ABCC9_RAT
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 03-AUG-2022, entry version 153.
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}.
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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 PDBsum; 7MIT; -.
DR PDBsum; 7MJO; -.
DR PDBsum; 7MJP; -.
DR PDBsum; 7MJQ; -.
DR AlphaFoldDB; Q63563; -.
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 GlyGen; Q63563; 3 sites.
DR PRIDE; Q63563; -.
DR ABCD; Q63563; 5 sequenced antibodies.
DR GeneID; 25560; -.
DR KEGG; rno:25560; -.
DR CTD; 10060; -.
DR RGD; 3787; Abcc9.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; Q63563; -.
DR OrthoDB; 138195at2759; -.
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:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0019829; F:ATPase-coupled 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:0061337; P:cardiac conduction; ISO:RGD.
DR GO; GO:0086003; P:cardiac muscle cell contraction; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IGI: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:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; 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 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; 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..219
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 257..277
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 295..311
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 350..393
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 407..415
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 417..426
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 434..449
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 452..461
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 463..497
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 510..558
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 565..606
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 675..681
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 707..715
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 762..767
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 774..784
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 787..792
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 796..798
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 799..806
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 810..822
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 841..854
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 855..859
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 880..885
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 892..895
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 901..909
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 962..965
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 966..971
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 977..982
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 988..990
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 991..1017
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1030..1072
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1077..1082
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1085..1101
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1103..1127
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1130..1133
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1135..1176
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1178..1184
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1187..1235
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1242..1257
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1260..1283
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1295..1297
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1302..1304
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1318..1320
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1343..1346
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1349..1355
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1366..1368
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1371..1376
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1378..1382
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 1399..1402
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1408..1413
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1417..1422
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1426..1429
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1443..1460
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1476..1488
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 1489..1491
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1511..1514
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1516..1519
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 1521..1524
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1527..1533
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 1535..1540
FT /evidence="ECO:0007829|PDB:7MIT"
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
