FEOB_ECOLI
ID FEOB_ECOLI Reviewed; 773 AA.
AC P33650; Q2M774; Q6IU42;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fe(2+) transporter FeoB {ECO:0000305};
DE AltName: Full=Ferrous iron transport protein B;
GN Name=feoB; OrderedLocusNames=b3409, JW3372;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=8407793; DOI=10.1128/jb.175.19.6212-6219.1993;
RA Kammler M., Schoen C., Hantke K.;
RT "Characterization of the ferrous iron uptake system of Escherichia coli.";
RL J. Bacteriol. 175:6212-6219(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 536-704.
RC STRAIN=B / Bc251;
RX PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA Lenski R.E., Winkworth C.L., Riley M.A.;
RT "Rates of DNA sequence evolution in experimental populations of Escherichia
RT coli during 20,000 generations.";
RL J. Mol. Evol. 56:498-508(2003).
RN [5]
RP FUNCTION, GTP-BINDING SITES, INDUCTION, DOMAIN, AND MUTAGENESIS OF ASP-94
RP AND ASP-123.
RX PubMed=12446835; DOI=10.1073/pnas.242338299;
RA Marlovits T.C., Haase W., Herrmann C., Aller S.G., Unger V.M.;
RT "The membrane protein FeoB contains an intramolecular G protein essential
RT for Fe(II) uptake in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16243-16248(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [8]
RP FUNCTION, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=23104801; DOI=10.1128/jb.01121-12;
RA Lau C.K., Ishida H., Liu Z., Vogel H.J.;
RT "Solution structure of Escherichia coli FeoA and its potential role in
RT bacterial ferrous iron transport.";
RL J. Bacteriol. 195:46-55(2013).
RN [9] {ECO:0007744|PDB:3HYR, ECO:0007744|PDB:3HYT}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-270 WITH AND WITHOUT GTP
RP ANALOG, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF SER-150 AND ARG-154.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19629046; DOI=10.1038/emboj.2009.208;
RA Guilfoyle A., Maher M.J., Rapp M., Clarke R., Harrop S., Jormakka M.;
RT "Structural basis of GDP release and gating in G protein coupled Fe2+
RT transport.";
RL EMBO J. 28:2677-2685(2009).
RN [10] {ECO:0007744|PDB:3I8S, ECO:0007744|PDB:3I8X, ECO:0007744|PDB:3I92}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-274, AND SUBUNIT.
RA Petermann N., Schmidt C.L., Hansen G., Wagner A.K., Hilgenfeld R., Hogg T.;
RT "Structural basis for the intrinsic GTPase and GDI activities of FeoB, a
RT prokaryotic transmembrane GTP/GDP-binding protein.";
RL Submitted (JUL-2009) to the PDB data bank.
RN [11] {ECO:0007744|PDB:4R98}
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF HYBRID MUTANT 1-270, FUNCTION,
RP AND MUTAGENESIS OF 150-SER--ALA-158.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25517170; DOI=10.1016/j.bpj.2014.10.064;
RA Guilfoyle A.P., Deshpande C.N., Font Sadurni J., Ash M.R., Tourle S.,
RA Schenk G., Maher M.J., Jormakka M.;
RT "A GTPase chimera illustrates an uncoupled nucleotide affinity and release
RT rate, providing insight into the activation mechanism.";
RL Biophys. J. 107:L45-L48(2014).
RN [12] {ECO:0007744|PDB:4Q00, ECO:0007744|PDB:4Q5I}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-261 MUTANT ALA-150, X-RAY
RP CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-261 MUTANT ALA-151, FUNCTION,
RP SUBUNIT, AND MUTAGENESIS OF SER-150; THR-151; ARG-152; GLY-153 AND ARG-154.
RX PubMed=25374115; DOI=10.1042/bsr20140152;
RA Guilfoyle A.P., Deshpande C.N., Schenk G., Maher M.J., Jormakka M.;
RT "Exploring the correlation between the sequence composition of the
RT nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic
RT rate of GDP release.";
RL Biosci. Rep. 34:E00158-E00158(2014).
CC -!- FUNCTION: Transporter of a GTP-driven Fe(2+) uptake system, probably
CC couples GTP-binding to channel opening and Fe(2+) uptake
CC (PubMed:12446835, PubMed:19629046). A guanine nucleotide-binding
CC protein (G proteins) in which the guanine nucleotide binding site
CC alternates between an active, GTP-bound state and an inactive, GDP-
CC bound state. This protein has fast intrinsic GDP release, mediated by
CC the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads
CC to conformational changes and channel closing (PubMed:19629046). A GDP
CC release mechanism involving a conformational change of the G5 loop (and
CC thus the removal of the nucleotide-binding and stabilizing
CC interactions) would significantly reduce the affinity for GDP, and
CC conceivably be sufficient for catalysing nucleotide release
CC (PubMed:25374115). {ECO:0000269|PubMed:12446835,
CC ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:23104801,
CC ECO:0000269|PubMed:25374115, ECO:0000269|PubMed:25517170,
CC ECO:0000269|PubMed:8407793}.
