FNR_ECOLI
ID FNR_ECOLI Reviewed; 250 AA.
AC P0A9E5; P03019;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Fumarate and nitrate reduction regulatory protein;
GN Name=fnr; Synonyms=nirR; OrderedLocusNames=b1334, JW1328;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6292868; DOI=10.1093/nar/10.19.6119;
RA Shaw D.J., Guest J.R.;
RT "Nucleotide sequence of the fnr gene and primary structure of the Enr
RT protein of Escherichia coli.";
RL Nucleic Acids Res. 10:6119-6130(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 PROTEIN SEQUENCE OF 1-19, AND SEQUENCE REVISION TO 29.
RX PubMed=2181237; DOI=10.1111/j.1365-2958.1990.tb02011.x;
RA Trageser M., Spiro S., Duchene A., Kojro E., Fahrenholz F., Guest J.R.,
RA Unden G.;
RT "Isolation of intact FNR protein (Mr 30,000) of Escherichia coli.";
RL Mol. Microbiol. 4:21-27(1990).
RN [6]
RP CHARACTERIZATION, AND MUTAGENESIS OF ASP-154.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8406003; DOI=10.1101/gad.7.10.1993;
RA Lazazzera B.A., Bates D.M., Kiley P.J.;
RT "The activity of the Escherichia coli transcription factor FNR is regulated
RT by a change in oligomeric state.";
RL Genes Dev. 7:1993-2005(1993).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=B;
RX PubMed=9177174; DOI=10.1073/pnas.94.12.6087;
RA Khoroshilova N., Popescu C., Muenck E., Beinert H., Kiley P.J.;
RT "Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by
RT O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6087-6092(1997).
RN [8]
RP CHARACTERIZATION, AND MUTAGENESIS.
RX PubMed=11251837; DOI=10.1111/j.1365-2958.2001.02326.x;
RA Ralph E.T., Scott C., Jordan P.A., Thomson A.J., Guest J.R., Green J.;
RT "Anaerobic acquisition of [4FE 4S] clusters by the inactive FNR(C20S)
RT variant and restoration of activity by second-site amino acid
RT substitutions.";
RL Mol. Microbiol. 39:1199-1211(2001).
RN [9]
RP MASS SPECTROMETRY, AND CHARACTERIZATION OF MUTANTS.
RX PubMed=8497198; DOI=10.1111/j.1365-2958.1993.tb01203.x;
RA Green J., Sharrocks A.D., Green B., Geisow M., Guest J.R.;
RT "Properties of FNR proteins substituted at each of the five cysteine
RT residues.";
RL Mol. Microbiol. 8:61-68(1993).
RN [10]
RP MUTAGENESIS OF CYS-16; CYS-20; CYS-23; CYS-29; GLU-64; GLY-96 AND CYS-122.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2226775; DOI=10.1016/0014-5793(90)81248-m;
RA Sharrocks A.D., Green J., Guest J.R.;
RT "In vivo and in vitro mutants of FNR the anaerobic transcriptional
RT regulator of E. coli.";
RL FEBS Lett. 270:119-122(1990).
RN [11]
RP MUTAGENESIS OF ASP-22; LEU-28; HIS-93; GLU-150 AND ASP-154.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1898918; DOI=10.1128/jb.173.1.16-22.1991;
RA Kiley P.J., Reznikoff W.S.;
RT "Fnr mutants that activate gene expression in the presence of oxygen.";
RL J. Bacteriol. 173:16-22(1991).
RN [12]
RP MUTAGENESIS OF ILE-81; THR-82; GLY-85; ASP-86; GLU-87 AND GLN-88.
RX PubMed=1762901; DOI=10.1093/nar/19.24.6705;
RA Williams R., Bell A., Sims G., Busby S.J.W.;
RT "The role of two surface exposed loops in transcription activation by the
RT Escherichia coli CRP and FNR proteins.";
RL Nucleic Acids Res. 19:6705-6712(1991).
