ID TLR9_BOVIN Reviewed; 1029 AA.
AC Q5I2M5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Toll-like receptor 9;
DE AltName: CD_antigen=CD289;
DE Flags: Precursor;
GN Name=TLR9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=16098606; DOI=10.1016/j.vetimm.2005.07.012;
RA Griebel P.J., Brownlie R., Manuja A., Nichani A., Mookherjee N.,
RA Popowych Y., Mutwiri G., Hecker R., Babiuk L.A.;
RT "Bovine toll-like receptor 9: a comparative analysis of molecular
RT structure, function and expression.";
RL Vet. Immunol. Immunopathol. 108:11-16(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 25-815 IN COMPLEX WITH AGONIST
RP CPG-DNA, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=25686612; DOI=10.1038/nature14138;
RA Ohto U., Shibata T., Tanji H., Ishida H., Krayukhina E., Uchiyama S.,
RA Miyake K., Shimizu T.;
RT "Structural basis of CpG and inhibitory DNA recognition by Toll-like
RT receptor 9.";
RL Nature 520:702-705(2015).
CC -!- FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-
CC like receptors) control host immune response against pathogens through
CC recognition of molecular patterns specific to microorganisms. TLR9 is a
CC nucleotide-sensing TLR which is activated by unmethylated cytidine-
CC phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6,
CC leading to NF-kappa-B activation, cytokine secretion and the
CC inflammatory response. Upon CpG stimulation, induces B-cell
CC proliferation, activation, survival and antibody production (By
CC similarity). {ECO:0000250|UniProtKB:Q9NR96,
CC ECO:0000269|PubMed:25686612}.
CC -!- SUBUNIT: Monomer and homodimer. Exists as a monomer in the absence of
CC unmethylated cytidine-phosphate-guanosine (CpG) ligand. Proteolytic
CC processing of an insertion loop (Z-loop) is required for
CC homodimerization upon binding to the unmethylated CpG ligand leading to
CC its activation (By similarity). Interacts with MYD88 via their
CC respective TIR domains (By similarity). Interacts with BTK (By
CC similarity). Interacts (via transmembrane domain) with UNC93B1.
CC Interacts with CD300LH; the interaction may promote full activation of
CC TLR9-triggered innate responses. Interacts with CNPY3 and HSP90B1; this
CC interaction is required for proper folding in the endoplasmic
CC reticulum. Interacts with SMPDL3B (By similarity).
CC {ECO:0000250|UniProtKB:Q2EEY0, ECO:0000250|UniProtKB:Q9EQU3,
CC ECO:0000250|UniProtKB:Q9NR96}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9EQU3}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9EQU3}. Endosome
CC {ECO:0000250|UniProtKB:Q9EQU3}. Lysosome
CC {ECO:0000250|UniProtKB:Q9EQU3}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9EQU3}. Note=Relocalizes from endoplasmic
CC reticulum to endosome and lysosome upon stimulation with agonist. Exit
CC from the ER requires UNC93B1. Endolysosomal localization is required
CC for proteolytic cleavage and subsequent activation. Intracellular
CC localization of the active receptor may prevent from responding to self
CC nucleic acid. {ECO:0000250|UniProtKB:Q9EQU3}.
CC -!- PTM: Activated by proteolytic cleavage of the flexible loop between
CC repeats LRR14 and LRR15 within the ectodomain. Cleavage requires
CC UNC93B1. Proteolytically processed by first removing the majority of
CC the ectodomain by either asparagine endopeptidase (AEP) or a cathepsin
CC followed by a trimming event that is solely cathepsin mediated and
CC required for optimal receptor signaling.
CC {ECO:0000250|UniProtKB:Q9EQU3}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AY859726; AAW50954.1; -; mRNA.
DR PDB; 3WPE; X-ray; 2.38 A; A=25-815.
DR PDB; 5Y3M; X-ray; 2.50 A; A/B=25-817.
DR PDBsum; 3WPE; -.
DR PDBsum; 5Y3M; -.
DR AlphaFoldDB; Q5I2M5; -.
DR SMR; Q5I2M5; -.
DR DIP; DIP-61514N; -.
DR STRING; 9913.ENSBTAP00000024223; -.
DR GlyCosmos; Q5I2M5; 13 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000024223; -.
DR eggNOG; KOG4641; Eukaryota.
DR InParanoid; Q5I2M5; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0036019; C:endolysosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050871; P:positive regulation of B cell activation; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR041283; LRR_12.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR47410; TOLL-LIKE RECEPTOR 7-RELATED; 1.
DR PANTHER; PTHR47410:SF3; TOLL-LIKE RECEPTOR 9; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF18837; LRR_12; 1.
