ID ABCC9_RAT Reviewed; 1545 AA. AC Q63563; O89115; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=ATP-binding cassette sub-family C member 9; DE AltName: Full=Sulfonylurea receptor 2; GN Name=Abcc9; Synonyms=Sur2; 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 SUR2A). RC TISSUE=Brain; RX PubMed=8630239; DOI=10.1016/s0896-6273(00)80124-5; RA Inagaki N., Gonoi T., Clement G., Wang C., Aguilar-Bryan L., Bryan J., RA Seino S.; RT "A family of sulfonylurea receptors determines the pharmacological RT properties of ATP-sensitive K+ channels."; RL Neuron 16:1011-1017(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SUR2B). RC STRAIN=Sprague-Dawley; RA Furuta H., Inagaki N., Gonoi T., Chien E., Seino S., Bell G.I.; RT "Rat sulfonylurea receptor 2B, alternatively spliced product."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SUR2B). RA Tanemoto M., Abe T., Hebert S.C.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. 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 -!- INTERACTION: CC Q63563-2; Q63563-2: Abcc9; NbExp=2; IntAct=EBI-8282518, EBI-8282518; 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=2; CC Name=SUR2A; CC IsoId=Q63563-1; Sequence=Displayed; CC Name=SUR2B; CC IsoId=Q63563-2; Sequence=VSP_000061; CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle CC and ovary. Moderate levels are found in brain, tongue and pancreatic CC islets. Low levels are found in lung, testis and adrenal gland. CC Expressed at very low levels in stomach, colon, thyroid and pituitary. 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; D83598; BAA12020.1; -; mRNA. DR EMBL; AF087838; AAC36347.1; -; mRNA. DR EMBL; AF019628; AAC24758.1; -; mRNA. DR PIR; T42751; T42751. DR PIR; T46645; T46645. DR RefSeq; NP_037172.2; NM_013040.2. [Q63563-2] DR PDB; 7MIT; EM; 3.40 A; E=1-1541. DR PDB; 7MJO; EM; 4.00 A; E/G=1-1541. DR PDB; 7MJP; EM; 4.20 A; E=1-1541. DR PDB; 7MJQ; EM; 4.20 A; E/G=1-1541. DR PDB; 7VLR; EM; 3.40 A; A=1-1541. DR PDB; 7VLS; EM; 3.30 A; A=1-1541. DR PDB; 7VLT; EM; 3.10 A; A=1-1541. DR PDB; 7VLU; EM; 3.30 A; A=1-1545. DR PDB; 7Y1J; EM; 3.00 A; A=1-1545. DR PDB; 7Y1K; EM; 3.80 A; A=1-1545. DR PDB; 7Y1L; EM; 3.73 A; A=1-1541. DR PDB; 7Y1M; EM; 3.57 A; A=1-1541. DR PDB; 7Y1N; EM; 3.61 A; A=1-1541. DR PDBsum; 7MIT; -. DR PDBsum; 7MJO; -. DR PDBsum; 7MJP; -. DR PDBsum; 7MJQ; -. DR PDBsum; 7VLR; -. DR PDBsum; 7VLS; -. DR PDBsum; 7VLT; -. DR PDBsum; 7VLU; -. DR PDBsum; 7Y1J; -. DR PDBsum; 7Y1K; -. DR PDBsum; 7Y1L; -. DR PDBsum; 7Y1M; -. DR PDBsum; 7Y1N; -. DR AlphaFoldDB; Q63563; -. DR EMDB; EMD-23864; -. DR EMDB; EMD-23880; -. DR EMDB; EMD-23881; -. DR EMDB; EMD-23882; -. DR EMDB; EMD-32024; -. DR EMDB; EMD-32025; -. DR EMDB; EMD-32026; -. DR EMDB; EMD-32027; -. DR EMDB; EMD-33563; -. DR EMDB; EMD-33564; -. DR EMDB; EMD-33565; -. DR EMDB; EMD-33566; -. DR EMDB; EMD-33567; -. DR SMR; Q63563; -. DR ComplexPortal; CPX-181; Inward rectifying potassium channel complex, Kir6.2-SUR2A. [Q63563-1] DR ComplexPortal; CPX-185; Inward rectifying potassium channel complex, Kir6.2-SUR2B. [Q63563-2] DR IntAct; Q63563; 1. DR MINT; Q63563; -. DR STRING; 10116.ENSRNOP00000052402; -. DR BindingDB; Q63563; -. DR ChEMBL; CHEMBL3244; -. DR GlyCosmos; Q63563; 3 sites, No reported glycans. DR GlyGen; Q63563; 3 sites. DR PhosphoSitePlus; Q63563; -. DR SwissPalm; Q63563; -. DR PaxDb; 10116-ENSRNOP00000052402; -. DR ABCD; Q63563; 5 sequenced antibodies. DR GeneID; 25560; -. DR KEGG; rno:25560; -. DR AGR; RGD:3787; -. DR CTD; 10060; -. DR RGD; 3787; Abcc9. DR eggNOG; KOG0054; Eukaryota. DR InParanoid; Q63563; -. DR OrthoDB; 3384185at2759; -. DR PhylomeDB; Q63563; -. DR Reactome; R-RNO-1296025; ATP sensitive Potassium channels. DR Reactome; R-RNO-382556; ABC-family proteins mediated transport. DR Reactome; R-RNO-5578775; Ion homeostasis. DR PRO; PR:Q63563; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD. DR GO; GO:0008282; C:inward rectifying potassium channel; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0030017; C:sarcomere; ISO:RGD. DR GO; GO:0030315; C:T-tubule; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IGI:ARUK-UCL. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:RGD. DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0008281; F:sulfonylurea receptor activity; IDA:BHF-UCL. DR GO; GO:0019905; F:syntaxin binding; IPI:RGD. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD. DR GO; GO:0001508; P:action potential; ISO:RGD. DR GO; GO:0001568; P:blood vessel development; ISO:RGD. DR GO; GO:0061337; P:cardiac conduction; ISO:RGD. DR GO; GO:0086003; P:cardiac muscle cell contraction; ISO:RGD. DR GO; GO:0072359; P:circulatory system development; ISO:RGD. DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD. DR GO; GO:0051607; P:defense response to virus; ISO:RGD. DR GO; GO:0048144; P:fibroblast proliferation; ISO:RGD. DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD. DR GO; GO:0098662; P:inorganic cation transmembrane transport; IGI:ARUK-UCL. DR GO; GO:0098655; P:monoatomic cation transmembrane transport; IMP:ARUK-UCL. DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:RGD. DR GO; GO:0006813; P:potassium ion transport; IDA:RGD. DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD. DR GO; GO:0033198; P:response to ATP; IGI:ARUK-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0006932; P:substrate-dependent cell migration, cell contraction; NAS:RGD. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd18591; ABC_6TM_SUR1_D1_like; 1. DR CDD; cd18602; ABC_6TM_SUR1_D2_like; 1. DR CDD; cd03290; ABCC_SUR1_N; 1. DR CDD; cd03288; ABCC_SUR2; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR000388; ABCC8/9. DR InterPro; IPR001475; ABCC9. DR InterPro; IPR047080; ABCC9_ATP-bd_dom1. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1. DR PANTHER; PTHR24223:SF173; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 9; 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; SSF90123; ABC transporter transmembrane region; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Alternative splicing; ATP-binding; Glycoprotein; Membrane; KW Nucleotide-binding; Receptor; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1545 FT /note="ATP-binding cassette sub-family C member 9" FT /id="PRO_0000093405" 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..347 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 348..368 FT /note="Helical; Name=7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 369..420 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 421..441 FT /note="Helical; Name=8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 442..452 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 453..473 FT /note="Helical; Name=9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 474..528 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 529..549 FT /note="Helical; Name=10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 550..568 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 569..589 FT /note="Helical; Name=11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 590..986 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 987..1007 FT /note="Helical; Name=12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1008..1030 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1031..1051 FT /note="Helical; Name=13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1052..1123 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1124..1144 FT /note="Helical; Name=14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1145..1241 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1242..1262 FT /note="Helical; Name=15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1263..1545 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 297..594 FT /note="ABC transmembrane type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 668..908 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 990..1270 FT /note="ABC transmembrane type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 1308..1542 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 940..963 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 946..962 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 701..708 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 1342..1349 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 CARBOHYD 331 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1504..1545 FT /note="SSIMDAGLVLVFSEGILVECDTGPNLLQHKNGLFSTLVMTNK -> HTILTA FT DLVIVMKRGNILEYDTPESLLAQEDGVFASFVRADM (in isoform SUR2B)" FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3" FT /id="VSP_000061" FT HELIX 10..13 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 23..47 FT /evidence="ECO:0007829|PDB:7MIT" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:7MIT" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 70..95 FT /evidence="ECO:0007829|PDB:7MIT" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7MIT" FT TURN 102..105 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 106..127 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 135..157 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 165..191 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 217..226 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 232..240 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 257..273 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 285..292 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 295..311 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 348..394 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 399..401 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 406..415 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 417..449 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 452..461 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 463..496 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 499..505 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 508..557 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 565..606 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 613..616 FT /evidence="ECO:0007829|PDB:7MIT" FT STRAND 666..692 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 695..700 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 703..706 FT /evidence="ECO:0007829|PDB:7VLT" FT HELIX 707..714 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 718..727 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 748..751 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 762..767 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 