Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

EGF domain-specific O-linked N-acetylglucosamine transferase

Gene

Eogt

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

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cation1 Publication

GO - Molecular functioni

  1. protein N-acetylglucosaminyltransferase activity Source: UniProtKB
  2. protein O-GlcNAc transferase activity Source: FlyBase

GO - Biological processi

  1. larval chitin-based cuticle development Source: FlyBase
  2. metabolic process Source: UniProtKB
  3. protein O-GlcNAcylation via threonine Source: FlyBase
  4. protein O-linked glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGT61. Glycosyltransferase Family 61.

Names & Taxonomyi

Protein namesi
Recommended name:
EGF domain-specific O-linked N-acetylglucosamine transferase (EC:2.4.1.255)
Alternative name(s):
Extracellular O-linked N-acetylglucosamine transferase
Gene namesi
Name:Eogt
ORF Names:CG9867
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0264672. Eogt.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 520504EGF domain-specific O-linked N-acetylglucosamine transferasePRO_0000418382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9VQB7.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ9VQB7.
ExpressionAtlasiQ9VQB7. differential.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0077447.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi292 – 2943Required for optimal activityBy similarity
Motifi517 – 5204Prevents secretion from ERPROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320328.
GeneTreeiENSGT00770000120599.
InParanoidiQ9VQB7.
KOiK18134.
OMAiDSKRVCF.
OrthoDBiEOG7D2FDQ.
PhylomeDBiQ9VQB7.

Family and domain databases

InterProiIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamiPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9VQB7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPILPILIGI LHLSLAEDAK HLDGFSLPSL PSEHLIRYLN TFPKLKQQLP
60 70 80 90 100
TNLTGKGTIS SACWGHERDC TPAGRFQTPQ CPGEHTGWAR SKEAQVRTFY
110 120 130 140 150
NQADFGYIQE QLSQLTPQCV PTYLGDSSLE CTHYLRFCRG RNLLFDFRGL
160 170 180 190 200
EQREERIRYH MDVLGPGQLL GHCKLNRTRL SGEMEHIGSA LQSWGPELRN
210 220 230 240 250
FDVLPHPVLE SGLCDVVVNT PTFIMKIDAT YNMYHHFCDF FNLYASLFVN
260 270 280 290 300
QSHPAAFNTD VQILIWETYP YDSPFRDTFK AFSQRPVWTL SDVEGKRVCF
310 320 330 340 350
KNVVLPLLPR MIFGLFYNTP IIQGCSNSGL FRAFSEFILH RLQIPYKPPQ
360 370 380 390 400
QKIRITYLSR RTKYRQVLNE DELLAPLEAN DKYDVQRVSY ERLPFTNQLA
410 420 430 440 450
ITRNTDILIG MHGAGLTHLL FLPNWACIFE LYNCEDPNCY KDLARLRGVR
460 470 480 490 500
YRTWEQRDLV YPQDEGHHPE GGAHAKFTNY SFDVKEFVHL VDGAAEEILS
510 520
HKEFPRRASE NPSKTQRNEL
Length:520
Mass (Da):60,083
Last modified:May 1, 2000 - v1
Checksum:iFE00E75C153E733E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB675601 mRNA. Translation: BAL41443.1.
AE014134 Genomic DNA. Translation: AAF51259.1.
AY058292 mRNA. Translation: AAL13521.1.
RefSeqiNP_001259934.1. NM_001273005.1.
NP_608678.1. NM_134834.3.
UniGeneiDm.4320.

Genome annotation databases

EnsemblMetazoaiFBtr0077767; FBpp0077447; FBgn0264672.
FBtr0330685; FBpp0303533; FBgn0264672.
GeneIDi33424.
KEGGidme:Dmel_CG9867.
UCSCiCG9867-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB675601 mRNA. Translation: BAL41443.1.
AE014134 Genomic DNA. Translation: AAF51259.1.
AY058292 mRNA. Translation: AAL13521.1.
RefSeqiNP_001259934.1. NM_001273005.1.
NP_608678.1. NM_134834.3.
UniGeneiDm.4320.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0077447.

Protein family/group databases

CAZyiGT61. Glycosyltransferase Family 61.

Proteomic databases

PRIDEiQ9VQB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077767; FBpp0077447; FBgn0264672.
FBtr0330685; FBpp0303533; FBgn0264672.
GeneIDi33424.
KEGGidme:Dmel_CG9867.
UCSCiCG9867-RA. d. melanogaster.

Organism-specific databases

CTDi285203.
FlyBaseiFBgn0264672. Eogt.

Phylogenomic databases

eggNOGiNOG320328.
GeneTreeiENSGT00770000120599.
InParanoidiQ9VQB7.
KOiK18134.
OMAiDSKRVCF.
OrthoDBiEOG7D2FDQ.
PhylomeDBiQ9VQB7.

Miscellaneous databases

GenomeRNAii33424.
NextBioi783494.
PROiQ9VQB7.

Gene expression databases

BgeeiQ9VQB7.
ExpressionAtlasiQ9VQB7. differential.

Family and domain databases

InterProiIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamiPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiEOGT_DROME
AccessioniPrimary (citable) accession number: Q9VQB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 94 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

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.