TLR13_MOUSE
ID TLR13_MOUSE Reviewed; 991 AA.
AC Q6R5N8; Q148Y7; Q3TDS2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Toll-like receptor 13;
DE Flags: Precursor;
GN Name=Tlr13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=14993594; DOI=10.1073/pnas.0400525101;
RA Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S.,
RA Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.;
RT "Toll-like receptors 9 and 3 as essential components of innate immune
RT defense against mouse cytomegalovirus infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682.
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH UNC93B1.
RX PubMed=17452530; DOI=10.1083/jcb.200612056;
RA Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.;
RT "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9
RT is crucial for TLR signaling.";
RL J. Cell Biol. 177:265-275(2007).
RN [7]
RP FUNCTION.
RX PubMed=21131352; DOI=10.1074/jbc.m110.159590;
RA Shi Z., Cai Z., Sanchez A., Zhang T., Wen S., Wang J., Yang J., Fu S.,
RA Zhang D.;
RT "A novel Toll-like receptor that recognizes vesicular stomatitis virus.";
RL J. Biol. Chem. 286:4517-4524(2011).
RN [8]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=22821982; DOI=10.1126/science.1220363;
RA Oldenburg M., Kruger A., Ferstl R., Kaufmann A., Nees G., Sigmund A.,
RA Bathke B., Lauterbach H., Suter M., Dreher S., Koedel U., Akira S.,
RA Kawai T., Buer J., Wagner H., Bauer S., Hochrein H., Kirschning C.J.;
RT "TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-
RT forming modification.";
RL Science 337:1111-1115(2012).
RN [9]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=22896636; DOI=10.4049/jimmunol.1200898;
RA Hidmark A., von Saint Paul A., Dalpke A.H.;
RT "TLR13 Is a Receptor for Bacterial RNA.";
RL J. Immunol. 189:2717-2721(2012).
CC -!- FUNCTION: Component of innate and adaptive immunity that recognizes and
CC binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host
CC immune response against pathogens through recognition of molecular
CC patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading
CC to NF-kappa-B activation, cytokine secretion and the inflammatory
CC response. Specifically binds the 5'-CGGAAAGACC-3' sequence on bacterial
CC 23S rRNA, a sequence also bound by MLS group antibiotics (including
CC erythromycin). May also recognize vesicular stomatitis virus; however,
CC these data require additional evidences. {ECO:0000269|PubMed:21131352,
CC ECO:0000269|PubMed:22821982, ECO:0000269|PubMed:22896636}.
CC -!- SUBUNIT: Binds MYD88 via their respective TIR domains (By similarity).
CC Interacts with UNC93B1. {ECO:0000250, ECO:0000269|PubMed:17452530}.
CC -!- INTERACTION:
CC Q6R5N8; Q6R5N8: Tlr13; NbExp=4; IntAct=EBI-16173901, EBI-16173901;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:22896636};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:22896636}.
CC -!- MISCELLANEOUS: The sequence 23S rRNA from clinical isolates of
CC erythromycin-resistant S.aureus is methylated and is not recognized by
CC Tlr13 anymore, suggesting a link between antibiotic resistance and
CC evasion from Tlr13 recognition. 23S rRNA modifications generating
CC resistance toward MLS antibiotics preventing recognition of bacteria
CC from Tlr13. These data may also explain why Tlr13 is not conserved in
CC human: human may instead possess a related rRNA-sensing pattern
CC recognition receptor that has evolved to recognize species that can
CC hide from Tlr13 owing to rRNA modifications (PubMed:22821982).
CC {ECO:0000305|PubMed:22821982}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAE41528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY510706; AAS37674.1; -; mRNA.
DR EMBL; AK170044; BAE41528.1; ALT_INIT; mRNA.
DR EMBL; AL672288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466564; EDL14060.1; -; Genomic_DNA.
DR EMBL; BC117913; AAI17914.1; -; mRNA.
DR EMBL; BC117914; AAI17915.1; -; mRNA.
DR CCDS; CCDS30338.1; -.
DR RefSeq; NP_991389.1; NM_205820.1.
DR PDB; 4Z0C; X-ray; 2.30 A; A/D=69-777.
DR PDBsum; 4Z0C; -.
DR AlphaFoldDB; Q6R5N8; -.
DR SMR; Q6R5N8; -.
DR BioGRID; 235006; 1.
DR DIP; DIP-61832N; -.
DR STRING; 10090.ENSMUSP00000043101; -.
DR GlyGen; Q6R5N8; 21 sites.
DR iPTMnet; Q6R5N8; -.
DR PhosphoSitePlus; Q6R5N8; -.
DR MaxQB; Q6R5N8; -.
DR PaxDb; Q6R5N8; -.
DR PeptideAtlas; Q6R5N8; -.
DR PRIDE; Q6R5N8; -.
DR ProteomicsDB; 258893; -.
DR DNASU; 279572; -.
DR Ensembl; ENSMUST00000040065; ENSMUSP00000043101; ENSMUSG00000033777.
DR GeneID; 279572; -.
DR KEGG; mmu:279572; -.
DR UCSC; uc009ubn.1; mouse.
DR CTD; 279572; -.
DR MGI; MGI:3045213; Tlr13.
DR VEuPathDB; HostDB:ENSMUSG00000033777; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00950000183593; -.
