CUSA_ECOLI
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 03-AUG-2022, entry version 168.
DE RecName: Full=Cation efflux system protein CusA;
GN Name=cusA; Synonyms=ybdE; OrderedLocusNames=b0575, JW0564;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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};
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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 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; P38054; -.
DR PRIDE; P38054; -.
DR EnsemblBacteria; AAC73676; AAC73676; b0575.
DR EnsemblBacteria; BAA35215; BAA35215; BAA35215.
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 PhylomeDB; P38054; -.
DR BioCyc; EcoCyc:YBDE-MON; -.
DR BioCyc; MetaCyc:YBDE-MON; -.
DR EvolutionaryTrace; P38054; -.
DR PRO; PR:P38054; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IC:ComplexPortal.
DR GO; GO:0035434; P:copper ion transmembrane transport; IC:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:1902601; P:silver ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015673; P:silver ion transport; IMP:EcoCyc.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004763; CzcA/CusA/SilA/NccA/HelA/CnrA.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00914; 2A0601; 1.
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
