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   27-MAR-2024, entry version 161.
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>3.3.co;2-k;
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 Head
RC   {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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q8WSF3; 3 sites, No reported glycans.
DR   GlyGen; Q8WSF3; 3 sites.
DR   PaxDb; 7227-FBpp0087058; -.
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   AGR; FB:FBgn0045063; -.
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; NTDCWTN; -.
DR   OrthoDB; 3388043at2759; -.
DR   PhylomeDB; Q8WSF3; -.
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   Reactome; R-DME-9840310; Glycosphingolipid catabolism.
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 cell types or tissues.
DR   ExpressionAtlas; Q8WSF3; baseline and differential.
DR   GO; GO:0005770; C:late endosome; IDA:FlyBase.
DR   GO; GO:0005764; C:lysosome; 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:0006689; P:ganglioside catabolic process; IBA:GO_Central.
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   CDD; cd06562; GH20_HexA_HexB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF3; BETA-HEXOSAMINIDASE FDL-RELATED; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   Genevisible; Q8WSF3; DM.
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
//