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Q9VQB7

- EOGT_DROME

UniProt

Q9VQB7 - EOGT_DROME

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Protein

EGF domain-specific O-linked N-acetylglucosamine transferase

Gene
Eogt, CG9867
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.

Cofactori

Divalent metal ions.1 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 Publication

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 – 1616 Reviewed predictionAdd
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...) Reviewed prediction
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi250 – 2501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi479 – 4791N-linked (GlcNAc...) Reviewed prediction

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.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0077447.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi292 – 2943Required for optimal activity By similarity
Motifi517 – 5204Prevents secretion from ER Reviewed prediction

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320328.
GeneTreeiENSGT00750000117715.
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

MPILPILIGI LHLSLAEDAK HLDGFSLPSL PSEHLIRYLN TFPKLKQQLP    50
TNLTGKGTIS SACWGHERDC TPAGRFQTPQ CPGEHTGWAR SKEAQVRTFY 100
NQADFGYIQE QLSQLTPQCV PTYLGDSSLE CTHYLRFCRG RNLLFDFRGL 150
EQREERIRYH MDVLGPGQLL GHCKLNRTRL SGEMEHIGSA LQSWGPELRN 200
FDVLPHPVLE SGLCDVVVNT PTFIMKIDAT YNMYHHFCDF FNLYASLFVN 250
QSHPAAFNTD VQILIWETYP YDSPFRDTFK AFSQRPVWTL SDVEGKRVCF 300
KNVVLPLLPR MIFGLFYNTP IIQGCSNSGL FRAFSEFILH RLQIPYKPPQ 350
QKIRITYLSR RTKYRQVLNE DELLAPLEAN DKYDVQRVSY ERLPFTNQLA 400
ITRNTDILIG MHGAGLTHLL FLPNWACIFE LYNCEDPNCY KDLARLRGVR 450
YRTWEQRDLV YPQDEGHHPE GGAHAKFTNY SFDVKEFVHL VDGAAEEILS 500
HKEFPRRASE NPSKTQRNEL 520
Length:520
Mass (Da):60,083
Last modified:May 1, 2000 - v1
Checksum:iFE00E75C153E733E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB675601 mRNA. Translation: BAL41443.1 .
AE014134 Genomic DNA. Translation: AAF51259.1 .
AY058292 mRNA. Translation: AAL13521.1 .
RefSeqi NP_001259934.1. NM_001273005.1.
NP_608678.1. NM_134834.3.
UniGenei Dm.4320.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0077447.

Protein family/group databases

CAZyi GT61. Glycosyltransferase Family 61.

Proteomic databases

PRIDEi Q9VQB7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0077767 ; FBpp0077447 ; FBgn0264672 .
FBtr0330685 ; FBpp0303533 ; FBgn0264672 .
GeneIDi 33424.
KEGGi dme:Dmel_CG9867.
UCSCi CG9867-RA. d. melanogaster.

Organism-specific databases

CTDi 285203.
FlyBasei FBgn0264672. Eogt.

Phylogenomic databases

eggNOGi NOG320328.
GeneTreei ENSGT00750000117715.
InParanoidi Q9VQB7.
KOi K18134.
OMAi DSKRVCF.
OrthoDBi EOG7D2FDQ.
PhylomeDBi Q9VQB7.

Miscellaneous databases

GenomeRNAii 33424.
NextBioi 783494.
PROi Q9VQB7.

Gene expression databases

Bgeei Q9VQB7.

Family and domain databases

InterProi IPR007657. Glycosyltransferase_AER61.
[Graphical view ]
Pfami PF04577. DUF563. 1 hit.
[Graphical view ]
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 90 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

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