ID TLR10_HUMAN Reviewed; 811 AA. AC Q9BXR5; A8K7L1; B3Y668; D1CS21; D1CS22; Q32MI7; Q32MI8; Q5FWG4; Q6UXL3; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Toll-like receptor 10; DE AltName: CD_antigen=CD290; DE Flags: Precursor; GN Name=TLR10; ORFNames=UNQ315/PRO358; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Spleen; RX PubMed=11267672; DOI=10.1016/s0167-4781(00)00289-x; RA Chuang T.-H., Ulevitch R.J.; RT "Identification of hTLR10: a novel human Toll-like receptor preferentially RT expressed in immune cells."; RL Biochim. Biophys. Acta 1518:157-161(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0; RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.; RT "Natural selection in the TLR-related genes in the course of primate RT evolution."; RL Immunogenetics 60:727-735(2008). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-381. RX PubMed=19924287; DOI=10.1371/journal.pone.0007803; RA Georgel P., Macquin C., Bahram S.; RT "The heterogeneous allelic repertoire of human Toll-Like receptor (TLR) RT genes."; RL PLoS ONE 4:E7803-E7803(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-241; LEU-369 AND RP VAL-775. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-241; LEU-369; RP THR-473 AND VAL-775. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 622-776, AND SUBUNIT. RX PubMed=18332149; DOI=10.1074/jbc.c800001200; RA Nyman T., Stenmark P., Flodin S., Johansson I., Hammarstrom M., RA Nordlund P.; RT "The crystal structure of the human toll-like receptor 10 cytoplasmic RT domain reveals a putative signaling dimer."; RL J. Biol. Chem. 283:11861-11865(2008). CC -!- FUNCTION: Participates in the innate immune response to microbial CC agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, CC cytokine secretion and the inflammatory response (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Binds MYD88 via their respective TIR domains (By similarity). CC Homodimer (Potential). {ECO:0000250, ECO:0000305}. CC -!- INTERACTION: CC Q9BXR5; P54252: ATXN3; NbExp=3; IntAct=EBI-16825459, EBI-946046; CC Q9BXR5; Q15399: TLR1; NbExp=3; IntAct=EBI-16825459, EBI-9009517; CC Q9BXR5; Q9BXR5: TLR10; NbExp=3; IntAct=EBI-16825459, EBI-16825459; CC Q9BXR5; O60603: TLR2; NbExp=3; IntAct=EBI-16825459, EBI-973722; CC Q9BXR5; O76024: WFS1; NbExp=3; IntAct=EBI-16825459, EBI-720609; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, lymph node, thymus, CC tonsil and at lower levels in lung. Highly expressed in promyelocytic CC HL-60 cells and in B-cell lines. CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}. CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite CC the presence of the catalytic Asp residue, the isolated TIR domain of CC human TLR4 lacks NADase activity (By similarity). Based on this, it is CC unlikely that Toll-like receptors have NADase activity. CC {ECO:0000250|UniProtKB:O00206, 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; AF296673; AAK26744.1; -; mRNA. DR EMBL; AB445680; BAG55077.1; -; mRNA. DR EMBL; DQ011504; AAY78479.1; -; mRNA. DR EMBL; DQ011505; AAY78480.1; -; mRNA. DR EMBL; AY358300; AAQ88667.1; -; mRNA. DR EMBL; AK292026; BAF84715.1; -; mRNA. DR EMBL; CH471069; EAW92897.1; -; Genomic_DNA. DR EMBL; BC089406; AAH89406.1; -; mRNA. DR EMBL; BC109111; AAI09112.1; -; mRNA. DR EMBL; BC109112; AAI09113.1; -; mRNA. DR CCDS; CCDS3445.1; -. DR RefSeq; NP_001017388.1; NM_001017388.2. DR RefSeq; NP_001182035.1; NM_001195106.1. DR RefSeq; NP_001182036.1; NM_001195107.1. DR RefSeq; NP_001182037.1; NM_001195108.1. DR RefSeq; NP_112218.2; NM_030956.3. DR RefSeq; XP_011512063.1; XM_011513761.2. DR RefSeq; XP_011512064.1; XM_011513762.2. DR PDB; 2J67; X-ray; 2.20 A; A/B=622-776. DR PDBsum; 2J67; -. DR AlphaFoldDB; Q9BXR5; -. DR SMR; Q9BXR5; -. DR BioGRID; 123585; 11. DR ComplexPortal; CPX-2524; TLR2-TLR10 toll-like receptor complex. DR ComplexPortal; CPX-2699; TLR1-TLR10 toll-like receptor complex. DR IntAct; Q9BXR5; 12. DR STRING; 9606.ENSP00000308925; -. DR GlyCosmos; Q9BXR5; 9 sites, No reported glycans. DR GlyGen; Q9BXR5; 9 sites. DR