TLR10_HUMAN
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 03-AUG-2022, entry version 184.
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 GlyGen; Q9BXR5; 9 sites.
DR iPTMnet; Q9BXR5; -.
DR PhosphoSitePlus; Q9BXR5; -.
DR BioMuta; TLR10; -.
DR DMDM; 116242819; -.
DR jPOST; Q9BXR5; -.
DR MassIVE; Q9BXR5; -.
DR PaxDb; Q9BXR5; -.
DR PeptideAtlas; Q9BXR5; -.
DR PRIDE; Q9BXR5; -.
DR ProteomicsDB; 79485; -.
DR Antibodypedia; 10452; 410 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 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; CHHEKNF; -.
DR OrthoDB; 282372at2759; -.
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; 24 hits in 1070 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 108 other tissues.
DR ExpressionAtlas; Q9BXR5; baseline and differential.
DR Genevisible; Q9BXR5; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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:0004888; F:transmembrane signaling receptor activity; TAS:UniProtKB.
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; IC:ComplexPortal.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:InterPro.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 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; IPR027182; TLR10.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF23; PTHR24365:SF23; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 9.
DR PROSITE; PS50104; TIR; 1.
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
