TOLL7_DROME
ID TOLL7_DROME Reviewed; 1446 AA.
AC Q7KIN0; E1NZA7; Q2XXU8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Toll-like receptor 7 {ECO:0000305};
DE Flags: Precursor;
GN Name=Toll-7 {ECO:0000312|FlyBase:FBgn0034476};
GN ORFNames=CG8595 {ECO:0000312|FlyBase:FBgn0034476};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAF86225.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10973475; DOI=10.1073/pnas.180130797;
RA Tauszig S., Jouanguy E., Hoffmann J.A., Imler J.L.;
RT "Toll-related receptors and the control of antimicrobial peptide expression
RT in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10520-10525(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:ABA86520.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-1435.
RC STRAIN=Ral1 {ECO:0000312|EMBL:ABA86520.1};
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
RN [5] {ECO:0000312|EMBL:ADN32842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1031.
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=12617819; DOI=10.1016/s1567-133x(02)00020-0;
RA Kambris Z., Hoffmann J.A., Imler J.L., Capovilla M.;
RT "Tissue and stage-specific expression of the Tolls in Drosophila embryos.";
RL Gene Expr. Patterns 2:311-317(2002).
RN [7] {ECO:0000305}
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21158756; DOI=10.1111/j.1440-169x.2010.01213.x;
RA Yagi Y., Nishida Y., Ip Y.T.;
RT "Functional analysis of Toll-related genes in Drosophila.";
RL Dev. Growth Differ. 52:771-783(2010).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY VIRAL INFECTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22464169; DOI=10.1016/j.immuni.2012.03.003;
RA Nakamoto M., Moy R.H., Xu J., Bambina S., Yasunaga A., Shelly S.S.,
RA Gold B., Cherry S.;
RT "Virus recognition by Toll-7 activates antiviral autophagy in Drosophila.";
RL Immunity 36:658-667(2012).
RN [9] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23892553; DOI=10.1038/nn.3474;
RA McIlroy G., Foldi I., Aurikko J., Wentzell J.S., Lim M.A., Fenton J.C.,
RA Gay N.J., Hidalgo A.;
RT "Toll-6 and Toll-7 function as neurotrophin receptors in the Drosophila
RT melanogaster CNS.";
RL Nat. Neurosci. 16:1248-1256(2013).
RN [10] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25741726; DOI=10.1016/j.neuron.2015.02.003;
RA Ward A., Hong W., Favaloro V., Luo L.;
RT "Toll receptors instruct axon and dendrite targeting and participate in
RT synaptic partner matching in a Drosophila olfactory circuit.";
RL Neuron 85:1013-1028(2015).
CC -!- FUNCTION: Toll-related receptor which binds to the neurotrophins NT1
CC and spz5 (PubMed:10973475, PubMed:23892553). Essential for antiviral
CC autophagy, it detects and binds to the vesicular stomatitis virus (vsv)
CC following infection (PubMed:22464169). This role is likely to be
CC independent of the canonical Toll, immune deficiency, and JAK-STAT
CC signaling pathways (PubMed:22464169). Functions in olfactory circuit
CC assembly by promoting synaptic partner matching between olfactory
CC receptor neurons (ORN) axons and projection neurons (PN) dendrites
CC partners in the antennal lobe (PubMed:25741726). Function in the Va1d
CC ORNs is necessary and sufficient for correct targeting to their partner
CC PN dendrites (PubMed:25741726). Also involved in the targeting of other
CC classes of ORN axons (PubMed:25741726). Functions with Toll-6 to
CC regulate motor axon targeting and neuronal survival in the central
CC nervous system (CNS) (PubMed:23892553). May be an upstream component of
CC the NF-kappa-B (rel) regulatory cascade (PubMed:23892553).
CC {ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:22464169,
CC ECO:0000269|PubMed:23892553, ECO:0000269|PubMed:25741726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22464169};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the fan-shaped body and the ellipsoid
CC body, which are components of the locomotion center in the CNS (at
CC protein level) (PubMed:23892553). {ECO:0000269|PubMed:23892553}.
CC -!- DEVELOPMENTAL STAGE: In embryos, expressed in the ventral neurons,
CC motor neurons and in the longitudinal interneuron axons (at protein
CC level) (PubMed:23892553). May also be expressed in the motor neuron
CC dendrites or possibly the glia (at protein level) (PubMed:23892553).
CC Expressed 48 hours after puparium formation in the lateral glomeruli of
CC the anterior and central regions of the antennal lobe, including the
CC DA1, VA1d and VA1v glomeruli (at protein level) (PubMed:25741726).
CC Expressed zygotically (PubMed:12617819). High levels of expression in
CC embryos and pupae, and relatively low levels of expression in larvae
CC and adults (PubMed:10973475). At germ band extension, expressed as 14
CC stripes in the embryo (PubMed:12617819). At germ band retraction,
CC expressed in a subset of neurons in the CNS, the precursors of the leg
CC imaginal disks and in the ventral epithelium of the large intestine
CC (PubMed:12617819). Expressed in the posterior and anterior spiracles
CC (PubMed:12617819). In stage 16 embryos, expression decreases and is
CC mainly localized to the CNS (PubMed:12617819). Expressed in the
CC proximal region of the wing imaginal disks, around the wing pouch and
CC hinge regions (PubMed:21158756). Also expressed in the distal segments
CC of the leg imaginal disks, with high levels of expression around the A-
CC P border of the tarsal to tibia segments (PubMed:21158756). In larvae,
CC detected in the fat body (PubMed:12617819).
CC {ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:12617819,
CC ECO:0000269|PubMed:21158756, ECO:0000269|PubMed:23892553,
CC ECO:0000269|PubMed:25741726}.
CC -!- INDUCTION: Up-regulated during vesicular stomatitis virus (VSV)
CC infection. {ECO:0000269|PubMed:22464169}.
CC -!- DISRUPTION PHENOTYPE: Mistargeting of VA1d ORN axons to a medial
CC position (PubMed:25741726). No effect on the immune response to septic
CC injury using a mixture of Gram-positive and Gram-negative bacteria;
CC adults are able induce expression of antibacterial peptide genes (Drs,
CC AttA, DptA and Mtk) and mount a proper innate immune response
CC (PubMed:21158756). RNAi-mediated knockdown results in adults that are
CC acutely sensitive to the vesicular stomatitis virus (vsv)
CC (PubMed:22464169). Following infection with vsv adult survival is
CC decreased, and adults show a dramatic increase in viral RNA production
CC 6 days post vsv infection and viral replication 9 days post infection
CC (PubMed:22464169). Reduced autophagy in adult fat body cells following
CC vsv infection (PubMed:22464169). Starvation-induced autophagy is not
CC affected (PubMed:22464169). {ECO:0000269|PubMed:21158756,
CC ECO:0000269|PubMed:22464169, ECO:0000269|PubMed:25741726}.
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}.
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DR EMBL; AF247765; AAF86225.1; -; mRNA.
DR EMBL; DQ138914; ABA86520.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57514.1; -; Genomic_DNA.
DR EMBL; BT125656; ADN32842.1; -; mRNA.
DR RefSeq; NP_523797.1; NM_079073.3.
DR AlphaFoldDB; Q7KIN0; -.
DR SMR; Q7KIN0; -.
DR STRING; 7227.FBpp0085638; -.
DR SwissPalm; Q7KIN0; -.
DR PaxDb; Q7KIN0; -.
DR EnsemblMetazoa; FBtr0086336; FBpp0085638; FBgn0034476.
DR GeneID; 37272; -.
DR KEGG; dme:Dmel_CG8595; -.
DR UCSC; CG8595-RA; d. melanogaster.
DR CTD; 37272; -.
DR FlyBase; FBgn0034476; Toll-7.
DR VEuPathDB; VectorBase:FBgn0034476; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000159318; -.
DR HOGENOM; CLU_004280_0_0_1; -.
DR InParanoid; Q7KIN0; -.
DR OMA; EWARCEL; -.
DR OrthoDB; 60380at2759; -.
DR PhylomeDB; Q7KIN0; -.
DR Reactome; R-DME-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-DME-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 37272; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37272; -.
DR PRO; PR:Q7KIN0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034476; Expressed in head epidermis primordium (Drosophila) and 32 other tissues.
DR ExpressionAtlas; Q7KIN0; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
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:0005030; F:neurotrophin receptor activity; IMP:FlyBase.
DR GO; GO:0038187; F:pattern recognition receptor activity; IC:FlyBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:FlyBase.
DR GO; GO:0046790; F:virion binding; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0009597; P:detection of virus; IDA:FlyBase.
DR GO; GO:0045087; P:innate immune response; IMP:FlyBase.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR GO; GO:0050688; P:regulation of defense response to virus; IMP:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:FlyBase.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 5.