RN [13]
RP MUTAGENESIS OF ASP-43; ARG-72; SER-73; GLY-74; THR-118; MET-120; PHE-181;
RP PHE-186; SER-187 AND PHE-191.
RX PubMed=9321653; DOI=10.1093/nar/25.20.4028;
RA Williams S.M., Savery N.J., Busby S.J.W., Wing H.J.;
RT "Transcription activation at class I FNR-dependent promoters:
RT identification of the activating surface of FNR and the corresponding
RT contact site in the C-terminal domain of the RNA polymerase alpha
RT subunit.";
RL Nucleic Acids Res. 25:4028-4034(1997).
RN [14]
RP MUTAGENESIS OF SER-73; GLY-85; THR-118 AND SER-187.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11115116; DOI=10.1046/j.1365-2958.2000.02172.x;
RA Lamberg K.E., Kiley P.J.;
RT "FNR-dependent activation of the class II dmsA and narG promoters of
RT Escherichia coli requires FNR-activating regions 1 and 3.";
RL Mol. Microbiol. 38:817-827(2000).
RN [15]
RP MUTAGENESIS OF ALL RESIDUES IN THE DIMERIZATION HELIX.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11581261; DOI=10.1074/jbc.m106569200;
RA Moore L.J., Kiley P.J.;
RT "Characterization of the dimerization domain in the FNR transcription
RT factor.";
RL J. Biol. Chem. 276:45744-45750(2001).
RN [16]
RP REVIEW.
RX PubMed=2248796; DOI=10.1111/j.1574-6968.1990.tb04109.x;
RA Spiro S., Guest J.R.;
RT "FNR and its role in oxygen-regulated gene expression in Escherichia
RT coli.";
RL FEMS Microbiol. Rev. 6:399-428(1990).
RN [17]
RP REVIEW.
RX PubMed=9990723; DOI=10.1111/j.1574-6976.1998.tb00375.x;
RA Kiley P.J., Beinert H.;
RT "Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur
RT cluster.";
RL FEMS Microbiol. Rev. 22:341-352(1998).
RN [18]
RP REVIEW.
RX PubMed=11407111; DOI=10.1016/s0065-2911(01)44010-0;
RA Green J., Scott C., Guest J.R.;
RT "Functional versatility in the CRP-FNR superfamily of transcription
RT factors: FNR and FLP.";
RL Adv. Microb. Physiol. 44:1-34(2001).
CC -!- FUNCTION: Global transcription factor that controls the expression of
CC over 100 target genes in response to anoxia. It facilitates the
CC adaptation to anaerobic growth conditions by regulating the expression
CC of gene products that are involved in anaerobic energy metabolism. When
CC the terminal electron acceptor, O(2), is no longer available, it
CC represses the synthesis of enzymes involved in aerobic respiration and
CC increases the synthesis of enzymes required for anaerobic respiration.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The amino acid residues contacting the FNR target site on the
CC DNA (5'-TTGATNNNNATCAA-3') are located in the putative DNA-recognition
CC helix (alphaF), which contains the FNR motif (EXXSR). Three surface-
CC exposed loops forming activating region 1 (AR1) in the downstream
CC subunit of the dimer contact the C-terminal domain of the alpha subunit
CC (alphaCTD) of RNA polymerase for activation of class I promoters (the
CC 161-121 loop is the major AR1 activating determinant). At class II
CC promoters, the AR1 of the upstream subunit contacts alphaCTD, promoting
CC open complex formation; activating region 3 (AR3) of the downstream
CC subunit contacts region 4 of the sigma70 subunit of RNA polymerase, to
CC effect direct activation. At promoters repressed by FNR, tandem FNR
CC dimers might interact with each other at AR1 to restrict access to a
CC promoter or jam the promoter by their dual interaction with RNA
CC polymerase alphaCTD.
