EOGT_DROME
ID EOGT_DROME Reviewed; 520 AA.
AC Q9VQB7;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=EGF domain-specific O-linked N-acetylglucosamine transferase;
DE EC=2.4.1.255 {ECO:0000269|PubMed:22158438};
DE AltName: Full=Extracellular O-linked N-acetylglucosamine transferase;
DE Flags: Precursor;
GN Name=Eogt; ORFNames=CG9867;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22158438; DOI=10.1038/ncomms1591;
RA Sakaidani Y., Nomura T., Matsuura A., Ito M., Suzuki E., Murakami K.,
RA Nadano D., Matsuda T., Furukawa K., Okajima T.;
RT "O-Linked-N-acetylglucosamine on extracellular protein domains mediates
RT epithelial cell-matrix interactions.";
RL Nat. Commun. 2:583-583(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from
CC UDP-GlcNAc to a serine or threonine residue in extracellular proteins
CC resulting in their modification with a beta-linked N-acetylglucosamine
CC (O-GlcNAc). Specifically glycosylates the Thr residue located between
CC the fifth and sixth conserved cysteines of folded EGF-like domains.
CC Involved in epithelial cell adhesion/interaction with the extracellular
CC matrix by mediating glycosylation of proteins in the secretory pathway,
CC such as Dumpy (Dp). {ECO:0000269|PubMed:22158438}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-
CC acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed:22158438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-
CC (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed:22158438};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:22158438};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:22158438}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Highly
CC expressed in preblastoderm-stage embryos. During the later stages of
CC embryogenesis, expression is ubiquitous with the level progressively
CC decreasing. {ECO:0000269|PubMed:22158438}.
CC -!- DISRUPTION PHENOTYPE: Defects in apical extracellular matrix. Embryos
CC show defects in the formation of the innermost layer of the apical
CC extracellular matrix and its attachment to the epidermis. Most larvae
CC die during second-instar or second/third-instar interface, but some
CC survive until early third-instar. Surviving larvae display cuticle
CC defect and irregular tracheal morphology. Ultrastructural analysis of
CC larval epidermis reveals disruption of the deposition zone of the
CC endocuticle, leading to separation of the epidermis from the chitin
CC layers. {ECO:0000269|PubMed:22158438}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB675601; BAL41443.1; -; mRNA.
DR EMBL; AE014134; AAF51259.1; -; Genomic_DNA.
DR EMBL; AY058292; AAL13521.1; -; mRNA.
DR RefSeq; NP_001259934.1; NM_001273005.1.
DR RefSeq; NP_608678.1; NM_134834.3.
DR AlphaFoldDB; Q9VQB7; -.
DR SMR; Q9VQB7; -.
DR BioGRID; 59652; 3.
DR IntAct; Q9VQB7; 1.
DR STRING; 7227.FBpp0077447; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyGen; Q9VQB7; 4 sites.
DR PaxDb; Q9VQB7; -.
DR DNASU; 33424; -.
DR EnsemblMetazoa; FBtr0077767; FBpp0077447; FBgn0264672.
DR EnsemblMetazoa; FBtr0330685; FBpp0303533; FBgn0264672.
DR GeneID; 33424; -.
DR KEGG; dme:Dmel_CG9867; -.
DR UCSC; CG9867-RA; d. melanogaster.
DR CTD; 285203; -.
DR FlyBase; FBgn0264672; Eogt.
DR VEuPathDB; VectorBase:FBgn0264672; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000156493; -.
DR HOGENOM; CLU_039300_0_0_1; -.
DR InParanoid; Q9VQB7; -.
DR OMA; RFQTPQC; -.
DR OrthoDB; 567582at2759; -.
DR PhylomeDB; Q9VQB7; -.
DR BRENDA; 2.4.1.255; 1994.
DR SignaLink; Q9VQB7; -.
DR BioGRID-ORCS; 33424; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33424; -.
DR PRO; PR:Q9VQB7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0264672; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q9VQB7; baseline and differential.
DR Genevisible; Q9VQB7; DM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IDA:FlyBase.
DR GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0097370; P:protein O-GlcNAcylation via threonine; IMP:FlyBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..520
FT /note="EGF domain-specific O-linked N-acetylglucosamine
FT transferase"
FT /id="PRO_0000418382"
FT MOTIF 292..294
FT /note="Required for optimal activity"
FT /evidence="ECO:0000250"
FT MOTIF 517..520
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 60083 MW; FE00E75C153E733E CRC64;
MPILPILIGI LHLSLAEDAK HLDGFSLPSL PSEHLIRYLN TFPKLKQQLP TNLTGKGTIS
SACWGHERDC TPAGRFQTPQ CPGEHTGWAR SKEAQVRTFY NQADFGYIQE QLSQLTPQCV
PTYLGDSSLE CTHYLRFCRG RNLLFDFRGL EQREERIRYH MDVLGPGQLL GHCKLNRTRL
SGEMEHIGSA LQSWGPELRN FDVLPHPVLE SGLCDVVVNT PTFIMKIDAT YNMYHHFCDF
FNLYASLFVN QSHPAAFNTD VQILIWETYP YDSPFRDTFK AFSQRPVWTL SDVEGKRVCF
KNVVLPLLPR MIFGLFYNTP IIQGCSNSGL FRAFSEFILH RLQIPYKPPQ QKIRITYLSR
RTKYRQVLNE DELLAPLEAN DKYDVQRVSY ERLPFTNQLA ITRNTDILIG MHGAGLTHLL
FLPNWACIFE LYNCEDPNCY KDLARLRGVR YRTWEQRDLV YPQDEGHHPE GGAHAKFTNY
SFDVKEFVHL VDGAAEEILS HKEFPRRASE NPSKTQRNEL
