FDL_DROME
ID FDL_DROME Reviewed; 660 AA.
AC Q8WSF3; Q8MZ16; Q95RY8; Q9V6C8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable beta-hexosaminidase fdl;
DE EC=3.2.1.52;
DE AltName: Full=Protein fused lobes;
DE Flags: Precursor;
GN Name=fdl; ORFNames=CG8824;
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|EMBL:AAL55992.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE (ISOFORM C), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10623899;
RX DOI=10.1002/(sici)1097-4695(200001)42:1<33::aid-neu4>3.0.co;2-t;
RA Boquet I., Hitier R., Dumas M., Chaminade M., Preat T.;
RT "Central brain postembryonic development in Drosophila: implication of
RT genes expressed at the interhemispheric junction.";
RL J. Neurobiol. 42:33-48(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29423.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM29423.1}, and
RC Head {ECO:0000312|EMBL:AAL28585.1};
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]
RP FUNCTION IN N-GLYCAN PROCESSING.
RA Leonard R., Altmann F.;
RL Submitted (APR-2003) to UniProtKB.
CC -!- FUNCTION: Involved in brain restructurization via hormonal control
CC during metamorphosis. Implicated in N-glycan processing.
CC {ECO:0000269|PubMed:10623899, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000250|UniProtKB:P49010};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C;
CC IsoId=Q8WSF3-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q8WSF3-2; Sequence=VSP_011911;
CC -!- TISSUE SPECIFICITY: In third instar larval and early pupal brains,
CC expressed in cells sending projections across the interhemispheric
CC junction. In adult brain, expressed in mushroom body, ellipsoid body
CC and pars intercerebralis. {ECO:0000269|PubMed:10623899}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF323977; AAL55992.1; -; mRNA.
DR EMBL; AE013599; AAM68691.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68692.1; -; Genomic_DNA.
DR EMBL; AY113418; AAM29423.1; -; mRNA.
DR EMBL; AY061037; AAL28585.1; ALT_INIT; mRNA.
DR RefSeq; NP_001286350.1; NM_001299421.1. [Q8WSF3-1]
DR RefSeq; NP_725178.2; NM_165908.2. [Q8WSF3-2]
DR RefSeq; NP_725179.1; NM_165909.3. [Q8WSF3-1]
DR AlphaFoldDB; Q8WSF3; -.
DR SMR; Q8WSF3; -.
DR BioGRID; 75345; 4.
DR DIP; DIP-21467N; -.
DR IntAct; Q8WSF3; 2.
DR STRING; 7227.FBpp0087058; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR GlyGen; Q8WSF3; 3 sites.
DR PaxDb; Q8WSF3; -.
DR EnsemblMetazoa; FBtr0087946; FBpp0087057; FBgn0045063. [Q8WSF3-1]
DR EnsemblMetazoa; FBtr0087947; FBpp0087058; FBgn0045063. [Q8WSF3-2]
DR EnsemblMetazoa; FBtr0346633; FBpp0312213; FBgn0045063. [Q8WSF3-1]
DR GeneID; 250735; -.
DR KEGG; dme:Dmel_CG8824; -.
DR CTD; 250735; -.
DR FlyBase; FBgn0045063; fdl.
DR VEuPathDB; VectorBase:FBgn0045063; -.
DR eggNOG; KOG2499; Eukaryota.
DR GeneTree; ENSGT00390000008107; -.
DR HOGENOM; CLU_007082_0_1_1; -.
DR InParanoid; Q8WSF3; -.
DR OMA; TYKCENE; -.
DR PhylomeDB; Q8WSF3; -.
DR Reactome; R-DME-1660662; Glycosphingolipid metabolism.
DR Reactome; R-DME-2022857; Keratan sulfate degradation.
DR Reactome; R-DME-2024101; CS/DS degradation.
DR Reactome; R-DME-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q8WSF3; -.
DR BioGRID-ORCS; 250735; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 250735; -.
DR PRO; PR:Q8WSF3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0045063; Expressed in egg cell and 25 other tissues.
DR ExpressionAtlas; Q8WSF3; baseline and differential.
DR Genevisible; Q8WSF3; DM.
DR GO; GO:0005770; C:late endosome; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:FlyBase.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; ISS:UniProtKB.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR GO; GO:0006491; P:N-glycan processing; IMP:FlyBase.
DR GO; GO:0006517; P:protein deglycosylation; IMP:FlyBase.
DR GO; GO:0016063; P:rhodopsin biosynthetic process; IMP:FlyBase.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..660
FT /note="Probable beta-hexosaminidase fdl"
FT /id="PRO_0000012017"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MRYVYESLRYLYKM (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_011911"
FT CONFLICT 154
FT /note="V -> G (in Ref. 4; AAM29423)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="C -> R (in Ref. 4; AAM29423)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="P -> Q (in Ref. 4; AAM29423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75486 MW; 0F14B47C9A55CD74 CRC64;
MSLAVSLRRA LLVLLTGAIF ILTVLYWNQG VTKAQAYNEA LERPHSHHDA SGFPIPVEKS
WTYKCENDRC MRVGHHGKSA KRVSFISCSM TCGDVNIWPH PTQKFLLSSQ THSFSVEDVQ
LHVDTAHREV RKQLQLAFDW FLKDLRLIQR LDYVGSSSEP TVSESSSKSR HHADLEPAAT
LFGATFGVKK AGDLTSVQVK ISVLKSGDLN FSLDNDETYQ LSTQTEGHRL QVEIIANSYF
GARHGLSTLQ QLIWFDDEDH LLHTYANSKV KDAPKFRYRG LMLDTSRHFF SVESIKRTIV
GMGLAKMNRF HWHLTDAQSF PYISRYYPEL AVHGAYSESE TYSEQDVREV AEFAKIYGVQ
VIPEIDAPAH AGNGWDWGPK RGMGELAMCI NQQPWSFYCG EPPCGQLNPK NNYTYLILQR
IYEELLQHTG PTDFFHLGGD EVNLDCWAQY FNDTDLRGLW CDFMLQAMAR LKLANNGVAP
KHVAVWSSAL TNTKCLPNSQ FTVQVWGGST WQENYDLLDN GYNVIFSHVD AWYLDCGFGS
WRATGDAACA PYRTWQNVYK HRPWERMRLD KKRKKQVLGG EVCMWTEQVD ENQLDNRLWP
RTAALAERLW TDPSDDHDMD IVPPDVFRRI SLFRNRLVEL GIRAEALFPK YCAQNPGECI