CC -!- SUBUNIT: The isolated N-terminal domain (residues 1-274) forms trimers
CC (PubMed:19629046, Ref.10,PubMed:25374115).
CC {ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:25374115,
CC ECO:0000269|Ref.10}.
CC -!- INTERACTION:
CC P33650; P33650: feoB; NbExp=5; IntAct=EBI-7131497, EBI-7131497;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
CC -!- INDUCTION: Iron uptake is repressed by the global regulator Fur in
CC presence of Fe(2+) (PubMed:12446835). Induced by hydroxyurea
CC (PubMed:20005847). {ECO:0000269|PubMed:12446835,
CC ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: Contains a guanine-nucleotide-specific nucleotide-binding site
CC (about residues 1-276) that shows slow GTP hydrolysis (PubMed:12446835,
CC PubMed:23104801). When a non-hydrolyzable GTP analog binds to the
CC trimeric N-terminal domain, it induces a structural shift which opens a
CC pore (PubMed:19629046). {ECO:0000269|PubMed:12446835,
CC ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:23104801}.
CC -!- DISRUPTION PHENOTYPE: Poor uptake of Fe(2+).
CC {ECO:0000269|PubMed:8407793}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. FeoB GTPase (TC 9.A.8) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01048}.
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DR EMBL; X71063; CAA50387.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58207.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76434.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77882.1; -; Genomic_DNA.
DR EMBL; AY625107; AAT42461.1; -; Genomic_DNA.
DR PIR; A36932; A36932.
DR RefSeq; NP_417868.1; NC_000913.3.
DR RefSeq; WP_000737039.1; NZ_SSZK01000008.1.
DR PDB; 3HYR; X-ray; 2.20 A; A/B/C=1-270.
DR PDB; 3HYT; X-ray; 2.74 A; A/B/C=1-270.
DR PDB; 3I8S; X-ray; 1.80 A; A/B/C=1-274.
DR PDB; 3I8X; X-ray; 2.25 A; A/B/C=1-274.
DR PDB; 3I92; X-ray; 3.00 A; A/B/C=1-274.
DR PDB; 4Q00; X-ray; 2.10 A; A/B/C=1-261.
DR PDB; 4Q5I; X-ray; 2.80 A; A/B/C/D/E/F=1-270.
DR PDB; 4R98; X-ray; 2.22 A; A/B=1-270.
DR PDBsum; 3HYR; -.
DR PDBsum; 3HYT; -.
DR PDBsum; 3I8S; -.
DR PDBsum; 3I8X; -.
DR PDBsum; 3I92; -.
DR PDBsum; 4Q00; -.
DR PDBsum; 4Q5I; -.
DR PDBsum; 4R98; -.
DR AlphaFoldDB; P33650; -.
DR SMR; P33650; -.
DR BioGRID; 4261727; 49.
DR BioGRID; 852228; 1.
DR DIP; DIP-9591N; -.
DR MINT; P33650; -.
DR STRING; 511145.b3409; -.
DR TCDB; 9.A.8.1.1; the ferrous iron uptake (feob) family.
DR jPOST; P33650; -.
DR PaxDb; P33650; -.
DR PRIDE; P33650; -.
DR EnsemblBacteria; AAC76434; AAC76434; b3409.
DR EnsemblBacteria; BAE77882; BAE77882; BAE77882.
DR GeneID; 947919; -.
DR KEGG; ecj:JW3372; -.
DR KEGG; eco:b3409; -.
DR PATRIC; fig|1411691.4.peg.3320; -.
DR EchoBASE; EB2026; -.
DR eggNOG; COG0370; Bacteria.
DR HOGENOM; CLU_013350_3_0_6; -.
DR InParanoid; P33650; -.
DR OMA; MEMPDYE; -.
DR PhylomeDB; P33650; -.
DR BioCyc; EcoCyc:FEOB-MON; -.
DR BioCyc; MetaCyc:FEOB-MON; -.
DR EvolutionaryTrace; P33650; -.
DR PRO; PR:P33650; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IMP:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:EcoCyc.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IDA:EcoCyc.
DR CDD; cd01879; FeoB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003373; Fe2_transport_prot-B.
DR InterPro; IPR011640; Fe2_transport_prot_B_C.
DR InterPro; IPR041069; FeoB_Cyto.
DR InterPro; IPR030389; G_FEOB_dom.
DR InterPro; IPR011642; Gate_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07664; FeoB_C; 1.
