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Protein

Probable beta-hexosaminidase fdl

Gene

fdl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in brain restructurization via hormonal control during metamorphosis. Implicated in N-glycan processing.2 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.By similarity

GO - Molecular functioni

  1. beta-N-acetylglucosaminidase activity Source: FlyBase
  2. beta-N-acetylhexosaminidase activity Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. N-glycan processing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_180740. Keratan sulfate degradation.
REACT_180747. Glycosphingolipid metabolism.
REACT_180778. CS/DS degradation.
REACT_212275. Hyaluronan uptake and degradation.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-hexosaminidase fdl (EC:3.2.1.52)
Alternative name(s):
Protein fused lobes
Gene namesi
Name:fdl
ORF Names:CG8824
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0045063. fdl.

Subcellular locationi

GO - Cellular componenti

  1. late endosome Source: FlyBase
  2. plasma membrane Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence AnalysisAdd
BLAST
Chaini37 – 660624Probable beta-hexosaminidase fdlPRO_0000012017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8WSF3.
PRIDEiQ8WSF3.

Expressioni

Tissue specificityi

In third instar larval and early pupal brains, expressed in cells sending projections across the interhemispheric junction. In adult brain, expressed in mushroom body, ellipsoid body and pars intercerebralis.1 Publication

Gene expression databases

BgeeiQ8WSF3.
ExpressionAtlasiQ8WSF3. differential.

Interactioni

Protein-protein interaction databases

BioGridi75345. 4 interactions.
DIPiDIP-21467N.
MINTiMINT-1665363.
STRINGi7227.FBpp0087058.

Structurei

3D structure databases

ProteinModelPortaliQ8WSF3.
SMRiQ8WSF3. Positions 177-652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
InParanoidiQ8WSF3.
KOiK12373.
OMAiVYKHRPW.
OrthoDBiEOG79W94H.
PhylomeDBiQ8WSF3.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform C (identifier: Q8WSF3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLAVSLRRA LLVLLTGAIF ILTVLYWNQG VTKAQAYNEA LERPHSHHDA
60 70 80 90 100
SGFPIPVEKS WTYKCENDRC MRVGHHGKSA KRVSFISCSM TCGDVNIWPH
110 120 130 140 150
PTQKFLLSSQ THSFSVEDVQ LHVDTAHREV RKQLQLAFDW FLKDLRLIQR
160 170 180 190 200
LDYVGSSSEP TVSESSSKSR HHADLEPAAT LFGATFGVKK AGDLTSVQVK
210 220 230 240 250
ISVLKSGDLN FSLDNDETYQ LSTQTEGHRL QVEIIANSYF GARHGLSTLQ
260 270 280 290 300
QLIWFDDEDH LLHTYANSKV KDAPKFRYRG LMLDTSRHFF SVESIKRTIV
310 320 330 340 350
GMGLAKMNRF HWHLTDAQSF PYISRYYPEL AVHGAYSESE TYSEQDVREV
360 370 380 390 400
AEFAKIYGVQ VIPEIDAPAH AGNGWDWGPK RGMGELAMCI NQQPWSFYCG
410 420 430 440 450
EPPCGQLNPK NNYTYLILQR IYEELLQHTG PTDFFHLGGD EVNLDCWAQY
460 470 480 490 500
FNDTDLRGLW CDFMLQAMAR LKLANNGVAP KHVAVWSSAL TNTKCLPNSQ
510 520 530 540 550
FTVQVWGGST WQENYDLLDN GYNVIFSHVD AWYLDCGFGS WRATGDAACA
560 570 580 590 600
PYRTWQNVYK HRPWERMRLD KKRKKQVLGG EVCMWTEQVD ENQLDNRLWP
610 620 630 640 650
RTAALAERLW TDPSDDHDMD IVPPDVFRRI SLFRNRLVEL GIRAEALFPK
660
YCAQNPGECI
Length:660
Mass (Da):75,486
Last modified:March 1, 2002 - v1
Checksum:i0F14B47C9A55CD74
GO
Isoform B (identifier: Q8WSF3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRYVYESLRYLYKM

Note: No experimental confirmation available.

