISN SLHRELSAGL VGLGLTYALM VSNYLNWMVR NLADMEIQLG AVKRIHTLLK
TEAESYEGLL APSLIPKNWP DQGKIQIQNL SVRYDSSLKP VLKHVNALIS PGQKIGICGR
TGSGKSSFSL AFFRMVDMFE GRIIIDGIDI AKLPLHTLRS RLSIILQDPV LFSGTIRFNL
DPEKKCSDST LWEALEIAQL KLVVKALPGG LDAIITEGGE NFSQGQRQLF CLARAFVRKT
SIFIMDEATA SIDMATENIL QKVVMTAFAD RTVVTIAHRV HTILSADLVM VLKRGAILEF
DKPEKLLSQK DSVFASFVRA DK
