LEDL3_DROME
ID LEDL3_DROME Reviewed; 150 AA.
AC Q59DY5; B3DNJ5; Q65Y00;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=C-type lectin 37Db {ECO:0000305};
DE Flags: Precursor;
GN Name=lectin-37Db {ECO:0000312|FlyBase:FBgn0053533};
GN Synonyms=DL3 {ECO:0000303|PubMed:16475980};
GN ORFNames=CG33533 {ECO:0000312|FlyBase:FBgn0053533};
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:BAD51434.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16475980; DOI=10.1042/bj20051921;
RA Tanji T., Ohashi-Kobayashi A., Natori S.;
RT "Participation of a galactose-specific C-type lectin in Drosophila
RT immunity.";
RL Biochem. J. 396:127-138(2006).
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:ACD99547.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=17287021; DOI=10.1016/j.molimm.2006.12.024;
RA Ao J., Ling E., Yu X.Q.;
RT "Drosophila C-type lectins enhance cellular encapsulation.";
RL Mol. Immunol. 44:2541-2548(2007).
CC -!- FUNCTION: Galactose-specific lectin that displays calcium-dependent
CC activity (PubMed:16475980, PubMed:17287021). Binds to the surface of
CC hemocytes and enhances hemocyte encapsulation and melanization
CC (PubMed:17287021). This is likely by interacting with carbohydrates on
CC the surface of the hemocytes (PubMed:17287021). Also displays
CC agglutination activity against the Gram-negative bacterium E.coli
CC (PubMed:17287021). {ECO:0000269|PubMed:16475980,
CC ECO:0000269|PubMed:17287021}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16475980}.
CC -!- DEVELOPMENTAL STAGE: Detected in adults and larvae.
CC {ECO:0000269|PubMed:16475980}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACD99547.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB190812; BAD51434.1; -; mRNA.
DR EMBL; AE014134; AAX52670.1; -; Genomic_DNA.
DR EMBL; AE014134; ADV37096.1; -; Genomic_DNA.
DR EMBL; BT032983; ACD99547.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014490.1; NM_001014490.2.
DR RefSeq; NP_001188847.1; NM_001201918.1.
DR AlphaFoldDB; Q59DY5; -.
DR SMR; Q59DY5; -.
DR IntAct; Q59DY5; 1.
DR GlyGen; Q59DY5; 2 sites.
DR PaxDb; Q59DY5; -.
DR DNASU; 3346221; -.
DR EnsemblMetazoa; FBtr0091499; FBpp0099538; FBgn0053533.
DR EnsemblMetazoa; FBtr0302362; FBpp0291558; FBgn0053533.
DR GeneID; 3346221; -.
DR KEGG; dme:Dmel_CG33533; -.
DR UCSC; CG33533-RA; d. melanogaster.
DR CTD; 3346221; -.
DR FlyBase; FBgn0053533; lectin-37Db.
DR VEuPathDB; VectorBase:FBgn0053533; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000172481; -.
DR HOGENOM; CLU_049894_10_0_1; -.
DR InParanoid; Q59DY5; -.
DR OMA; KTNWFEA; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; Q59DY5; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 3346221; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3346221; -.
DR PRO; PR:Q59DY5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0053533; Expressed in adult midgut (Drosophila) and 19 other tissues.
DR ExpressionAtlas; Q59DY5; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005534; F:galactose binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:FlyBase.
DR GO; GO:0035010; P:encapsulation of foreign target; IDA:FlyBase.
DR GO; GO:0035006; P:melanization defense response; IDA:FlyBase.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hemagglutinin; Lectin;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..150
FT /note="C-type lectin 37Db"
FT /id="PRO_5007209827"
FT DOMAIN 31..148
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 52..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 122..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 101
FT /note="L -> V (in Ref. 1; BAD51434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17053 MW; 7B4F97248BE97FD9 CRC64;
MMVKLLLLFL VCWSALPLES SPLGNRYNLE IGEKQYYISL AKTNWFEASN HCRQNGGFLL
NLESREELEL LSPHLHPAYS YWLSINDLGE RGVYVSEATG LEAPFLNWSA GEPDNSSGYD
RCVELWLSTT SFQMNDLPCY SSVAFICQLN
