LEDL2_DROME
ID LEDL2_DROME Reviewed; 186 AA.
AC Q59DY6; Q4V3L4; Q65Y01;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=C-type lectin 37Da {ECO:0000305};
DE Flags: Precursor;
GN Name=lectin-37Da {ECO:0000312|FlyBase:FBgn0053532};
GN Synonyms=DL2 {ECO:0000303|PubMed:16475980};
GN ORFNames=CG33532 {ECO:0000312|FlyBase:FBgn0053532};
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|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 [2] {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 [3] {ECO:0000312|EMBL:BAD51433.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-186, 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 [4] {ECO:0000312|EMBL:AAY55758.1, ECO:0000312|EMBL:AAY55802.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-186.
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2005) 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 larvae and expressed from the late
CC pupal stage onwards. Highest levels of expression in adults.
CC {ECO:0000269|PubMed:16475980}.
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DR EMBL; AE014134; AAX52669.1; -; Genomic_DNA.
DR EMBL; AE014134; ADV37095.1; -; Genomic_DNA.
DR EMBL; AB190811; BAD51433.1; -; mRNA.
DR EMBL; BT023342; AAY55758.1; -; mRNA.
DR EMBL; BT023386; AAY55802.1; -; mRNA.
DR RefSeq; NP_001014489.1; NM_001014489.2.
DR RefSeq; NP_001188846.1; NM_001201917.1.
DR AlphaFoldDB; Q59DY6; -.
DR SMR; Q59DY6; -.
DR STRING; 7227.FBpp0099709; -.
DR GlyGen; Q59DY6; 2 sites.
DR PaxDb; Q59DY6; -.
DR EnsemblMetazoa; FBtr0091498; FBpp0099709; FBgn0053532.
DR EnsemblMetazoa; FBtr0302361; FBpp0291557; FBgn0053532.
DR GeneID; 3346222; -.
DR KEGG; dme:Dmel_CG33532; -.
DR UCSC; CG33532-RA; d. melanogaster.
DR CTD; 3346222; -.
DR FlyBase; FBgn0053532; lectin-37Da.
DR VEuPathDB; VectorBase:FBgn0053532; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00650000093533; -.
DR HOGENOM; CLU_049894_13_2_1; -.
DR InParanoid; Q59DY6; -.
DR OMA; VTIKRWA; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; Q59DY6; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 3346222; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3346222; -.
DR PRO; PR:Q59DY6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0053532; Expressed in adult Malpighian tubule (Drosophila) and 12 other tissues.
DR ExpressionAtlas; Q59DY6; 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..186
FT /note="C-type lectin 37Da"
FT /id="PRO_5007209829"
FT DOMAIN 46..169
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 140..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 186 AA; 21380 MW; E723B2026051DBCF CRC64;
MLKTLVQLFL VVAGFAPGFG YDKYTTHIQN GNPYNLTVDM TPFIKINESY YVFGQTKVNW
YVAYENCRRL QSELVTFETA EEFDAIAAFL NARGDRSEHW TSGNDLGKTG THYWFSNAQL
VTIKRWAPKQ PDNAGGREHC IHLGYIYGYS TEFQLNDRPC HNHASSLFKY ICEAPKQETV
SIVVWK