CC -!- MASS SPECTROMETRY: Mass=26823; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8497198};
CC -!- MISCELLANEOUS: FNR senses the oxygen concentration directly via the
CC disassembly and reassembly of the [4Fe-4S] clusters. Anaerobic, de novo
CC acquisition of the iron-sulfur cluster converts monomeric, inactive
CC apo-FNR into a dimeric form containing two [4Fe-4S] clusters. This, in
CC turn, enhances the affinity of FNR for specific DNA targets and
CC mediates transcription regulation by establishing direct FNR-RNA
CC polymerase contacts. With the increase in intracellular oxygen
CC concentration, the [4Fe-4S] cluster is oxidized, producing a [2Fe-2S]
CC cluster, which decays to apo-FNR. Apo-FNR [4SH] can be reversibly
CC oxidized to a disulfide form [2SH,S-S], suggesting that FNR may be able
CC to sense oxidative stress as well as normoxia. This interconversion may
CC be mediated by agents such as glutathione or thioredoxin.
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DR EMBL; J01608; AAA87981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC74416.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14927.1; -; Genomic_DNA.
DR PIR; A64883; RGECF.
DR RefSeq; NP_415850.1; NC_000913.3.
DR RefSeq; WP_000611911.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P0A9E5; -.
DR SMR; P0A9E5; -.
DR BioGRID; 4261852; 11.
DR BioGRID; 850273; 2.
DR DIP; DIP-9669N; -.
DR IntAct; P0A9E5; 8.
DR STRING; 511145.b1334; -.
DR jPOST; P0A9E5; -.
DR PaxDb; P0A9E5; -.
DR PRIDE; P0A9E5; -.
DR EnsemblBacteria; AAC74416; AAC74416; b1334.
DR EnsemblBacteria; BAA14927; BAA14927; BAA14927.
DR GeneID; 66674838; -.
DR GeneID; 945908; -.
DR KEGG; ecj:JW1328; -.
DR KEGG; eco:b1334; -.
DR PATRIC; fig|1411691.4.peg.943; -.
DR EchoBASE; EB0321; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_0_2_6; -.
DR InParanoid; P0A9E5; -.
DR OMA; AEVCVMP; -.
DR PhylomeDB; P0A9E5; -.
DR BioCyc; EcoCyc:PD00197; -.
DR PHI-base; PHI:4876; -.
DR PHI-base; PHI:7248; -.
DR PRO; PR:P0A9E5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_000007e0; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP:EcoCyc.
DR GO; GO:0071731; P:response to nitric oxide; IEP:EcoCyc.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00325; Crp; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00042; HTH_CRP_1; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Activator; Cytoplasm; Direct protein sequencing; DNA-binding; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..250
FT /note="Fumarate and nitrate reduction regulatory protein"
FT /id="PRO_0000100161"
FT DOMAIN 164..237
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 197..216
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT REGION 20..29
FT /note="Essential for the oxygen-regulated activity"
FT REGION 47..50
FT /note="Activating region 2A"
FT /evidence="ECO:0000255"
FT REGION 60..61
FT /note="Activating region 3A"
FT /evidence="ECO:0000255"
FT REGION 71..75
FT /note="Activating region 1A"
FT /evidence="ECO:0000255"
FT REGION 81
FT /note="Activating region 3B"
FT /evidence="ECO:0000255"
FT REGION 85..87
FT /note="Activating region 3C"
FT /evidence="ECO:0000255"
FT REGION 112
FT /note="Activating region 3D"
FT /evidence="ECO:0000255"
FT REGION 116..121
FT /note="Activating region 1B"
FT /evidence="ECO:0000255"
FT REGION 123..124
FT /note="Activating region 2B"
FT /evidence="ECO:0000255"
FT REGION 127..128
FT /note="Activating region 2C"
FT /evidence="ECO:0000255"
FT REGION 140..159
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 181..191
FT /note="Activating region 1C"
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MUTAGEN 16
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 20
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 22
FT /note="D->G: Loss of regulation by O(2)."
