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Q7KT91

- C3390_DROME

UniProt

Q7KT91 - C3390_DROME

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Protein

Non-lysosomal glucosylceramidase

Gene

CG33090

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide to free glucose and ceramide.By similarity

Catalytic activityi

D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB
  2. glucosylceramidase activity Source: UniProtKB-EC

GO - Biological processi

  1. bile acid metabolic process Source: UniProtKB
  2. glucosylceramide catabolic process Source: InterPro
  3. glycoside catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_180747. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH116. Glycoside Hydrolase Family 116.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-lysosomal glucosylceramidase (EC:3.2.1.45)
Short name:
NLGase
Gene namesi
ORF Names:CG33090
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0028916. CG33090.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 736736ExtracellularSequence AnalysisAdd
BLAST
Transmembranei737 – 75317HelicalSequence AnalysisAdd
BLAST
Topological domaini754 – 948195CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 948948Non-lysosomal glucosylceramidasePRO_0000283761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Modified residuei214 – 2141Phosphoserine1 Publication
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei669 – 6691Phosphoserine1 Publication
Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ7KT91.
PRIDEiQ7KT91.

Expressioni

Gene expression databases

BgeeiQ7KT91.
ExpressionAtlasiQ7KT91. differential.

Interactioni

Protein-protein interaction databases

BioGridi60860. 1 interaction.
STRINGi7227.FBpp0080197.

Structurei

3D structure databases

ProteinModelPortaliQ7KT91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4354.
GeneTreeiENSGT00390000010998.
InParanoidiQ7KT91.
KOiK17108.
OMAiEISITRC.
OrthoDBiEOG7ZGX2B.
PhylomeDBiQ7KT91.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view]
PfamiPF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view]
PIRSFiPIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMiSSF48208. SSF48208. 2 hits.

Sequencei

Sequence statusi: Complete.

Q7KT91-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEPLAVETK PLSNGNANGN AVGIAESASA VFQEKLKLQQ QEESNEIAAV
60 70 80 90 100
PKYGLKLKFD HVWPEKRIQN VRASIRQTLP MVPLVCRYAA YYWKVSREGR
110 120 130 140 150
RVYMDYYYME NGKQIYGVPI GGIGGGTIGR GYAGEFCRFQ MRPGIYEYNV
160 170 180 190 200
VLANQFIVTI KDPKGCTIFQ SLLSKCSTRD KTSDPDGDPD GERTKCQLPN
210 220 230 240 250
CSSRAKQPLS AWHSNIEDTR CSYTGLYPRS WTEYDLSHYG VRLTCRQVSP
260 270 280 290 300
VIPHEYRESS LPCAVFVWSV ENVCDQERKV SITFTFKNGT GNKKQDAEGG
310 320 330 340 350
AESQLISEGN AKGVSIRQKI SEMPCSYNLA CRVLPEISIT RCPQFDPAGN
360 370 380 390 400
GEQLWAQLKE HGQLSEHPTS EALKTKDIGV AVCGQVALKP MASHDLEFVL
410 420 430 440 450
AWDMPKIQFP RKMQTHTRYY TKYFDDSGDS GPRICEYALR QYSTWERLID
460 470 480 490 500
AWQRPILNDE TLPDWYKCAI FNQLYFISDG GTIWLKCDSS LGKELAYDDP
510 520 530 540 550
RLAYGRFGYL EGHEYRMYNT YDVHFYASPA LAHLWPNLQV SLQYDFKDAI
560 570 580 590 600
AAELNDTRKM LYDGKVMPRK VKNCVPHDLG DPDEEPFTLI NCYNIHDVND
610 620 630 640 650
WKDLNTKFVL QVYRDYYVLN ELAQAQSDNA SKFSSIEFID KESLYELYSQ
660 670 680 690 700
DNKRKNSADE KQQNRKSASM YINETNGKVY LMDAIGYLKA MYASCKAIME
710 720 730 740 750
RTIEYDKDND GLIENTKMPD QTYDSWVMDG PSAYCSGLWL AALQAMSAMA
760 770 780 790 800
TILDQPNDCL RYQDILEKGK RSLEEKLWNG SYYRFDLSHS HRDTIMADQL
810 820 830 840 850
CGHWYLKSCG FDYEIYPKEN VRTALKRIYD NNVMGFHEGN IGAANGFIAN
860 870 880 890 900
ASEPTKPGHV DNSNIQAEEV WPGVVYALAA TMIQEGMFEE AFQTAGGMYK
910 920 930 940
TLSQRIGMNF ETPEALYGEK RYRSIGYMRP LSIWSMQVAL ERRRAQRD
Length:948
Mass (Da):108,291
Last modified:July 5, 2004 - v1
Checksum:i095184C4EC0F0DD7
GO

Sequence cautioni

The sequence AAL13692.1 differs from that shown. Reason: Frameshift at position 887. Curated
The sequence AAL13692.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ABC86280.1 differs from that shown. Reason: Frameshift at position 526. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAO41192.2.
BT024218 mRNA. Translation: ABC86280.1. Frameshift.
BT044085 mRNA. Translation: ACH92150.1.
AY058463 mRNA. Translation: AAL13692.1. Sequence problems.
RefSeqiNP_788055.2. NM_176041.2.
UniGeneiDm.7918.

Genome annotation databases

EnsemblMetazoaiFBtr0080624; FBpp0080197; FBgn0028916.
GeneIDi34835.
KEGGidme:Dmel_CG33090.
UCSCiCG33090-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAO41192.2 .
BT024218 mRNA. Translation: ABC86280.1 . Frameshift.
BT044085 mRNA. Translation: ACH92150.1 .
AY058463 mRNA. Translation: AAL13692.1 . Sequence problems.
RefSeqi NP_788055.2. NM_176041.2.
UniGenei Dm.7918.

3D structure databases

ProteinModelPortali Q7KT91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60860. 1 interaction.
STRINGi 7227.FBpp0080197.

Protein family/group databases

CAZyi GH116. Glycoside Hydrolase Family 116.

Proteomic databases

PaxDbi Q7KT91.
PRIDEi Q7KT91.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080624 ; FBpp0080197 ; FBgn0028916 .
GeneIDi 34835.
KEGGi dme:Dmel_CG33090.
UCSCi CG33090-RB. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0028916. CG33090.

Phylogenomic databases

eggNOGi COG4354.
GeneTreei ENSGT00390000010998.
InParanoidi Q7KT91.
KOi K17108.
OMAi EISITRC.
OrthoDBi EOG7ZGX2B.
PhylomeDBi Q7KT91.

Enzyme and pathway databases

Reactomei REACT_180747. Glycosphingolipid metabolism.

Miscellaneous databases

GenomeRNAii 34835.
NextBioi 790459.
PROi Q7KT91.

Gene expression databases

Bgeei Q7KT91.
ExpressionAtlasi Q7KT91. differential.

Family and domain databases

InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view ]
Pfami PF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMi SSF48208. SSF48208. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-948.
    Strain: Berkeley.
    Tissue: Head.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-667 AND SER-669, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiC3390_DROME
AccessioniPrimary (citable) accession number: Q7KT91
Secondary accession number(s): B5RIG1, Q29R22, Q95TX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 77 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