GLEC_DROME
ID GLEC_DROME Reviewed; 228 AA.
AC Q9VD73; A9UNC5; Q24166; Q8T0Q9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Gliolectin {ECO:0000303|PubMed:8631270};
GN Name=glec {ECO:0000312|EMBL:AAF55926.1}; ORFNames=CG6575;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB04114.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAB04114.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:8631270};
RX PubMed=8631270; DOI=10.1242/dev.122.3.925;
RA Tiemeyer M., Goodman C.S.;
RT "Gliolectin is a novel carbohydrate-binding protein expressed by a subset
RT of glia in the embryonic Drosophila nervous system.";
RL Development 122:925-936(1996).
RN [2] {ECO:0000312|EMBL:AAF55926.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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:0000305, ECO:0000312|EMBL:AAF55926.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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:0000305, ECO:0000312|EMBL:AAL39267.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:ABY20530.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABY20530.1}; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11714683; DOI=10.1242/dev.128.22.4585;
RA Sharrow M., Tiemeyer M.;
RT "Gliolectin-mediated carbohydrate binding at the Drosophila midline ensures
RT the fidelity of axon pathfinding.";
RL Development 128:4585-4595(2001).
CC -!- FUNCTION: Has a role in intercellular carbohydrate-mediated cell
CC adhesion. {ECO:0000269|PubMed:11714683, ECO:0000269|PubMed:8631270}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8631270}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:8631270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:8631270};
CC IsoId=Q9VD73-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:12537569};
CC IsoId=Q9VD73-2; Sequence=VSP_052894;
CC -!- TISSUE SPECIFICITY: Expressed by a subset of glial cells found at the
CC midline of the embryo stage 12 nervous system. Expression is highest
CC during the formation of the embryonic axonal commissures, a process
CC requiring midline glial cell function (at protein level).
CC {ECO:0000269|PubMed:11714683, ECO:0000269|PubMed:8631270}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit disruption of the formation of
CC commissural pathways and shows delays the completion of longitudinal
CC pathfinding. The disruption in commissure formation is accompanied by
CC reduced axon-glial contact, such that extending axons grow on other
CC axons and form a tightly fasciculated bundle that arches over the
CC midline. {ECO:0000269|PubMed:11714683}.
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DR EMBL; U42989; AAB04114.1; -; mRNA.
DR EMBL; AE014297; AAF55926.1; -; Genomic_DNA.
DR EMBL; AY069122; AAL39267.1; -; mRNA.
DR EMBL; BT031289; ABY20530.1; -; mRNA.
DR RefSeq; NP_524443.2; NM_079719.3. [Q9VD73-1]
DR AlphaFoldDB; Q9VD73; -.
DR SMR; Q9VD73; -.
DR BioGRID; 67533; 3.
DR IntAct; Q9VD73; 8.
DR STRING; 7227.FBpp0083555; -.
DR GlyGen; Q9VD73; 6 sites.
DR PaxDb; Q9VD73; -.
DR DNASU; 42571; -.
DR EnsemblMetazoa; FBtr0084157; FBpp0083555; FBgn0015229. [Q9VD73-1]
DR GeneID; 42571; -.
DR KEGG; dme:Dmel_CG6575; -.
DR UCSC; CG6575-RA; d. melanogaster. [Q9VD73-1]
DR CTD; 42571; -.
DR FlyBase; FBgn0015229; glec.
DR VEuPathDB; VectorBase:FBgn0015229; -.
DR HOGENOM; CLU_1251842_0_0_1; -.
DR InParanoid; Q9VD73; -.
DR OMA; NSTRHGQ; -.
DR PhylomeDB; Q9VD73; -.
DR BioGRID-ORCS; 42571; 0 hits in 1 CRISPR screen.
DR ChiTaRS; glec; fly.
DR GenomeRNAi; 42571; -.
DR PRO; PR:Q9VD73; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015229; Expressed in brain and 30 other tissues.
DR ExpressionAtlas; Q9VD73; baseline and differential.
DR Genevisible; Q9VD73; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Lectin; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..228
FT /note="Gliolectin"
FT /id="PRO_0000347283"
FT TOPO_DOM 1..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..137
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 141..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 175..228
FT /note="MYNVRKTVNGISKPNVKNGYNNNNNSSSSNNNSNMNINNKIVDNGTSELADQ
FT KQ -> RFFFSMICMFLFHLKRWVLAQNIRIMITLWFQVIKFNILSSYC (in
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_052894"
FT CONFLICT 49
FT /note="Q -> H (in Ref. 5; ABY20530)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="A -> P (in Ref. 1; AAB04114)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> T (in Ref. 1; AAB04114)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="K -> Q (in Ref. 1; AAB04114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 24933 MW; 410BE79D4569B5BF CRC64;
MLCPPMALGP FLAAPVPRPP PSASEKKRIC RNLFNNAPGD SNIDQLLAQE QHTQRLYVKE
RYGYDIQLES NRDADANTDA DADTDAHCQV LRGMRYPTSR TISSTDADEC NPKAVSQAPR
GMALTPAQIS ASAKLILQKC PESDRKKSNG SADLANCTRH GQKPYARQPQ GLKGMYNVRK
TVNGISKPNV KNGYNNNNNS SSSNNNSNMN INNKIVDNGT SELADQKQ