FT /evidence="ECO:0000269|PubMed:1898918"
FT MUTAGEN 23
FT /note="C->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 28
FT /note="L->H: Loss of regulation by O(2)."
FT /evidence="ECO:0000269|PubMed:1898918"
FT MUTAGEN 29
FT /note="C->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 43
FT /note="D->G: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
FT MUTAGEN 64
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 72
FT /note="R->H: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
FT MUTAGEN 73
FT /note="S->F: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:11115116,
FT ECO:0000269|PubMed:9321653"
FT MUTAGEN 81
FT /note="I->T: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:1762901"
FT MUTAGEN 82
FT /note="T->P: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:1762901"
FT MUTAGEN 85
FT /note="G->A: Decrease in activity; no effect on DNA-
FT binding. Trace activity; when associated with P-187."
FT /evidence="ECO:0000269|PubMed:11115116,
FT ECO:0000269|PubMed:1762901"
FT MUTAGEN 86
FT /note="D->A: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:1762901"
FT MUTAGEN 87
FT /note="E->K: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:1762901"
FT MUTAGEN 88
FT /note="Q->E: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:1762901"
FT MUTAGEN 93
FT /note="H->R: Loss of regulation by O(2)."
FT /evidence="ECO:0000269|PubMed:1898918"
FT MUTAGEN 96
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 118
FT /note="T->A,P: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:11115116,
FT ECO:0000269|PubMed:9321653"
FT MUTAGEN 120
FT /note="M->I,R,T,V: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
FT MUTAGEN 122
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2226775"
FT MUTAGEN 140
FT /note="R->A: Decrease in activity."
FT MUTAGEN 143
FT /note="M->A: Decrease in activity."
FT MUTAGEN 144
FT /note="M->A: Decrease in activity due to faulty
FT dimerization."
FT MUTAGEN 145
FT /note="R->A: Decrease in activity."
FT MUTAGEN 146
FT /note="L->A: Decrease in activity."
FT MUTAGEN 147
FT /note="M->A: Decrease in activity due to faulty
FT dimerization."
FT MUTAGEN 150
FT /note="E->K: Loss of regulation by O(2)."
FT /evidence="ECO:0000269|PubMed:1898918"
FT MUTAGEN 151
FT /note="I->A: Decrease in activity due to faulty
FT dimerization."
FT MUTAGEN 154
FT /note="D->A,G,V: Loss of regulation by O(2)."
FT /evidence="ECO:0000269|PubMed:1898918,
FT ECO:0000269|PubMed:8406003"
FT MUTAGEN 158
FT /note="I->A: Decrease in activity due to faulty
FT dimerization."
FT MUTAGEN 181
FT /note="F->L: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
FT MUTAGEN 186
FT /note="F->S: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
FT MUTAGEN 187
FT /note="S->P: Decrease in activity; no effect on DNA-
FT binding. Trace activity; when associated with A-85."
FT /evidence="ECO:0000269|PubMed:11115116,
FT ECO:0000269|PubMed:9321653"
FT MUTAGEN 191
FT /note="F->L: Decrease in activity; no effect on DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:9321653"
SQ SEQUENCE 250 AA; 27967 MW; 33F7BFA2972FF703 CRC64;
MIPEKRIIRR IQSGGCAIHC QDCSISQLCI PFTLNEHELD QLDNIIERKK PIQKGQTLFK
AGDELKSLYA IRSGTIKSYT ITEQGDEQIT GFHLAGDLVG FDAIGSGHHP SFAQALETSM
VCEIPFETLD DLSGKMPNLR QQMMRLMSGE IKGDQDMILL LSKKNAEERL AAFIYNLSRR
FAQRGFSPRE FRLTMTRGDI GNYLGLTVET ISRLLGRFQK SGMLAVKGKY ITIENNDALA
QLAGHTRNVA