DR Pfam; PF13855; LRR_8; 4.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 17.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Lysosome; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1029
FT /note="Toll-like receptor 9"
FT /id="PRO_0000227006"
FT TOPO_DOM 25..815
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 837..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 61..84
FT /note="LRR 1"
FT REPEAT 86..109
FT /note="LRR 2"
FT REPEAT 121..146
FT /note="LRR 3"
FT REPEAT 149..165
FT /note="LRR 4"
FT REPEAT 166..189
FT /note="LRR 5"
FT REPEAT 197..220
FT /note="LRR 6"
FT REPEAT 222..241
FT /note="LRR 7"
FT REPEAT 242..267
FT /note="LRR 8"
FT REPEAT 282..305
FT /note="LRR 9"
FT REPEAT 307..331
FT /note="LRR 10"
FT REPEAT 332..355
FT /note="LRR 11"
FT REPEAT 362..385
FT /note="LRR 12"
FT REPEAT 389..412
FT /note="LRR 13"
FT REPEAT 414..439
FT /note="LRR 14"
FT REPEAT 469..492
FT /note="LRR 15"
FT REPEAT 494..517
FT /note="LRR 16"
FT REPEAT 518..541
FT /note="LRR 17"
FT REPEAT 543..570
FT /note="LRR 18"
FT REPEAT 572..596
FT /note="LRR 19"
FT REPEAT 598..620
FT /note="LRR 20"
FT REPEAT 625..648
FT /note="LRR 21"
FT REPEAT 650..673
FT /note="LRR 22"
FT REPEAT 674..697
FT /note="LRR 23"
FT REPEAT 699..721
FT /note="LRR 24"
FT REPEAT 722..745
FT /note="LRR 25"
FT REPEAT 747..770
FT /note="LRR 26"
FT DOMAIN 864..1009
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 46..50
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT BINDING 71..76
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT BINDING 94..108
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT BINDING 131
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000250|UniProtKB:Q2EEY0"
FT BINDING 178..180
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000250|UniProtKB:Q2EEY0"
FT BINDING 207
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000250|UniProtKB:Q2EEY0"
FT BINDING 261
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="CpG-containing DNA"
FT /evidence="ECO:0000250|UniProtKB:Q2EEY0"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..44
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 97..109
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 177..183
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 254..267
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 257..264
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 469..498
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 762..788
FT /evidence="ECO:0000269|PubMed:25686612,
FT ECO:0007744|PDB:3WPE"
FT DISULFID 764..807
FT /evidence="ECO:0000250|UniProtKB:Q2EEY0"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5Y3M"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 115..120
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 191..196
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5Y3M"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 380..383
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:5Y3M"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 536..541
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 615..624
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 643..647
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 654..657
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:3WPE"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 743..745
FT /evidence="ECO:0007829|PDB:5Y3M"
FT HELIX 746..749
FT /evidence="ECO:0007829|PDB:5Y3M"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:3WPE"
FT HELIX 768..774
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 775..778
FT /evidence="ECO:0007829|PDB:3WPE"
FT TURN 780..785
FT /evidence="ECO:0007829|PDB:5Y3M"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:3WPE"
SQ SEQUENCE 1029 AA; 115407 MW; 02BD73CFE59E1F8D CRC64;
MGPYCAPHPL SLLVQAAALA AALAEGTLPA FLPCELQPHG QVDCNWLFLK SVPHFSAGAP
RANVTSLSLI SNRIHHLHDS DFVHLSNLRV LNLKWNCPPA GLSPMHFPCR MTIEPNTFLA
VPTLEELNLS YNGITTVPAL PSSLVSLSLS HTSILVLGPT HFTGLHALRF LYMDGNCYYM
NPCPRALEVA PGALLGLGNL THLSLKYNNL TEVPRRLPPS LDTLLLSYNH IVTLAPEDLA
NLTALRVLDV GGNCRRCDHA RNPCRECPKN FPKLHPDTFS HLSRLEGLVL KDSSLYKLEK
DWFRGLGRLQ VLDLSENFLY DYITKTTIFN DLTQLRRLNL SFNYHKKVSF AHLHLASSFG
SLVSLEKLDM HGIFFRSLTN ITLQSLTRLP KLQSLHLQLN FINQAQLSIF GAFPSLLFVD
LSDNRISGAA TPAAALGEVD SRVEVWRLPR GLAPGPLDAV SSKDFMPSCN LNFTLDLSRN
NLVTIQQEMF TRLSRLQCLR LSHNSISQAV NGSQFVPLTS LRVLDLSHNK LDLYHGRSFT
ELPQLEALDL SYNSQPFSMQ GVGHNLSFVA QLPSLRYLSL AHNGIHSRVS QKLSSASLRA
LDFSGNSLSQ MWAEGDLYLC FFKGLRNLVQ LDLSENHLHT LLPRHLDNLP KSLRQLRLRD
NNLAFFNWSS LTVLPRLEAL DLAGNQLKAL SNGSLPPGIR LQKLDVSSNS IGFVIPGFFV
RATRLIELNL SANALKTVDP SWFGSLAGTL KILDVSANPL HCACGAAFVD FLLERQEAVP
GLSRRVTCGS PGQLQGRSIF TQDLRLCLDE TLSLDCFGLS LLMVALGLAV PMLHHLCGWD
LWYCFHLCLA HLPRRRRQRG EDTLLYDAVV VFDKVQSAVA DWVYNELRVQ LEERRGRRAL
RLCLEERDWL PGKTLFENLW ASVYSSRKTM FVLDHTDRVS GLLRASFLLA QQRLLEDRKD
VVVLVILRPA AYRSRYVRLR QRLCRQSVLL WPHQPSGQGS FWANLGIALT RDNRHFYNRN
FCRGPTTAE
//