DR HOGENOM; CLU_006000_4_0_1; -.
DR InParanoid; Q6R5N8; -.
DR OMA; CWIVTID; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q6R5N8; -.
DR TreeFam; TF325595; -.
DR BioGRID-ORCS; 279572; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q6R5N8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6R5N8; protein.
DR Bgee; ENSMUSG00000033777; Expressed in stroma of bone marrow and 92 other tissues.
DR Genevisible; Q6R5N8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IGI:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IGI:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0034178; P:toll-like receptor 13 signaling pathway; IDA:UniProtKB.
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; -; 5.
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; PTHR24365; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; RNA-binding; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..68
FT /evidence="ECO:0000255"
FT CHAIN 69..991
FT /note="Toll-like receptor 13"
FT /id="PRO_0000042795"
FT TOPO_DOM 69..783
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..125
FT /note="LRR 1"
FT REPEAT 128..149
FT /note="LRR 2"
FT REPEAT 152..174
FT /note="LRR 3"
FT REPEAT 175..196
FT /note="LRR 4"
FT REPEAT 199..220
FT /note="LRR 5"
FT REPEAT 225..246
FT /note="LRR 6"
FT REPEAT 248..268
FT /note="LRR 7"
FT REPEAT 271..292
FT /note="LRR 8"
FT REPEAT 295..315
FT /note="LRR 9"
FT REPEAT 318..338
FT /note="LRR 10"
FT REPEAT 348..368
FT /note="LRR 11"
FT REPEAT 372..394
FT /note="LRR 12"
FT REPEAT 397..418
FT /note="LRR 13"
FT REPEAT 421..442
FT /note="LRR 14"
FT REPEAT 445..466
FT /note="LRR 15"
FT REPEAT 469..490
FT /note="LRR 16"
FT REPEAT 493..514
FT /note="LRR 17"
FT REPEAT 517..538
FT /note="LRR 18"
FT REPEAT 541..562
FT /note="LRR 19"
FT REPEAT 565..585
FT /note="LRR 20"
FT REPEAT 594..617
FT /note="LRR 21"
FT REPEAT 620..641
FT /note="LRR 22"
FT REPEAT 644..665
FT /note="LRR 23"
FT REPEAT 672..693
FT /note="LRR 24"
FT REPEAT 696..716
FT /note="LRR 25"
FT DOMAIN 729..779
FT /note="LRRCT"
FT DOMAIN 832..975
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
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 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 120..125
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 144..149
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 191..196
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 437..442
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 509..514
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 533..538
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 557..562
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 588..591
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 612..617
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 664..669
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:4Z0C"
FT TURN 712..717
FT /evidence="ECO:0007829|PDB:4Z0C"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 769..771
FT /evidence="ECO:0007829|PDB:4Z0C"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:4Z0C"
SQ SEQUENCE 991 AA; 114443 MW; 6FB622DC62F37E74 CRC64;
MSGLYRILVQ LEQSPYVKTV PLNMRRDFFF LVVTWMPKTV KMNGSSFVPS LQLLLMLVGF
SLPPVAETYG FNKCTQYEFD IHHVLCIRKK ITNLTEAISD IPRYTTHLNL THNEIQVLPP
WSFTNLSALV DLRLEWNSIW KIDEGAFRGL ENLTLLNLVE NKIQSVNNSF EGLSSLKTLL
LSHNQITHIH KDAFTPLIKL KYLSLSRNNI SDFSGILEAV QHLPCLERLD LTNNSIMYLD
HSPRSLVSLT HLSFEGNKLR ELNFSALSLP NLTNLSASRN GNKVIQNVYL KTLPQLKSLN
LSGTVIKLEN LSAKHLQNLR AMDLSNWELR HGHLDMKTVC HLLGNLPKLE TLVFQKNVTN
AEGIKQLAKC TRLLFLDLGQ NSDLIYLNDS EFNALPSLQK LNLNKCQLSF INNRTWSSLQ
NLTSLDLSHN KFKSFPDFAF SPLKHLEFLS LSRNPITELN NLAFSGLFAL KELNLAACWI
VTIDRYSFTQ FPNLEVLDLG DNNIRTLNHG TFRPLKKLQS LILSHNCLKI LEPNSFSGLT
NLRSLDLMYN SLSYFHEHLF SGLEKLLILK LGFNKITYET TRTLQYPPFI KLKSLKQLNL
EGQRHGIQVV PSNFFQGLGS LQELLLGKNP SVFLDHHQFD PLINLTKLDI SGTKDGDRSL
YLNASLFQNL KRLKILRLEN NNLESLVPDM FSSLQSLQVF SLRFNNLKVI NQSHLKNLKS
LMFFDVYGNK LQCTCDNLWF KNWSMNTEEV HIPFLRSYPC QQPGSQSLLI DFDDAMCNFD
LGKVYFLCSF SMVLSTMVFS WFSTKMIASL WYGLYICRAW YLTKWHKTEK KFLYDAFVSF
SATDEAWVYK ELVPALEQGS QTTFKLCLHQ RDFEPGIDIF ENIQNAINTS RKTLCVVSNH
YLHSEWCRLE VQLASMKMFY EHKDVIILIF LEEIPNYKLS SYHRLRKLIN KQTFITWPDS
VHQQPLFWAR IRNALGKETV EKENTHLIVV E
