ID CUSA_ECOLI Reviewed; 1047 AA. AC P38054; P77767; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 24-JAN-2024, entry version 175. DE RecName: Full=Cation efflux system protein CusA; GN Name=cusA; Synonyms=ybdE; OrderedLocusNames=b0575, JW0564; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 871-1047. RC STRAIN=K12; RX PubMed=1711024; DOI=10.1128/jb.173.12.3622-3629.1991; RA Pi J., Wookey P.J., Pittard A.J.; RT "Cloning and sequencing of the pheP gene, which encodes the phenylalanine- RT specific transport system of Escherichia coli."; RL J. Bacteriol. 173:3622-3629(1991). RN [6] RP IDENTIFICATION. RX PubMed=7984428; DOI=10.1093/nar/22.22.4756; RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial RT genome."; RL Nucleic Acids Res. 22:4756-4767(1994). RN [7] RP GENE NAME. RC STRAIN=K12 / DH5-alpha; RX PubMed=11004187; DOI=10.1128/jb.182.20.5864-5871.2000; RA Munson G.P., Lam D.L., Outten F.W., O'Halloran T.V.; RT "Identification of a copper-responsive two-component system on the RT chromosome of Escherichia coli K-12."; RL J. Bacteriol. 182:5864-5871(2000). RN [8] RP FUNCTION IN COPPER HOMEOSTASIS. RC STRAIN=K12; RX PubMed=11399769; DOI=10.1074/jbc.m104122200; RA Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.; RT "The independent cue and cus systems confer copper tolerance during aerobic RT and anaerobic growth in Escherichia coli."; RL J. Biol. Chem. 276:30670-30677(2001). RN [9] RP INDUCTION. RC STRAIN=K38; RX PubMed=11283292; DOI=10.1099/00221287-147-4-965; RA Franke S., Grass G., Nies D.H.; RT "The product of the ybdE gene of the Escherichia coli chromosome is RT involved in detoxification of silver ions."; RL Microbiology 147:965-972(2001). RN [10] RP FUNCTION, AND MUTAGENESIS OF ALA-399; ASP-405; GLU-412; MET-573; MET-623; RP MET-640; MET-672; MET-738; MET-755; MET-792; MET-812 AND MET-833. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=12813074; DOI=10.1128/jb.185.13.3804-3812.2003; RA Franke S., Grass G., Rensing C., Nies D.H.; RT "Molecular analysis of the copper-transporting efflux system CusCFBA of RT Escherichia coli."; RL J. Bacteriol. 185:3804-3812(2003). CC -!- FUNCTION: Part of a cation efflux system that mediates resistance to CC copper and silver. {ECO:0000269|PubMed:11399769, CC ECO:0000269|PubMed:12813074}. CC -!- SUBUNIT: The cus efflux system is composed of CusA, CusB, CusC and CC CusF. CC -!- INTERACTION: CC P38054; P77239: cusB; NbExp=2; IntAct=EBI-1126317, EBI-1118842; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- INDUCTION: Transcriptionally regulated by CusR in response to copper CC and silver ions. {ECO:0000269|PubMed:11283292}. CC -!- MISCELLANEOUS: The cus system plays an important role in copper CC tolerance under anaerobic growth and, under extreme copper stress, in CC aerobic growth. CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND) CC (TC 2.A.6) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=M58000; Type=Frameshift; Evidence={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; U82598; AAB40773.1; -; Genomic_DNA. DR EMBL; U00096; AAC73676.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35215.1; -; Genomic_DNA. DR EMBL; M58000; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; E64790; E64790. DR RefSeq; NP_415107.1; NC_000913.3. DR RefSeq; WP_000573945.1; NZ_SSZK01000024.1. DR PDB; 3K07; X-ray; 3.52 A; A=1-1047. DR PDB; 3K0I; X-ray; 4.12 A; A=1-1047. DR PDB; 3KSO; X-ray; 4.37 A; A=1-1047. DR PDB; 3KSS; X-ray; 3.88 A; A=1-1047. DR PDB; 3NE5; X-ray; 2.90 A; A=2-1047. DR PDB; 3T51; X-ray; 3.90 A; A=1-1047. DR PDB; 3T53; X-ray; 3.37 A; A=1-1047. DR PDB; 3T56; X-ray; 3.42 A; A=1-1047. DR PDB; 4DNR; X-ray; 3.68 A; A=1-1047. DR PDB; 4DNT; X-ray; 3.10 A; A=1-1047. DR PDB; 4DOP; X-ray; 4.20 A; A=1-1047. DR PDB; 7KF5; EM; 3.20 A; A/B/C=1-1047. DR PDB; 7KF6; EM; 3.40 A; A/B/C=1-1047. DR PDB; 7KF7; EM; 2.80 A; A/B/C=1-1047. DR PDB; 7KF8; EM; 3.00 A; A/B/C=1-1047. DR PDBsum; 3K07; -. DR PDBsum; 3K0I; -. DR PDBsum; 3KSO; -. DR PDBsum; 3KSS; -. DR PDBsum; 3NE5; -. DR PDBsum; 3T51; -. DR PDBsum; 3T53; -. DR PDBsum; 3T56; -. DR PDBsum; 4DNR; -. DR PDBsum; 4DNT; -. DR PDBsum; 4DOP; -. DR PDBsum; 7KF5; -. DR PDBsum; 7KF6; -. DR PDBsum; 7KF7; -. DR PDBsum; 7KF8; -. DR AlphaFoldDB; P38054; -. DR EMDB; EMD-22843; -. DR EMDB; EMD-22844; -. DR EMDB; EMD-22845; -. DR EMDB; EMD-22846; -. DR SMR; P38054; -. DR BioGRID; 4260908; 278. DR ComplexPortal; CPX-2254; Cus cation efflux complex. DR DIP; DIP-9345N; -. DR IntAct; P38054; 5. DR STRING; 511145.b0575; -. DR TCDB; 2.A.6.1.4; the resistance-nodulation-cell division (rnd) superfamily. DR PaxDb; 511145-b0575; -. DR EnsemblBacteria; AAC73676; AAC73676; b0575. DR GeneID; 945191; -. DR KEGG; ecj:JW0564; -. DR KEGG; eco:b0575; -. DR PATRIC; fig|1411691.4.peg.1699; -. DR EchoBASE; EB2270; -. DR eggNOG; COG3696; Bacteria. DR HOGENOM; CLU_002755_1_2_6; -. DR InParanoid; P38054; -. DR OMA; NSWTYPI; -. DR OrthoDB; 9758757at2; -. DR PhylomeDB; P38054; -. DR BioCyc; EcoCyc:YBDE-MONOMER; -. DR BioCyc; MetaCyc:YBDE-MONOMER; -. DR EvolutionaryTrace; P38054; -. DR PRO; PR:P38054; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; IDA:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0005507; F:copper ion binding; IGI:EcoCyc. DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IGI:EcoCyc. DR GO; GO:0015080; F:silver ion transmembrane transporter activity; IMP:EcoCyc. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0060003; P:copper ion export; IGI:EcoCyc. DR GO; GO:0035434; P:copper ion transmembrane transport; NAS:ComplexPortal. DR GO; GO:0010273; P:detoxification of copper ion; IGI:EcoCyc. DR GO; GO:0006878; P:intracellular copper ion homeostasis; IGI:EcoCyc. DR GO; GO:0015679; P:plasma membrane copper ion transport; IGI:EcoCyc. DR GO; GO:0046688; P:response to copper ion; IMP:EcoliWiki. DR GO; GO:0010272; P:response to silver ion; IMP:EcoCyc. DR GO; GO:0009636; P:response to toxic substance; NAS:ComplexPortal. DR GO; GO:1902601; P:silver ion transmembrane transport; NAS:ComplexPortal. DR GO; GO:0015673; P:silver ion transport; IMP:EcoCyc. DR Gene3D; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2. DR Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 1. DR Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR027463; AcrB_DN_DC_subdom. DR InterPro; IPR001036; Acrflvin-R. DR InterPro; IPR004763; CusA-like. DR NCBIfam; TIGR00914; 2A0601; 1. DR PANTHER; PTHR32063; -; 1. DR PANTHER; PTHR32063:SF19; CATION EFFLUX SYSTEM PROTEIN CUSA; 1. DR Pfam; PF00873; ACR_tran; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Copper; Copper transport; KW Ion transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1047 FT /note="Cation efflux system protein CusA" FT /id="PRO_0000161815" FT TRANSMEM 14..34 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 338..358 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 363..383 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 391..411 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 446..466 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 485..505 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 532..552 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 871..891 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 898..918 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 928..948 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 985..1005 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1012..1032 FT /note="Helical" FT /evidence="ECO:0000255" FT MUTAGEN 399 FT /note="A->D: Strong decrease in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 405 FT /note="D->N: Loss of copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 412 FT /note="E->D: Slight decrease in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 412 FT /note="E->Q: Loss of copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 573 FT /note="M->I: Loss of copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 623 FT /note="M->I: Loss of copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 640 FT /note="M->I: No change in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 672 FT /note="M->I: Loss of copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 738 FT /note="M->I: No change in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 755 FT /note="M->I: Slight decrease in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 792 FT /note="M->I: No change in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 812 FT /note="M->I: Slight decrease in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT MUTAGEN 833 FT /note="M->I: Slight decrease in copper resistance." FT /evidence="ECO:0000269|PubMed:12813074" FT CONFLICT 897..898 FT /note="AL -> SV (in Ref. 5; M58000)" FT /evidence="ECO:0000305" FT HELIX 7..11 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 13..32 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 66..73 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 88..97 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 103..118 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:3T53" FT HELIX 153..167 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 174..182 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 193..199 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 203..210 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 241..245 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:3NE5" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 285..291 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:3T56" FT HELIX 297..310 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 311..314 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 319..327 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 328..357 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 360..367 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 369..384 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 390..424 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 432..461 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 462..466 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 470..495 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 497..503 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 518..534 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 536..548 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 551..556 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:3T53" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 582..596 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 603..610 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 613..616 FT /evidence="ECO:0007829|PDB:7KF6" FT STRAND 626..629 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 633..635 FT /evidence="ECO:0007829|PDB:3NE5" FT HELIX 642..652 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 658..663 FT /evidence="ECO:0007829|PDB:3T53" FT HELIX 665..674 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 678..688 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 690..704 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 707..709 FT /evidence="ECO:0007829|PDB:7KF6" FT STRAND 712..715 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 721..728 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 730..735 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 740..748 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 749..752 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 758..761 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 764..771 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 774..776 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 777..779 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 780..783 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 787..789 FT /evidence="ECO:0007829|PDB:3NE5" FT STRAND 795..797 FT /evidence="ECO:0007829|PDB:3NE5" FT TURN 799..801 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 802..809 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 813..827 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 829..831 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 833..846 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 854..860 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 861..891 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 894..901 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 904..918 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 921..923 FT /evidence="ECO:0007829|PDB:4DNT" FT HELIX 924..954 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 957..961 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 962..964 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 967..977 FT /evidence="ECO:0007829|PDB:7KF7" FT TURN 978..980 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 982..993 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 996..1000 FT /evidence="ECO:0007829|PDB:7KF7" FT STRAND 1003..1005 FT /evidence="ECO:0007829|PDB:7KF7" FT HELIX 1006..1039 FT /evidence="ECO:0007829|PDB:7KF7" SQ SEQUENCE 1047 AA; 114707 MW; D20BAB10118D4C52 CRC64; MIEWIIRRSV ANRFLVLMGA LFLSIWGTWT IINTPVDALP DLSDVQVIIK TSYPGQAPQI VENQVTYPLT TTMLSVPGAK TVRGFSQFGD SYVYVIFEDG TDPYWARSRV LEYLNQVQGK LPAGVSAELG PDATGVGWIY EYALVDRSGK HDLADLRSLQ DWFLKYELKT IPDVAEVASV GGVVKEYQVV IDPQRLAQYG ISLAEVKSAL DASNQEAGGS SIELAEAEYM VRASGYLQTL DDFNHIVLKA SENGVPVYLR DVAKVQIGPE MRRGIAELNG EGEVAGGVVI LRSGKNAREV IAAVKDKLET LKSSLPEGVE IVTTYDRSQL IDRAIDNLSG KLLEEFIVVA VVCALFLWHV RSALVAIISL PLGLCIAFIV MHFQGLNANI MSLGGIAIAV GAMVDAAIVM IENAHKRLEE WQHQHPDATL DNKTRWQVIT DASVEVGPAL FISLLIITLS FIPIFTLEGQ EGRLFGPLAF TKTYAMAGAA LLAIVVIPIL MGYWIRGKIP PESSNPLNRF LIRVYHPLLL KVLHWPKTTL LVAALSVLTV LWPLNKVGGE FLPQINEGDL LYMPSTLPGI SAAEAASMLQ KTDKLIMSVP EVARVFGKTG KAETATDSAP LEMVETTIQL KPQEQWRPGM TMDKIIEELD NTVRLPGLAN LWVPPIRNRI DMLSTGIKSP IGIKVSGTVL ADIDAMAEQI EEVARTVPGV ASALAERLEG GRYINVEINR EKAARYGMTV ADVQLFVTSA VGGAMVGETV EGIARYPINL RYPQSWRDSP QALRQLPILT PMKQQITLAD VADIKVSTGP SMLKTENARP TSWIYIDARD RDMVSVVHDL QKAIAEKVQL KPGTSVAFSG QFELLERANH KLKLMVPMTL MIIFVLLYLA FRRVGEALLI ISSVPFALVG GIWLLWWMGF HLSVATGTGF IALAGVAAEF GVVMLMYLRH AIEAVPSLNN PQTFSEQKLD EALYHGAVLR VRPKAMTVAV IIAGLLPILW GTGAGSEVMS RIAAPMIGGM ITAPLLSLFI IPAAYKLMWL HRHRVRK //