Q8WSF3 (FDL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable beta-hexosaminidase fdl
EC=3.2.1.52

Alternative name(s):
Protein fused lobes

Gene names

Name:	fdl
ORF Names:	CG8824

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in brain restructurization via hormonal control during metamorphosis. Implicated in N-glycan processing. Ref.1 Ref.5
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. UniProtKB P49010
Tissue specificity	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. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.
Sequence caution	The sequence AAL28585.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Developmental protein Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-glycan processing Inferred from mutant phenotype. Source: FlyBase brain development Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular component	late endosome Inferred from direct assay. Source: FlyBase plasma membrane Inferred from direct assay. Source: FlyBase
Molecular function	beta-N-acetylglucosaminidase activity Inferred from direct assay. Source: FlyBase cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform C (identifier: Q8WSF3-1)

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.

Isoform B (identifier: Q8WSF3-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Potential
	Chain	37 – 660	624	Probable beta-hexosaminidase fdl		PRO_0000012017
Amino acid modifications
	Glycosylation	210	1	N-linked (GlcNAc...) Potential
	Glycosylation	412	1	N-linked (GlcNAc...) Potential
	Glycosylation	452	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1	1	M → MRYVYESLRYLYKM in isoform B.		VSP_011911
Experimental info
	Sequence conflict	154	1	V → G in AAM29423. Ref.4
	Sequence conflict	495	1	C → R in AAM29423. Ref.4
	Sequence conflict	551	1	P → Q in AAM29423. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform C [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 0F14B47C9A55CD74	FASTA	660	75,486
	10 20 30 40 50 60 MSLAVSLRRA LLVLLTGAIF ILTVLYWNQG VTKAQAYNEA LERPHSHHDA SGFPIPVEKS 70 80 90 100 110 120 WTYKCENDRC MRVGHHGKSA KRVSFISCSM TCGDVNIWPH PTQKFLLSSQ THSFSVEDVQ 130 140 150 160 170 180 LHVDTAHREV RKQLQLAFDW FLKDLRLIQR LDYVGSSSEP TVSESSSKSR HHADLEPAAT 190 200 210 220 230 240 LFGATFGVKK AGDLTSVQVK ISVLKSGDLN FSLDNDETYQ LSTQTEGHRL QVEIIANSYF 250 260 270 280 290 300 GARHGLSTLQ QLIWFDDEDH LLHTYANSKV KDAPKFRYRG LMLDTSRHFF SVESIKRTIV 310 320 330 340 350 360 GMGLAKMNRF HWHLTDAQSF PYISRYYPEL AVHGAYSESE TYSEQDVREV AEFAKIYGVQ 370 380 390 400 410 420 VIPEIDAPAH AGNGWDWGPK RGMGELAMCI NQQPWSFYCG EPPCGQLNPK NNYTYLILQR 430 440 450 460 470 480 IYEELLQHTG PTDFFHLGGD EVNLDCWAQY FNDTDLRGLW CDFMLQAMAR LKLANNGVAP 490 500 510 520 530 540 KHVAVWSSAL TNTKCLPNSQ FTVQVWGGST WQENYDLLDN GYNVIFSHVD AWYLDCGFGS 550 560 570 580 590 600 WRATGDAACA PYRTWQNVYK HRPWERMRLD KKRKKQVLGG EVCMWTEQVD ENQLDNRLWP 610 620 630 640 650 660 RTAALAERLW TDPSDDHDMD IVPPDVFRRI SLFRNRLVEL GIRAEALFPK YCAQNPGECI
	Isoform B [UniParc]. Checksum: 7A73275BB491AE7D	FASTA	673	77,252
	10 20 30 40 50 60 MRYVYESLRY LYKMSLAVSL RRALLVLLTG AIFILTVLYW NQGVTKAQAY NEALERPHSH 70 80 90 100 110 120 HDASGFPIPV EKSWTYKCEN DRCMRVGHHG KSAKRVSFIS CSMTCGDVNI WPHPTQKFLL 130 140 150 160 170 180 SSQTHSFSVE DVQLHVDTAH REVRKQLQLA FDWFLKDLRL IQRLDYVGSS SEPTVSESSS 190 200 210 220 230 240 KSRHHADLEP AATLFGATFG VKKAGDLTSV QVKISVLKSG DLNFSLDNDE TYQLSTQTEG 250 260 270 280 290 300 HRLQVEIIAN SYFGARHGLS TLQQLIWFDD EDHLLHTYAN SKVKDAPKFR YRGLMLDTSR 310 320 330 340 350 360 HFFSVESIKR TIVGMGLAKM NRFHWHLTDA QSFPYISRYY PELAVHGAYS ESETYSEQDV 370 380 390 400 410 420 REVAEFAKIY GVQVIPEIDA PAHAGNGWDW GPKRGMGELA MCINQQPWSF YCGEPPCGQL 430 440 450 460 470 480 NPKNNYTYLI LQRIYEELLQ HTGPTDFFHL GGDEVNLDCW AQYFNDTDLR GLWCDFMLQA 490 500 510 520 530 540 MARLKLANNG VAPKHVAVWS SALTNTKCLP NSQFTVQVWG GSTWQENYDL LDNGYNVIFS 550 560 570 580 590 600 HVDAWYLDCG FGSWRATGDA ACAPYRTWQN VYKHRPWERM RLDKKRKKQV LGGEVCMWTE 610 620 630 640 650 660 QVDENQLDNR LWPRTAALAE RLWTDPSDDH DMDIVPPDVF RRISLFRNRL VELGIRAEAL 670 FPKYCAQNPG ECI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10623899] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). Strain: Berkeley. Tissue: Embryo and Head.
[5]	Leonard R., Altmann F. Submitted (APR-2003) to UniProtKB Cited for: FUNCTION IN N-GLYCAN PROCESSING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_725178.2. NM_165908.1. NP_725179.1. NM_165909.2.
UniGene	Dm.3735.
3D structure databases
ProteinModelPortal	Q8WSF3.
SMR	Q8WSF3. Positions 57-660.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21467N.
MINT	MINT-1665363.
STRING	Q8WSF3.
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PRIDE	Q8WSF3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087946; FBpp0087057; FBgn0045063.
GeneID	250735.
KEGG	dme:Dmel_CG8824.
Organism-specific databases
CTD	250735.
FlyBase	FBgn0045063. fdl.
Phylogenomic databases
eggNOG	inNOG04701.
GeneTree	EMGT00050000013125.
InParanoid	Q8WSF3.
OMA	VYKHRPW.
OrthoDB	EOG4JDFNT.
PhylomeDB	Q8WSF3.
Gene expression databases
Bgee	Q8WSF3.
GermOnline	CG8824. Drosophila melanogaster.
Family and domain databases
InterPro	IPR015882. Acetylhexosaminidase_sua/b. IPR001540. Glyco_hydro_20. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K12373.
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	843498.

Entry information

Entry name

FDL_DROME

Accession

Primary (citable) accession number: Q8WSF3
Secondary accession number(s): Q8MZ16, Q95RY8, Q9V6C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project