TOLL6_DROME
ID TOLL6_DROME Reviewed; 1514 AA.
AC Q9VUN0; Q6NN49; Q9NBK9;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Toll-like receptor 6 {ECO:0000305};
DE Flags: Precursor;
GN Name=Toll-6 {ECO:0000312|FlyBase:FBgn0036494};
GN Synonyms=Tl-6 {ECO:0000312|FlyBase:FBgn0036494};
GN ORFNames=CG7250 {ECO:0000312|FlyBase:FBgn0036494};
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:AAF86226.1}
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:AAR99103.1, ECO:0000312|EMBL:ACM16686.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR99103.1, ECO:0000312|EMBL:ACM16686.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR99103.1};
RA Carlson J., Booth B., Chavez C., Frise E., George R., Pacleb J., Park S.,
RA Rubin G.M., Stapleton M., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {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 [6] {ECO:0000305}
RP 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 [7] {ECO:0000305}
RP FUNCTION, 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 [8] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25363762; DOI=10.1038/nature13953;
RA Pare A.C., Vichas A., Fincher C.T., Mirman Z., Farrell D.L., Mainieri A.,
RA Zallen J.A.;
RT "A positional Toll receptor code directs convergent extension in
RT Drosophila.";
RL Nature 515:523-527(2014).
RN [9] {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 neurotrophin spz5
CC (PubMed:10973475, PubMed:23892553). 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). Involved in the
CC targeting of specific classes of PN dendrites (Va1d, Va1v, DC3 and DA1)
CC (PubMed:25741726). Functions with Toll-7 to regulate motor axon
CC targeting and neuronal survival in the central nervous system (CNS)
CC (PubMed:23892553). Possibly functions with 18w and Toll-8 during
CC convergent extension, to help direct proper planar cell polarity, cell
CC intercalation and axis elongation (PubMed:25363762). Promotes
CC heterophilic cell adhesion with 18w in vitro (PubMed:25363762). May be
CC an upstream component of the NF-kappa-B (rel) regulatory cascade
CC (PubMed:23892553). {ECO:0000269|PubMed:10973475,
CC ECO:0000269|PubMed:23892553, ECO:0000269|PubMed:25363762,
CC ECO:0000269|PubMed:25741726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed 48 hours after puparium formation in
CC lateral glomeruli in the anterior and central regions of the antennal
CC lobe, including the DA1, VA1d, VA1v, DC3. DC1, DA4l and DA4m glomeruli
CC (at protein level) (PubMed:25741726). Expressed zygotically
CC (PubMed:12617819). High levels of expression in embryos and pupae, and
CC relatively low levels of expression in larvae and adults
CC (PubMed:10973475). At cellular blastoderm stage, expressed as several
CC segmentally separated stripes, with the anterior stripes appearing
CC first (PubMed:12617819). At germ band extension, strongly expressed in
CC the delaminating neuroblasts (PubMed:12617819). Expression decreases at
CC germ band extension, remaining in a specific subset of neurons in the
CC central nervous system (PubMed:12617819). Expressed in 6 segmentally
CC repeated stripes in the germband (PubMed:25363762). In larvae, detected
CC in the fat body (PubMed:12617819). In larvae, expressed in the optic
CC lobes and the ventral nerve cord of the CNS (PubMed:23892553).
CC Expressed 48 hours after puparium formation in ORN axons and PN
CC dendrites that target to largely overlaping glomeruli
CC (PubMed:25741726). {ECO:0000269|PubMed:10973475,
CC ECO:0000269|PubMed:12617819, ECO:0000269|PubMed:23892553,
CC ECO:0000269|PubMed:25363762, ECO:0000269|PubMed:25741726}.
CC -!- DISRUPTION PHENOTYPE: Viable (PubMed:25741726). Dorsomedial or
CC dorsolateral mistargeting of VA1d ORN axons (PubMed:25741726). No
CC effect on the immune response to septic injury using a mixture of Gram-
CC positive and Gram-negative bacteria; adult flies are able induce
CC expression of antibacterial peptide genes (Drs, AttA, DptA and Mtk) and
CC mount a proper innate immune response (PubMed:21158756).
CC {ECO:0000269|PubMed:21158756, 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; AF247766; AAF86226.1; -; mRNA.
DR EMBL; AE014296; AAF49645.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04436.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04437.1; -; Genomic_DNA.
DR EMBL; BT011445; AAR99103.1; -; mRNA.
DR EMBL; BT057976; ACM16686.1; -; mRNA.
DR RefSeq; NP_001246765.1; NM_001259836.2.
DR RefSeq; NP_001246766.1; NM_001259837.3.
DR RefSeq; NP_524081.1; NM_079357.4.
DR AlphaFoldDB; Q9VUN0; -.
DR IntAct; Q9VUN0; 4.
DR STRING; 7227.FBpp0297411; -.
DR GlyGen; Q9VUN0; 17 sites.
DR PaxDb; Q9VUN0; -.
DR PRIDE; Q9VUN0; -.
DR EnsemblMetazoa; FBtr0075614; FBpp0075367; FBgn0036494.
DR EnsemblMetazoa; FBtr0306307; FBpp0297410; FBgn0036494.
DR EnsemblMetazoa; FBtr0306308; FBpp0297411; FBgn0036494.
DR GeneID; 39663; -.
DR KEGG; dme:Dmel_CG7250; -.
DR UCSC; CG7250-RA; d. melanogaster.
DR CTD; 39663; -.
DR FlyBase; FBgn0036494; Toll-6.
DR VEuPathDB; VectorBase:FBgn0036494; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000168338; -.
DR HOGENOM; CLU_004280_0_0_1; -.
DR InParanoid; Q9VUN0; -.
DR OMA; TFMHKTN; -.
