ABCC9_RABIT
ID ABCC9_RABIT Reviewed; 1549 AA.
AC P82451;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP-binding cassette sub-family C member 9;
DE AltName: Full=Sulfonylurea receptor 2;
GN Name=ABCC9; Synonyms=SUR2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Winkfein R.J., Light P.E., French R.J.;
RT "Rabbit cardiac ventricle sulfonyl urea receptor.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney proximal tubule;
RX PubMed=11788443; DOI=10.1152/ajprenal.00063.2001;
RA Brochiero E., Wallendorf B., Gagnon D., Laprade R., Lapointe J.Y.;
RT "Cloning of rabbit Kir6.1, SUR2A, and SUR2B: possible candidates for a
RT renal K(ATP) channel.";
RL Am. J. Physiol. 282:F289-F300(2002).
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 -!- 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; AF087468; AAD52090.1; -; mRNA.
DR EMBL; AF417510; AAL07505.1; -; mRNA.
DR RefSeq; NP_001075513.1; NM_001082044.1.
DR AlphaFoldDB; P82451; -.
DR SMR; P82451; -.
DR STRING; 9986.ENSOCUP00000006942; -.
DR GeneID; 100008700; -.
DR KEGG; ocu:100008700; -.
DR CTD; 10060; -.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; P82451; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; 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_0000093404"
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 665..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 CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1549 AA; 174171 MW; D00DF9ACEEEC0075 CRC64;
MSLSFCGNNI SSYNIYDGVL QNPCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH
NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSRRESR HLHLFMPAVM GFVATTTSIV
YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYWQSGW GVSDLRFCIT GIMVILNGLL
MAVEINVIRI RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHK
KPIDLKAIGK LPIAMRAVTN YVCLKDAYEE QKKKAADHPN RTPSIWLAMY RAFGRPILLS
STFRYLADLL GFAGPLCISG IVQRVNETQN GTNNTTGISE ILSSKEFLEN AYVLAVLLFL
ALILQRTFLQ ASYYVTIETG INLRGALLAM IYNKILRLST SNLSMGEMTL GQINNLVAIE
TNQLMWFLFL CPNLWAMPVQ IIMGVILLYN LLGSSALVGA AVIVLLAPMQ YFIATKLAEA
QKSTLDYSTE RLKKTNEILK GIKLLKLYAW EHIFCKSVEE TRVKELSSLK AFALYTSLSI
FMNAAIPIAA VLATFVTHAY ASGNNLQPAE AFASLSLFHI LVTPLFLLST VVRFAVKAII
SVQKLNEFLL SDEIGDDSWR TGEASLPFES CKKHTGVQPK TINRKQPGRY HLDSYEQSTR
RLRPMETEDI AIKVTNGCFS WGSGAATLSN IDIRIPTGQL TMIVGQVGCG KSSLLLAILG
EMQTLDGKVH WSNVNESEPS FEATRSRNRY SVAYAAQKPW LLNATVEENI TFGSPFNKQR
YKAVTDACSL QPDIDLLPFG DQTEIGERGI NLSGGQTERI CVARALYQNT NIVFLDDPFS
ALDIHLSDHL MQEGILKFLQ DDKRTLVLVT HKLQYLTHAD WIIAMKDGSV LREGTLKDIQ
TKDVELYEHW KTLMNRQDQE LEKDMEADQT TLERKTLRRA MYSREAKAQM EDEDEEEEEE
EDEDDNMSTV MRLRTKMPWK TCWRYLTSGG FFLLFLMIFS KLLKHSVIVA IDYWLATWTS
EYSINNTGKA DQTYYVAGFS ILCGAGIFLC LVTSLTVEWM GLTAAKNLHH NLLNKIILGP
IRFFDTTPLG LILNRFSADT NIIDQHIPPT LESLTRSTLL CLSAIGMISY ATPVFLVALV
PLGVAFYFIQ KYFRVASKDL QELDDSTQLP LLCHFSETAE GLTTIRAFRH EARFKQRMLE
LTDTNNIAYL FLSAANRWLE VRTDYLGACI VLTASIASIS GSSNSGLVGL GLLYALTITN
YLNWVVRNLA DLEVQMGAVK KVNSFLTMES ENYEGTMDPS QVPEHWPQEG EIKIHDLCVR
YENNLKPVLK HVKAYIKPGQ KVGICGRTGS GKSSLSLAFF RMVDIFDGKI VIDGIDISKL
PLHTLRSRLS IILQDPILFS GSIRFNLDPE CKCTDDRLWE ALEIAQLKNM VKSLSGGLDA
VVTEGGENFS VGQRQLFCLA RAFVRKSSIL IMDEATASID MATENILQKV VMTAFADRTV
VTIAHRVSSI VDADLVLVFS EGILVECDTG PNLLTHKNGL FSTLVMTNK
