Q9VQB7 (EOGT_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Eogt
ORF Names:	CG9867

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	520 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	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 reveal disruption of the deposition zone of the endocuticle, leading to separation of the epidermis from the chitin layers. Ref.1

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	larval chitin-based cuticle development Inferred from mutant phenotype Ref.1. Source: FlyBase protein O-GlcNAcylation via threonine Inferred from mutant phenotype Ref.1. Source: FlyBase
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	protein N-acetylglucosaminyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB protein O-GlcNAc transferase activity Inferred from direct assay Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 520	504	EGF domain-specific O-linked N-acetylglucosamine transferase		PRO_0000418382
Regions
	Motif	517 – 520	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	176	1	N-linked (GlcNAc...) Potential
	Glycosylation	250	1	N-linked (GlcNAc...) Potential
	Glycosylation	479	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9VQB7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FE00E75C153E733E	FASTA	520	60,083
	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

References

	« Hide 'large scale' referencesShow '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, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[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]	"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] [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.
RefSeq	NP_001259934.1. NM_001273005.1. NP_608678.1. NM_134834.3.
UniGene	Dm.4320.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT61. Glycosyltransferase Family 61.
Proteomic databases
PRIDE	Q9VQB7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077767; FBpp0077447; FBgn0264672. FBtr0330685; FBpp0303533; FBgn0264672.
GeneID	33424.
KEGG	dme:Dmel_CG9867.
UCSC	CG9867-RA. d. melanogaster.
Organism-specific databases
CTD	285203.
FlyBase	FBgn0031421. CG9867.
Phylogenomic databases
eggNOG	NOG320328.
GeneTree	ENSGT00390000008553.
InParanoid	Q9VQB7.
OMA	DSKRVCF.
OrthoDB	EOG4R4XHX.
PhylomeDB	Q9VQB7.
Gene expression databases
Bgee	Q9VQB7.
Family and domain databases
InterPro	IPR007657. Glycosyltransferase_AER61. [Graphical view]
Pfam	PF04577. DUF563. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	33424.
NextBio	783494.

Entry information

Entry name

EOGT_DROME

Accession

Primary (citable) accession number: Q9VQB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2012
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project