iPTMnet; Q9BXR5; -. DR PhosphoSitePlus; Q9BXR5; -. DR BioMuta; TLR10; -. DR DMDM; 116242819; -. DR jPOST; Q9BXR5; -. DR MassIVE; Q9BXR5; -. DR PaxDb; 9606-ENSP00000308925; -. DR PeptideAtlas; Q9BXR5; -. DR ProteomicsDB; 79485; -. DR Antibodypedia; 10452; 432 antibodies from 35 providers. DR DNASU; 81793; -. DR Ensembl; ENST00000308973.9; ENSP00000308925.4; ENSG00000174123.11. DR Ensembl; ENST00000361424.6; ENSP00000354459.2; ENSG00000174123.11. DR Ensembl; ENST00000506111.1; ENSP00000421483.1; ENSG00000174123.11. DR Ensembl; ENST00000508334.1; ENSP00000424923.1; ENSG00000174123.11. DR Ensembl; ENST00000613579.4; ENSP00000478206.1; ENSG00000174123.11. DR Ensembl; ENST00000622002.4; ENSP00000478985.1; ENSG00000174123.11. DR GeneID; 81793; -. DR KEGG; hsa:81793; -. DR MANE-Select; ENST00000308973.9; ENSP00000308925.4; NM_030956.4; NP_112218.2. DR UCSC; uc003gti.3; human. DR AGR; HGNC:15634; -. DR CTD; 81793; -. DR DisGeNET; 81793; -. DR GeneCards; TLR10; -. DR HGNC; HGNC:15634; TLR10. DR HPA; ENSG00000174123; Tissue enriched (lymphoid). DR MIM; 606270; gene. DR neXtProt; NX_Q9BXR5; -. DR OpenTargets; ENSG00000174123; -. DR PharmGKB; PA38011; -. DR VEuPathDB; HostDB:ENSG00000174123; -. DR eggNOG; KOG4641; Eukaryota. DR GeneTree; ENSGT00940000163662; -. DR HOGENOM; CLU_006000_3_0_1; -. DR InParanoid; Q9BXR5; -. DR OMA; ICLYERY; -. DR OrthoDB; 21383at2759; -. DR PhylomeDB; Q9BXR5; -. DR TreeFam; TF351113; -. DR PathwayCommons; Q9BXR5; -. DR Reactome; R-HSA-168142; Toll Like Receptor 10 (TLR10) Cascade. DR Reactome; R-HSA-5603037; IRAK4 deficiency (TLR5). DR Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane. DR SignaLink; Q9BXR5; -. DR BioGRID-ORCS; 81793; 28 hits in 1146 CRISPR screens. DR EvolutionaryTrace; Q9BXR5; -. DR GeneWiki; TLR10; -. DR GenomeRNAi; 81793; -. DR Pharos; Q9BXR5; Tbio. DR PRO; PR:Q9BXR5; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9BXR5; Protein. DR Bgee; ENSG00000174123; Expressed in lymph node and 110 other cell types or tissues. DR ExpressionAtlas; Q9BXR5; baseline and differential. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central. DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0035663; F:Toll-like receptor 2 binding; IBA:GO_Central. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:UniProtKB. DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; IBA:GO_Central. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; NAS:ComplexPortal. DR GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:ComplexPortal. 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; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR000157; TIR_dom. DR InterPro; IPR017241; Toll-like_receptor. DR InterPro; IPR035897; Toll_tir_struct_dom_sf. DR PANTHER; PTHR24365; TOLL-LIKE RECEPTOR; 1. DR PANTHER; PTHR24365:SF23; TOLL-LIKE RECEPTOR 10; 1. DR Pfam; PF13855; LRR_8; 1. DR Pfam; PF01582; TIR; 1. DR PIRSF; PIRSF037595; Toll-like_receptor; 1. DR SMART; SM00364; LRR_BAC; 4. DR SMART; SM00369; LRR_TYP; 4. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00255; TIR; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1. DR PROSITE; PS51450; LRR; 9. DR PROSITE; PS50104; TIR; 1. DR Genevisible; Q9BXR5; HS. PE 1: Evidence at protein level; KW 3D-structure; Glycoprotein; Immunity; Inflammatory response; KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..811 FT /note="Toll-like receptor 10" FT /id="PRO_0000034739" FT TOPO_DOM 20..576 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 577..597 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 598..811 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 24..46 FT /note="LRR 1" FT REPEAT 49..70 FT /note="LRR 2" FT REPEAT 73..94 FT /note="LRR 3" FT REPEAT 97..118 FT /note="LRR 4" FT REPEAT 119..139 FT /note="LRR 5" FT REPEAT 143..166 FT /note="LRR 6" FT REPEAT 296..321 FT /note="LRR 7" FT REPEAT 325..348 FT /note="LRR 8" FT REPEAT 349..368 FT /note="LRR 9" FT REPEAT 373..394 FT /note="LRR 10" FT REPEAT 398..419 FT /note="LRR 11" FT REPEAT 422..442 FT /note="LRR 12" FT REPEAT 444..465 