Show »
Length:673
Mass (Da):77,252
Checksum:i7A73275BB491AE7D
GO

Sequence cautioni

The sequence AAL28585.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541V → G in AAM29423 (PubMed:12537569).Curated
Sequence conflicti495 – 4951C → R in AAM29423 (PubMed:12537569).Curated
Sequence conflicti551 – 5511P → Q in AAM29423 (PubMed:12537569).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRYVYESLRYLYKM in isoform B. CuratedVSP_011911

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323977 mRNA. Translation: AAL55992.1.
AE013599 Genomic DNA. Translation: AAM68691.2.
AE013599 Genomic DNA. Translation: AAM68692.1.
AY113418 mRNA. Translation: AAM29423.1.
AY061037 mRNA. Translation: AAL28585.1. Different initiation.
RefSeqiNP_001286350.1. NM_001299421.1. [Q8WSF3-1]
NP_725178.2. NM_165908.2. [Q8WSF3-2]
NP_725179.1. NM_165909.3. [Q8WSF3-1]
UniGeneiDm.3735.

Genome annotation databases

EnsemblMetazoaiFBtr0087946; FBpp0087057; FBgn0045063. [Q8WSF3-1]
FBtr0346633; FBpp0312213; FBgn0045063. [Q8WSF3-1]
GeneIDi250735.
KEGGidme:Dmel_CG8824.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323977 mRNA. Translation: AAL55992.1.
AE013599 Genomic DNA. Translation: AAM68691.2.
AE013599 Genomic DNA. Translation: AAM68692.1.
AY113418 mRNA. Translation: AAM29423.1.
AY061037 mRNA. Translation: AAL28585.1. Different initiation.
RefSeqiNP_001286350.1. NM_001299421.1. [Q8WSF3-1]
NP_725178.2. NM_165908.2. [Q8WSF3-2]
NP_725179.1. NM_165909.3. [Q8WSF3-1]
UniGeneiDm.3735.

3D structure databases

ProteinModelPortaliQ8WSF3.
SMRiQ8WSF3. Positions 177-652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi75345. 4 interactions.
DIPiDIP-21467N.
MINTiMINT-1665363.
STRINGi7227.FBpp0087058.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbiQ8WSF3.
PRIDEiQ8WSF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087946; FBpp0087057; FBgn0045063. [Q8WSF3-1]
FBtr0346633; FBpp0312213; FBgn0045063. [Q8WSF3-1]
GeneIDi250735.
KEGGidme:Dmel_CG8824.

Organism-specific databases

CTDi250735.
FlyBaseiFBgn0045063. fdl.

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
InParanoidiQ8WSF3.
KOiK12373.
OMAiVYKHRPW.
OrthoDBiEOG79W94H.
PhylomeDBiQ8WSF3.

Enzyme and pathway databases

ReactomeiREACT_180740. Keratan sulfate degradation.
REACT_180747. Glycosphingolipid metabolism.
REACT_180778. CS/DS degradation.
REACT_212275. Hyaluronan uptake and degradation.

Miscellaneous databases

ChiTaRSifdl. fly.
GenomeRNAii250735.
NextBioi843498.

Gene expression databases

BgeeiQ8WSF3.
ExpressionAtlasiQ8WSF3. differential.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Central brain postembryonic development in Drosophila: implication of genes expressed at the interhemispheric junction."
    Boquet I., Hitier R., Dumas M., Chaminade M., Preat T.
    J. Neurobiol. 42:33-48(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM C), FUNCTION, TISSUE SPECIFICITY.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: BerkeleyImported.
    Tissue: EmbryoImported and HeadImported.
  5. Leonard R., Altmann F.
    Submitted (APR-2003) to UniProtKB
    Cited for: FUNCTION IN N-GLYCAN PROCESSING.

Entry informationi

Entry nameiFDL_DROME
AccessioniPrimary (citable) accession number: Q8WSF3
Secondary accession number(s): Q8MZ16, Q95RY8, Q9V6C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2002
Last modified: March 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.