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; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 6.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00369; LRR_TYP; 20.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 23.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Immunity;
KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1446
FT /note="Toll-like receptor 7"
FT /id="PRO_5006489795"
FT TOPO_DOM 17..1049
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1050..1070
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1071..1446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 133..156
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 158..180
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 188..211
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 213..235
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 246..270
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 271..294
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 295..318
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 320..342
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 344..368
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 369..392
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 393..416
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 417..440
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 442..464
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 465..488
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 489..511
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 513..535
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 536..559
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 561..582
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 584..605
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 606..629
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 631..652
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 653..675
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 677..699
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT DOMAIN 716..773
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT REPEAT 828..851
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 852..875
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 876..899
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 900..923
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 925..947
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 951..979
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT DOMAIN 1096..1233
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 1301..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 722..772
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 796..802
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 800..815
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 966..993
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT CONFLICT 58
FT /note="P -> L (in Ref. 4; ABA86520)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="T -> K (in Ref. 4; ABA86520)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426
FT /note="Missing (in Ref. 4; ABA86520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1446 AA; 160950 MW; 80D281BDA9500ABC CRC64;
MAAILLLLLG FSWSLAVESA LAPKESESSA SAMLGAGTGA AATVSLSGDY SSLLSNVPAA
SPVPANPSQP SGPANQCSWS YNGTSSVHCA LRLIERQPGL DLQGADGSSQ LTIQCSELYL
FESTLPVAVF ARLQTLEALR LDSCKLLQLP NNAFEGLATL KSLRLSTHNS EWGPTRTLEL
FPDSLGGLKQ LTDLDLGDNN LRQLPSGFLC PVGNLQVLNL TRNRIRTAEQ MGFADMNCGA
GSGSAGSELQ VLDASHNELR SISESWGISR LRRLQHLNLA YNNLSELSGE ALAGLASLRI
VNLSNNHLET LPEGLFAGSK ELREIHLQQN ELYELPKGLF HRLEQLLVVD LSGNQLTSNH
VDNTTFAGLI RLIVLNLAHN ALTRIDYRTF KELYFLQILN LRNNSIGHIE DNAFLPLYNL
HTLNLAENRL HTLDDKLFNG LYVLSKLTLN NNLISVVEPA VFKNCSDLKE LDLSSNQLNE
VPRALQDLAM LRTLDLGENQ IRTFDNQSFK NLHQLTGLRL IDNQIGNITV GMFQDLPRLS
VLNLAKNRIQ SIERGSFDKN FELEAIRLDR NFLADINGVF ATLVSLLWLN LSENHLVWFD
YAFIPSNLKW LDIHGNYIEA LGNYYKLQEE IRVKTLDASH NRITEIGPMS IPNTIELLFI
NNNLIGNVQP NAFVDKANLA RVDLYANQLS KLQLQQLRVA PVVAPKPLPE FYLGGNPFEC
DCTMDWLQRI NNLTTRQHPR VMDMANIECV MPHARGAAVR PLSGLRPQDF LCRYESHCFA
LCHCCDFDAC DCEMTCPSNC TCYHDQIWST NVVDCGGQQT TELPRRVPMD SSVVYLDGNN
FPVLKNHAFI GRKNLRALYV NGSQVAAIQN RTFASLASLQ LLHLADNKLR TLHGYEFEQL
SALRELYLQN NQLTTIENAT LAPLAALELI RIDGNRLVTL PIWQMHATHF GTRLKSISLG
RNQWSCRCQF LQALTSYVAD NALIVQDAQD IYCMAASSGT GSAALEDSSS NSGSLEKREL
DFNATGAACT DYYSGGSMLQ HGIPESYIPL LAAALALLFL LVVIAMVFAF RESLRIWLFA
HYGVRVFGPR CEESEKLYDA VLLHSAKDSE FVCQHLAAQL ETGRPPLRVC LQHRDLAHDA
THYQLLEATR VSRRVVILLT RNFLQTEWAR CELRRSVHDA LRGRPQKLVI IEEPEVAFEA
ESDIELLPYL KTSAVHRIRR SDRHFWEKLR YALPVDYPTF RGNNYTLELD HHNHERVKQP
ASPGLLYRQA PPPAYCGPAD AVGIGAVPQV VPVNASVPAE QNYSTATTAT PSPRPQRRGE
QPGSGSGGNH HLHAQYYQHH GMRPPSEHIY SSIDSDYSTL DNEQHMLMMP GAPGGLAMEA
AQRAQTWRPK REQLHLQQAQ AGTLGSKASQ AAHQQQQQQQ QQQQQQPNPT AVSGQQQGPH
VQAYLV