768..770 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 774..783 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 787..791 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 796..798 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 800..806 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 810..823 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 827..833 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 834..837 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 840..849 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 850..853 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 854..857 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 861..865 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 869..874 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 876..890 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 892..898 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 900..920 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 925..936 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 962..965 FT /evidence="ECO:0007829|PDB:7MIT" FT HELIX 967..970 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 975..983 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 987..1015 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1029..1073 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1077..1082 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1085..1101 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1103..1127 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1131..1175 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1178..1184 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1187..1236 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1241..1282 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 1295..1297 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 1300..1303 FT /evidence="ECO:0007829|PDB:7VLS" FT STRAND 1308..1318 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1324..1332 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1338..1343 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1346..1348 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1349..1355 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1359..1368 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 1373..1375 FT /evidence="ECO:0007829|PDB:7VLT" FT HELIX 1378..1383 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1385..1388 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1396..1398 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1399..1403 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1411..1420 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1424..1429 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1433..1435 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1440..1442 FT /evidence="ECO:0007829|PDB:7VLT" FT HELIX 1447..1461 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1464..1470 FT /evidence="ECO:0007829|PDB:7Y1J" FT TURN 1471..1474 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1477..1490 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1492..1499 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1503..1506 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1510..1516 FT /evidence="ECO:0007829|PDB:7Y1J" FT STRAND 1519..1524 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1526..1531 FT /evidence="ECO:0007829|PDB:7Y1J" FT HELIX 1536..1541 FT /evidence="ECO:0007829|PDB:7Y1J" SQ SEQUENCE 1545 AA; 174118 MW; 768DA1F58E9945E7 CRC64; MSLSFCGNNI SSYNIYHGVL QNPCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSQRASR HLHLFMPAVM GFVATTTSIV YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYWQLGW GMSDLRFCIT GVMVILNGLL MAVEINVIRV RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHR KPIDLKAIGK LPIAMRAVTN YVCLKEAYEE QKKKAADHPN RTPSIWLAMY RAFGRPILLS STFRYLADLL GFAGPLCISG IVQRVNEPKN NTTRFSETLS SKEFLENAHV LAVLLFLALI LQRTFLQASY YVTIETGINL RGALLAMIYN KILRLSTSNL SMGEMTLGQI NNLVAIETNQ LMWFLFLCPN LWAMPVQIIM GVILLYNLLG SSALVGAAVI VLLAPIQYFI ATKLAEAQKS TLDYSTERLK KTNEILKGIK LLKLYAWEHI FCKSVEETRM KELSSLKTFA LYTSLSIFMN AAIPIAAVLA TFVTHAYASG NNLKPAEAFA SLSLFHILVT PLFLLSTVVR FAVKAIISVQ KLNEFLLSDE IGEDSWRTGE GTLPFESCKK HTGVQSKPIN RKQPGRYHLD NYEQARRLRP AETEDVAIKV TNGYFSWGSG LATLSNIDIR IPTGQLTMIV GQVGCGKSSL LLAILGEMQT LEGKVYWNNV NESEPSFEAT RSRSRYSVAY AAQKPWLLNA TVEENITFGS SFNRQRYKAV TDACSLQPDI DLLPFGDQTE IGERGINLSG GQRQRICVAR ALYQNTNIVF LDDPFSALDI HLSDHLMQEG ILKFLQDDKR TVVLVTHKLQ YLTHADWIIA MKDGSVLREG TLKDIQTKDV ELYEHWKTLM NRQDQELEKD MEADQTTLER KTLRRAMYSR EAKAQMEDED EEEEEEEDED DNMSTVMRLR TKMPWKTCWW YLTSGGFFLL FLMIFSKLLK HSVIVAIDYW LATWTSEYSI NDPGKADQTF YVAGFSILCG AGIFLCLVTS LTVEWMGLTA AKNLHHNLLN KIILGPIRFF DTTPLGLILN RFSADTNIID QHIPPTLESL TRSTLLCLSA IGMISYATPV FLIALAPLGV AFYFIQKYFR VASKDLQELD DSTQLPLLCH FSETAEGLTT IRAFRHETRF KQRMLELTDT NNIAYLFLSA ANRWLEVRTD YLGACIVLTA SIASISGSSN SGLVGLGLLY ALTITNYLNW VVRNLADLEV QMGAVKKVNS FLTMESENYE GTMDPSQVPE HWPQEGEIKI HDLCVRYENN LKPVLKHVKA YIKPGQKVGI CGRTGSGKSS LSLAFFRMVD IFDGKIVIDG IDISKLPLHT LRSRLSIILQ DPILFSGSIR FNLDPECKCT DDRLWEALEI AQLKNMVKSL PGGLDATVTE GGENFSVGQR QLFCLARAFV RKSSILIMDE ATASIDMATE NILQKVVMTA FADRTVVTIA HRVSSIMDAG LVLVFSEGIL VECDTGPNLL QHKNGLFSTL VMTNK //