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Q9VQB7 (EOGT_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EGF domain-specific O-linked N-acetylglucosamine transferase

EC=2.4.1.255
Alternative name(s):
Extracellular O-linked N-acetylglucosamine transferase
Gene names
Name:Eogt
ORF Names:CG9867
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. Involved in epithelial cell adhesion/interaction with the extracellular matrix by mediating glycosylation of proteins in the secretory pathway, such as Dumpy (Dp). Ref.1

Catalytic activity

UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine. Ref.1

UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.

Cofactor

Divalent metal ions. Ref.1

Subcellular location

Endoplasmic reticulum lumen Ref.1.

Developmental stage

Expressed both maternally and zygotically. Highly expressed in preblastoderm-stage embryos. During the later stages of embryogenesis, expression is ubiquitous with the level progressively decreasing. Ref.1

Disruption phenotype

Defects in apical extracellular matrix. Embryos show defects in the formation of the innermost layer of the apical extracellular matrix and its attachment to the epidermis. Most larvae die during second-instar or second/third-instar interface, but some survive until early third-instar. Surviving larvae display cuticle defect and irregular tracheal morphology. Ultrastructural analysis of larval epidermis reveals disruption of the deposition zone of the endocuticle, leading to separation of the epidermis from the chitin layers. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 520504EGF domain-specific O-linked N-acetylglucosamine transferase
PRO_0000418382

Regions

Motif517 – 5204Prevents secretion from ER Potential

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9VQB7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FE00E75C153E733E

FASTA52060,083
        10         20         30         40         50         60 
MPILPILIGI LHLSLAEDAK HLDGFSLPSL PSEHLIRYLN TFPKLKQQLP TNLTGKGTIS 

        70         80         90        100        110        120 
SACWGHERDC TPAGRFQTPQ CPGEHTGWAR SKEAQVRTFY NQADFGYIQE QLSQLTPQCV 

       130        140        150        160        170        180 
PTYLGDSSLE CTHYLRFCRG RNLLFDFRGL EQREERIRYH MDVLGPGQLL GHCKLNRTRL 

       190        200        210        220        230        240 
SGEMEHIGSA LQSWGPELRN FDVLPHPVLE SGLCDVVVNT PTFIMKIDAT YNMYHHFCDF 

       250        260        270        280        290        300 
FNLYASLFVN QSHPAAFNTD VQILIWETYP YDSPFRDTFK AFSQRPVWTL SDVEGKRVCF 

       310        320        330        340        350        360 
KNVVLPLLPR MIFGLFYNTP IIQGCSNSGL FRAFSEFILH RLQIPYKPPQ QKIRITYLSR 

       370        380        390        400        410        420 
RTKYRQVLNE DELLAPLEAN DKYDVQRVSY ERLPFTNQLA ITRNTDILIG MHGAGLTHLL 

       430        440        450        460        470        480 
FLPNWACIFE LYNCEDPNCY KDLARLRGVR YRTWEQRDLV YPQDEGHHPE GGAHAKFTNY 

       490        500        510        520 
SFDVKEFVHL VDGAAEEILS HKEFPRRASE NPSKTQRNEL 

« Hide

References

« Hide 'large scale' references
[1]"O-Linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions."
Sakaidani Y., Nomura T., Matsuura A., Ito M., Suzuki E., Murakami K., Nadano D., Matsuda T., Furukawa K., Okajima T.
Nat. Commun. 2:583-583(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[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. expand/collapse author list , 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]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB675601 mRNA. Translation: BAL41443.1.
AE014134 Genomic DNA. Translation: AAF51259.1.
AY058292 mRNA. Translation: AAL13521.1.
RefSeqNP_001259934.1. NM_001273005.1.
NP_608678.1. NM_134834.3.
UniGeneDm.4320.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0077447.

Protein family/group databases

CAZyGT61. Glycosyltransferase Family 61.

Proteomic databases

PRIDEQ9VQB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077767; FBpp0077447; FBgn0264672.
FBtr0330685; FBpp0303533; FBgn0264672.
GeneID33424.
KEGGdme:Dmel_CG9867.
UCSCCG9867-RA. d. melanogaster.

Organism-specific databases

CTD285203.
FlyBaseFBgn0264672. Eogt.

Phylogenomic databases

eggNOGNOG320328.
GeneTreeENSGT00750000117715.
InParanoidQ9VQB7.
OMADSKRVCF.
OrthoDBEOG7D2FDQ.
PhylomeDBQ9VQB7.

Gene expression databases

BgeeQ9VQB7.

Family and domain databases

InterProIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33424.
NextBio783494.
PROQ9VQB7.

Entry information

Entry nameEOGT_DROME
AccessionPrimary (citable) accession number: Q9VQB7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase