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   27-MAR-2024, entry version 141.
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}.
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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   GlyCosmos; Q9VQB7; 4 sites, No reported glycans.
DR   GlyGen; Q9VQB7; 4 sites.
DR   PaxDb; 7227-FBpp0077447; -.
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   AGR; FB:FBgn0264672; -.
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; GHCELNR; -.
DR   OrthoDB; 316918at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q9VQB7; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR   GO; GO:0097363; F:protein O-acetylglucosaminyltransferase 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; IPR049625; Glyco_transf_61_cat.
DR   InterPro; IPR007657; Glycosyltransferase_61.
DR   PANTHER; PTHR20961:SF124; EGF DOMAIN-SPECIFIC O-LINKED N-ACETYLGLUCOSAMINE TRANSFERASE; 1.
DR   PANTHER; PTHR20961; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF04577; Glyco_transf_61; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q9VQB7; DM.
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
//