DR OrthoDB; 737804at2759; -.
DR PhylomeDB; Q9VUN0; -.
DR Reactome; R-DME-376176; Signaling by ROBO receptors.
DR Reactome; R-DME-428890; Role of ABL in ROBO-SLIT signaling.
DR SignaLink; Q9VUN0; -.
DR BioGRID-ORCS; 39663; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39663; -.
DR PRO; PR:Q9VUN0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036494; Expressed in anlage in statu nascendi and 36 other tissues.
DR ExpressionAtlas; Q9VUN0; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin 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:0005030; F:neurotrophin receptor activity; IMP:FlyBase.
DR GO; GO:0048495; F:Roundabout binding; IBA:GO_Central.
DR GO; GO:0003401; P:axis elongation; IGI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0060026; P:convergent extension; IGI:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IGI:FlyBase.
DR GO; GO:0007165; P:signal transduction; IMP:FlyBase.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 6.
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; PF13855; LRR_8; 6.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 23.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 24.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1514
FT /note="Toll-like receptor 6"
FT /id="PRO_0000436858"
FT TOPO_DOM 15..1057
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1058..1078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1079..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 145..168
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 170..191
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 199..222
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 224..246
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 276..299
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 300..323
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 324..347
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 349..372
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 374..398
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 399..422
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 424..446
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 448..470
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 471..494
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 495..518
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 519..541
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 543..565
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 566..589
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 591..612
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 614..635
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 636..658
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 660..682
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 683..705
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 707..729
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 858..881
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 883..905
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 906..929
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 930..953
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 955..977
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT DOMAIN 1111..1244
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 242..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 752..802
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 826..832
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 830..845
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 993..1020
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT CONFLICT 249
FT /note="K -> Q (in Ref. 1; AAF86226)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="Y -> C (in Ref. 4; AAR99103)"
FT /evidence="ECO:0000305"
FT CONFLICT 1475
FT /note="V -> A (in Ref. 1; AAF86226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1514 AA; 170158 MW; 5BC45E5EE9A1E28F CRC64;
MIYYMLLILP VVLAQDQQHT TESLSTKHHQ QQQLSHSNAI MGEAGVSNSQ LMQPSTPART
LRPLTAGAGG DPSLYDAPDD CHFMPAAGLD QPEIALTCNL RTVNSEFDTT NFSVIPAEHT
IALHILCNDE IMAKSRLEAQ SFAHLVRLQQ LSIQYCKLGR LGRQVLDGLE QLRNLTLRTH
NILWPALNFE IEADAFSVTR RLERLDLSSN NIWSLPDNIF CTLSELSALN MSENRLQDVN
ELGFRDRSKE PTNGSTESTS TTESAKKSSS SSTSCSLDLE YLDVSHNDFV VLPANGFGTL
RRLRVLSVNN NGISMIADKA LSGLKNLQIL NLSSNKIVAL PTELFAEQAK IIQEVYLQNN
SISVLNPQLF SNLDQLQALD LSMNQITSTW IDKNTFVGLI RLVLLNLSHN KLTKLEPEIF
SDLYTLQILN LRHNQLENIA ADTFAPMNNL HTLLLSHNKL KYLDAYALNG LYVLSLLSLD
NNALIGVHPD AFRNCSALQD LNLNGNQLKT VPLALRNMRH LRTVDLGENM ITVMEDSAFK
GLGNLYGLRL IGNYLENITM HTFRDLPNLQ ILNLARNRIA VVEPGAFEMT SSIQAVRLDG
NELNDINGLF SNMPSLLWLN ISDNRLESFD YGHVPSTLQW LDLHKNRLSS LSNRFGLDSE
LKLQTLDVSF NQLQRIGPSS IPNSIELLFL NDNLITTVDP DTFMHKTNLT RVDLYANQIT
TLDIKSLRIL PVWEHRALPE FYIGGNPFTC DCNIDWLQKI NHITSRQYPR IMDLETIYCK
LLNNRERAYI PLIEAEPKHF LCTYKTHCFA VCHCCEFDAC DCEMTCPTNC TCFHDQTWST
NIVECSGAAY SEMPRRVPMD TSELYIDGNN FVELAGHSFL GRKNLAVLYA NNSNVAHIYN
TTFSGLKRLL ILHLEDNHII SLEGNEFHNL ENLRELYLQS NKIASIANGS FQMLRKLEVL
RLDGNRLMHF EVWQLSANPY LVEISLADNQ WSCECGYLAR FRNYLGQSSE KIIDASRVSC
IYNNATSVLR EKNGTKCTLR DGVAHYMHTN EIEGLLPLLL VATCAFVAFF GLIFGLFCYR
HELKIWAHST NCLMNFCYKS PRFVDQLDKE RPNDAYFAYS LQDEHFVNQI LAQTLENDIG
YRLCLHYRDV NINAYITDAL IEAAESAKQF VLVLSKNFLY NEWSRFEYKS ALHELVKRRK
RVVFILYGDL PQRDIDMDMR HYLRTSTCIE WDDKKFWQKL RLALPLPNGR GNNNKRVVSG
CLSGRTPSVN MYATSHEYQA GNGGVIPPPS ARYADCGSNN YATINECAAA GGGRGYKPIP
TSASAAAAAC KFNTMNQLSK KQQRDLSVAG MAKTLEHQHH HNHQANRRSQ HEYAVPSYLP
SAAPAYDSVD YAKQQIRNNA NCECVNLGTA KRAAGKNPAS GLPSSFSSNF VPPGGASYNC
KKSCSCIGDD ELLCSCGGGG GIGVNLLESG TQSSVTMSSS SNNSRQPELT HYESNLSLND
DEDEDHDQQK NLWA
