ID Q9Z2P2_MOUSE Unreviewed; 899 AA. AC Q9Z2P2; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 04-NOV-2026, entry version 136. DE SubName: Full=Sulfonylurea receptor-1 {ECO:0000313|EMBL:AAC72292.1}; DE Flags: Fragment; GN Name=SUR-1 {ECO:0000313|EMBL:AAC72292.1}; 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 {ECO:0000313|EMBL:AAC72292.1}; RN [1] {ECO:0000313|EMBL:AAC72292.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=129/Sv {ECO:0000313|EMBL:AAC72292.1}; RX PubMed=10370080; DOI=10.1007/s004240050872; RA Beesley A.H., Qureshi I.Z., Giesberts A.N., Parker A.J., White S.J.; RT "Expression of sulphonylurea receptor protein in mouse kidney."; RL Pflugers Arch. 438:1-7(1999). RN [2] {ECO:0000313|EMBL:AAC72292.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=129/Sv {ECO:0000313|EMBL:AAC72292.1}; RX PubMed=12149271; DOI=10.1074/jbc.M206757200; RA Shiota C., Larsson O., Shelton K.D., Shiota M., Efanov A.M., Hoy M., RA Lindner J., Kooptiwut S., Juntti-Berggren L., Gromada J., Berggren P.O., RA Magnuson M.A.; RT "Sulfonylurea receptor type 1 knock-out mice have intact feeding-stimulated RT insulin secretion despite marked impairment in their response to glucose."; RL J. Biol. Chem. 277:37176-37183(2002). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family. CC Conjugate transporter (TC 3.A.1.208) subfamily. CC {ECO:0000256|ARBA:ARBA00009726}. 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; AH006979; AAC72292.1; -; Genomic_DNA. DR EMBL; AF037274; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037275; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037276; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037278; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037279; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037280; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037281; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037282; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037283; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037284; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037285; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037286; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037287; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037288; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037289; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037290; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037291; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037292; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037293; AAC72292.1; JOINED; Genomic_DNA. DR EMBL; AF037294; AAC72292.1; JOINED; Genomic_DNA. DR AlphaFoldDB; Q9Z2P2; -. DR GlyCosmos; Q9Z2P2; 1 site, No reported glycans. DR UCSC; uc009gyf.1; mouse. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-ARBA. DR GO; GO:0032991; C:protein-containing complex; IEA:UniProtKB-ARBA. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR CDD; cd18591; ABC_6TM_SUR1_D1_like; 1. DR FunFam; 1.20.1560.10:FF:000416; ATP-binding cassette sub-family C member 8; 1. DR FunFam; 3.40.50.300:FF:003233; ATP-binding cassette sub-family C member 8; 1. DR FunFam; 1.20.1560.10:FF:000369; ATP-binding cassette, sub-family C (CFTR/MRP), member 8; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; IPR050173; ABC_transporter_C-like. DR InterPro; IPR000844; ABCC8. DR InterPro; IPR000388; ABCC8/9. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1. DR PANTHER; PTHR24223:SF187; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 8; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PRINTS; PR01093; SULFNYLUR1. DR PRINTS; PR01092; SULFNYLUREAR. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00434}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00434}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AAC72292.1}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 33..52 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 73..94 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 106..124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 136..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 166..185 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 307..324 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 351..368 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 430..454 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 460..478 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 536..559 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 571..593 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 300..602 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 679..894 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 741..768 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..766 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 /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" FT NON_TER 899 FT /evidence="ECO:0000313|EMBL:AAC72292.1" SQ SEQUENCE 899 AA; 101088 MW; 278FF6625FDA1B25 CRC64; MPLAFCGTEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI HHSTWLHFPG HNLRWILTFM LLFVLVCEIA EGILSDGVTE SRHLHLYMPA GMAFMAAITS VVYYHNIETS NFPKLLIALL IYWTLAFITK TIKFVKFYDH AISFSQLRFC LTGLLVILYG MLLLVEINVI RVRRYIFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA HRKPIDLRAI GKLPIAMRAL TNYQRLCAAF DAQARKDRQS QQGARAIWRA LCHAFGRRLV LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NHVFQPKTQF LGVYFVSSQE FLGNAYVLAV LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HLSTSNLSMG EMTAGQICNL VAIDTNQLMW FFFLCPNLWA MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK LSQAQRSTLE YSNERLKQTN EMLRGIKLLK LYAWENIFCS RVEMTRRKEM TSLRAFAVYT SISIFMNTAI PIAAVLITFV GHVSFFKESD FSPSVAFASL SLFHILVTPL FLLSSVVRST VKALVSVQKL SEFLSSAEIR EEQCAPREPA PQGQAGKYQA VPLKVVNRKR PAREEVRDLL GPLQRLTPSM DGDADNFCVQ IIGGFFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS SLLLATLGEM QRVSGAVFWN SSLPDSEGED PSNPERETAA DSDARSRGPV AYASQKPWLL NATVEENITF ESPFNKQRYK MVIEACSLQP DIDILPHGDQ TQIGERGINL SGGQRQRISV ARALYQHTNV VFLDDPFSAL DVHLSDHLMQ AGILELLRDD KRTVVLVTHK LQYLPHADW //