ABCC8_CRICR
ID ABCC8_CRICR Reviewed; 1582 AA.
AC Q09427;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ATP-binding cassette sub-family C member 8;
DE AltName: Full=Sulfonylurea receptor 1;
GN Name=ABCC8; Synonyms=SUR;
OS Cricetus cricetus (Black-bellied hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetus.
OX NCBI_TaxID=10034;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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 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).
RN [3]
RP TOPOLOGY, AND GLYCOSYLATION AT ASN-10.
RX PubMed=10506167; DOI=10.1074/jbc.274.41.29122;
RA Raab-Graham K.F., Cirilo L.J., Boettcher A.A., Radeke C.M.,
RA Vandenberg C.A.;
RT "Membrane topology of the amino-terminal region of the sulfonylurea
RT receptor.";
RL J. Biol. Chem. 274:29122-29129(1999).
CC -!- FUNCTION: Subunit of the beta-cell ATP-sensitive potassium channel
CC (KATP). Regulator of ATP-sensitive potassium channels and insulin
CC release. {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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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; L40623; AAA99201.1; -; mRNA.
DR PDB; 5TWV; EM; 6.30 A; B/D/F/H=1-1582.
DR PDB; 5YWB; EM; 5.20 A; B/D/F/H=1-1582.
DR PDB; 6BAA; EM; 3.63 A; E/F/G/H=1-1582.
DR PDB; 6PZ9; EM; 3.65 A; C=1-1582.
DR PDB; 6PZA; EM; 3.74 A; C=1-1582.
DR PDB; 6PZB; EM; 4.55 A; G=1-1582.
DR PDB; 6PZC; EM; 4.34 A; H=1-1582.
DR PDB; 6PZI; EM; 4.50 A; G=1-1582.
DR PDBsum; 5TWV; -.
DR PDBsum; 5YWB; -.
DR PDBsum; 6BAA; -.
DR PDBsum; 6PZ9; -.
DR PDBsum; 6PZA; -.
DR PDBsum; 6PZB; -.
DR PDBsum; 6PZC; -.
DR PDBsum; 6PZI; -.
DR AlphaFoldDB; Q09427; -.
DR SMR; Q09427; -.
DR CORUM; Q09427; -.
DR iPTMnet; Q09427; -.
DR ABCD; Q09427; 1 sequenced antibody.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro.
DR DisProt; DP01429; -.
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 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Nucleotide-binding; Receptor; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1582
FT /note="ATP-binding cassette sub-family C member 8"
FT /id="PRO_0000093399"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10506167"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT TOPO_DOM 56..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10506167"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT TOPO_DOM 97..101
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10506167"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT TOPO_DOM 123..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10506167"
FT TRANSMEM 135..154
FT /note="Helical; Name=4"
FT TOPO_DOM 155..167
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10506167"
FT TRANSMEM 168..194
FT /note="Helical; Name=5"
FT TOPO_DOM 195..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10506167"
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:0000269|PubMed:10506167"
FT TRANSMEM 1006..1026
FT /note="Helical; Name=12"
FT TOPO_DOM 1027..1073
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10506167"
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:0000269|PubMed:10506167"
FT TRANSMEM 1278..1298
FT /note="Helical; Name=17"
FT TOPO_DOM 1299..1582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10506167"
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..766
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 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:10506167,
FT ECO:0000269|PubMed:8942641"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
SQ SEQUENCE 1582 AA; 177147 MW; B7FFDFD8E7124BA4 CRC64;
MPLAFCGTEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI
HHSTWLHFPG HNLRWILTFI LLFVLVCEIA EGILSDGVTE SRHLHLYMPA GMAFMAAITS
VVYYHNIETS NFPKLLIALL IYWTLAFITK TIKFVKFYDH AIGFSQLRFC LTGLLVILYG
MLLLVEVNVI RVRRYIFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA
HKKPIDLRAI AKLPIAMRAL TNYQRLCVAF DAQARKDTQS PQGARAIWRA LCHAFGRRLI
LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NHVFQPKTQF LGVYFVSSQE FLGNAYVLAV
LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HMSTSNLSMG EMTAGQICNL
VAIDTNQLMW FFFLCPNLWT MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK
LSQAQRTTLE HSNERLKQTN EMLRGMKLLK LYAWESIFCS RVEVTRRKEM TSLRAFAVYT
SISIFMNTAI PIAAVLITFV GHVSFFKESD LSPSVAFASL SLFHILVTPL FLLSSVVRST
VKALVSVQKL SEFLSSAEIR EEQCAPREPA PQGQAGKYQA VPLKVVNRKR PAREEVRDLL
GPLQRLAPSM DGDADNFCVQ IIGGFFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS
SLLLATLGEM QKVSGAVFWN SNLPDSEGED PSSPERETAA GSDIRSRGPV AYASQKPWLL
NATVEENITF ESPFNKQRYK MVIEACSLQP DIDILPHGDQ TQIGERGINL SGGQRQRISV
ARALYQQTNV VFLDDPFSAL DVHLSDHLMQ AGILELLRDD KRTVVLVTHK LQYLPHADWI
IAMKDGTIQR EGTLKDFQRS ECQLFEHWKT LMNRQDQELE KETVMERKAS EPSQGLPRAM
SSRDGLLLDE EEEEEEAAES EEDDNLSSVL HQRAKIPWRA CTKYLSSAGI LLLSLLVFSQ
LLKHMVLVAI DYWLAKWTDS ALVLSPAARN CSLSQECDLD QSVYAMVFTL LCSLGIVLCL
VTSVTVEWTG LKVAKRLHRS LLNRIILAPM RFFETTPLGS ILNRFSSDCN TIDQHIPSTL
ECLSRSTLLC VSALTVISYV TPVFLVALLP LAVVCYFIQK YFRVASRDLQ QLDDTTQLPL
VSHFAETVEG LTTIRAFRYE ARFQQKLLEY TDSNNIASLF LTAANRWLEV CMEYIGACVV
LIAAATSISN SLHRELSAGL VGLGLTYALM VSNYLNWMVR NLADMEIQLG AVKRIHALLK
TEAESYEGLL APSLIPKNWP DQGKIQIQNL SVRYDSSLKP VLKHVNTLIS PGQKIGICGR
TGSGKSSFSL AFFRMVDMFE GRIIIDGIDI AKLPLHTLRS RLSIILQDPV LFSGTIRFNL
DPEKKCSDST LWEALEIAQL KLVVKALPGG LDAIITEGGE NFSQGQRQLF CLARAFVRKT
SIFIMDEATA SIDMATENIL QKVVMTAFAD RTVVTIAHRV HTILSADLVM VLKRGAILEF
DKPETLLSQK DSVFASFVRA DK