FT /note="LRR 13" FT REPEAT 467..488 FT /note="LRR 14" FT REPEAT 489..509 FT /note="LRR 15" FT DOMAIN 522..576 FT /note="LRRCT" FT DOMAIN 632..775 FT /note="TIR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 189 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 236 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 416 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 427 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 163 FT /note="A -> S (in dbSNP:rs11466649)" FT /id="VAR_024669" FT VARIANT 167 FT /note="L -> P (in dbSNP:rs11466650)" FT /id="VAR_028125" FT VARIANT 241 FT /note="N -> H (in dbSNP:rs11096957)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_024670" FT VARIANT 298 FT /note="V -> I (in dbSNP:rs11466651)" FT /id="VAR_028126" FT VARIANT 326 FT /note="M -> T (in dbSNP:rs11466653)" FT /id="VAR_024671" FT VARIANT 369 FT /note="I -> L (in dbSNP:rs11096955)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_024672" FT VARIANT 381 FT /note="G -> D (in dbSNP:rs11466655)" FT /evidence="ECO:0000269|PubMed:19924287" FT /id="VAR_024673" FT VARIANT 469 FT /note="R -> G (in dbSNP:rs11466656)" FT /id="VAR_028127" FT VARIANT 473 FT /note="I -> T (in dbSNP:rs11466657)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_028128" FT VARIANT 525 FT /note="R -> W (in dbSNP:rs11466658)" FT /id="VAR_024674" FT VARIANT 736 FT /note="Y -> C (in dbSNP:rs11466660)" FT /id="VAR_028129" FT VARIANT 775 FT /note="I -> F (in dbSNP:rs4129009)" FT /id="VAR_059832" FT VARIANT 775 FT /note="I -> L (in dbSNP:rs4129009)" FT /id="VAR_028130" FT VARIANT 775 FT /note="I -> V (in dbSNP:rs4129009)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_059833" FT VARIANT 799 FT /note="R -> L (in dbSNP:rs4129008)" FT /id="VAR_059834" FT VARIANT 799 FT /note="R -> P (in dbSNP:rs4129008)" FT /id="VAR_059835" FT VARIANT 799 FT /note="R -> Q (in dbSNP:rs4129008)" FT /id="VAR_028131" FT CONFLICT 96 FT /note="K -> R (in Ref. 5; BAF84715)" FT /evidence="ECO:0000305" FT CONFLICT 562 FT /note="T -> I (in Ref. 1; AAK26744)" FT /evidence="ECO:0000305" FT STRAND 634..639 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 642..644 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 645..650 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 652..656 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 668..671 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 678..687 FT /evidence="ECO:0007829|PDB:2J67" FT STRAND 689..696 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 698..703 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 705..707 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 709..712 FT /evidence="ECO:0007829|PDB:2J67" FT TURN 717..719 FT /evidence="ECO:0007829|PDB:2J67" FT STRAND 725..731 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 735..737 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 743..750 FT /evidence="ECO:0007829|PDB:2J67" FT STRAND 754..756 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 761..763 FT /evidence="ECO:0007829|PDB:2J67" FT HELIX 764..775 FT /evidence="ECO:0007829|PDB:2J67" SQ SEQUENCE 811 AA; 94564 MW; 6BFAAEF76886BFBA CRC64; MRLIRNIYIF CSIVMTAEGD APELPEEREL MTNCSNMSLR KVPADLTPAT TTLDLSYNLL FQLQSSDFHS VSKLRVLILC HNRIQQLDLK TFEFNKELRY LDLSNNRLKS VTWYLLAGLR YLDLSFNDFD TMPICEEAGN MSHLEILGLS GAKIQKSDFQ KIAHLHLNTV FLGFRTLPHY EEGSLPILNT TKLHIVLPMD TNFWVLLRDG IKTSKILEMT NIDGKSQFVS YEMQRNLSLE NAKTSVLLLN KVDLLWDDLF LILQFVWHTS VEHFQIRNVT FGGKAYLDHN SFDYSNTVMR TIKLEHVHFR VFYIQQDKIY LLLTKMDIEN LTISNAQMPH MLFPNYPTKF QYLNFANNIL TDELFKRTIQ LPHLKTLILN GNKLETLSLV SCFANNTPLE HLDLSQNLLQ HKNDENCSWP ETVVNMNLSY NKLSDSVFRC LPKSIQILDL NNNQIQTVPK ETIHLMALRE LNIAFNFLTD LPGCSHFSRL SVLNIEMNFI LSPSLDFVQS CQEVKTLNAG RNPFRCTCEL KNFIQLETYS EVMMVGWSDS YTCEYPLNLR GTRLKDVHLH ELSCNTALLI VTIVVIMLVL GLAVAFCCLH FDLPWYLRML GQCTQTWHRV RKTTQEQLKR NVRFHAFISY SEHDSLWVKN ELIPNLEKED GSILICLYES YFDPGKSISE NIVSFIEKSY KSIFVLSPNF VQNEWCHYEF YFAHHNLFHE NSDHIILILL EPIPFYCIPT RYHKLKALLE KKAYLEWPKD RRKCGLFWAN LRAAINVNVL ATREMYELQT FTELNEESRG STISLMRTDC L //