DR Pfam; PF17910; FeoB_Cyto; 1.
DR Pfam; PF02421; FeoB_N; 1.
DR Pfam; PF07670; Gate; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00437; feoB; 1.
DR PROSITE; PS51711; G_FEOB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; GTP-binding;
KW Ion transport; Iron; Iron transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..773
FT /note="Fe(2+) transporter FeoB"
FT /id="PRO_0000210821"
FT TOPO_DOM 1..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..308
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..382
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..452
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..663
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..721
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 3..169
FT /note="FeoB-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT REGION 1..274
FT /note="NFeoB, GTPase protein domain, binds GTP but not ATP"
FT /evidence="ECO:0000269|PubMed:12446835,
FT ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:23104801,
FT ECO:0000269|PubMed:25374115, ECO:0000269|PubMed:25517170"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19629046"
FT BINDING 35..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 56..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19629046, ECO:0000305|PubMed:12446835"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01048,
FT ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:25374115,
FT ECO:0000305"
FT MUTAGEN 94
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:12446835"
FT MUTAGEN 123
FT /note="D->N: Loss of guanine nucleotide-binding specificity
FT and Fe(2+) uptake."
FT /evidence="ECO:0000269|PubMed:12446835"
FT MUTAGEN 150..158
FT /note="STRGRGIEA->ATDTKNVQFV: 10-fold reduced affinity for
FT GDP, corresponds to the G5 loop of human GNAI1, a slow GDP-
FT releasing protein, in construct of residues 1-270."
FT /evidence="ECO:0000269|PubMed:25517170"
FT MUTAGEN 150
FT /note="S->A: Dramatically reduced GDP release-rate, 5-fold
FT increase in affinity for GDP, in construct of residues 1-
FT 270. GTP hydrolysis rate 1.5-fold higher than wild-type."
FT /evidence="ECO:0000269|PubMed:19629046,
FT ECO:0000269|PubMed:25374115"
FT MUTAGEN 151
FT /note="T->A: GTP hydrolysis rate 4-fold slower than wild-
FT type, releases GDP very quickly."
FT /evidence="ECO:0000269|PubMed:25374115"
FT MUTAGEN 152
FT /note="R->A: GTP hydrolysis rate 1.3-fold slower than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:25374115"
FT MUTAGEN 153
FT /note="G->A: GTP hydrolysis rate 1.8-fold slower than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:25374115"
FT MUTAGEN 154
FT /note="R->A: Dramatically reduced GDP release-rate, in
FT construct of residues 1-270. GTP hydrolysis rate 2.7-fold
FT slower than wild-type."
FT /evidence="ECO:0000269|PubMed:19629046,
FT ECO:0000269|PubMed:25374115"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:3I8S"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:3I8S"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3I8S"
SQ SEQUENCE 773 AA; 84474 MW; 1150A14B131AB9AE CRC64;
MKKLTIGLIG NPNSGKTTLF NQLTGSRQRV GNWAGVTVER KEGQFSTTDH QVTLVDLPGT
YSLTTISSQT SLDEQIACHY ILSGDADLLI NVVDASNLER NLYLTLQLLE LGIPCIVALN
MLDIAEKQNI RIEIDALSAR LGCPVIPLVS TRGRGIEALK LAIDRYKANE NVELVHYAQP
LLNEADSLAK VMPSDIPLKQ RRWLGLQMLE GDIYSRAYAG EASQHLDAAL ARLRNEMDDP
ALHIADARYQ CIAAICDVVS NTLTAEPSRF TTAVDKIVLN RFLGLPIFLF VMYLMFLLAI
NIGGALQPLF DVGSVALFVH GIQWIGYTLH FPDWLTIFLA QGLGGGINTV LPLVPQIGMM
YLFLSFLEDS GYMARAAFVM DRLMQALGLP GKSFVPLIVG FGCNVPSVMG ARTLDAPRER
LMTIMMAPFM SCGARLAIFA VFAAAFFGQN GALAVFSLYM LGIVMAVLTG LMLKYTIMRG
EATPFVMELP VYHVPHVKSL IIQTWQRLKG FVLRAGKVII IVSIFLSAFN SFSLSGKIVD
NINDSALASV SRVITPVFKP IGVHEDNWQA TVGLFTGAMA KEVVVGTLNT LYTAENIQDE
EFNPAEFNLG EELFSAIDET WQSLKDTFSL SVLMNPIEAS KGDGEMGTGA MGVMDQKFGS
AAAAYSYLIF VLLYVPCISV MGAIARESSR GWMGFSILWG LNIAYSLATL FYQVASYSQH
PTYSLVCILA VILFNIVVIG LLRRARSRVD IELLATRKSV SSCCAASTTG DCH
