ID   EOGT_RAT                Reviewed;         527 AA.
AC   Q5NDL0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=EGF domain-specific O-linked N-acetylglucosamine transferase;
DE            EC=2.4.1.255 {ECO:0000250|UniProtKB:Q8BYW9};
DE   AltName: Full=Extracellular O-linked N-acetylglucosamine transferase;
DE   Flags: Precursor;
GN   Name=Eogt; Synonyms=Aer61;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V.,
RA   Mollicone R., Oriol R.;
RT   "Phylogeny of xylosyltransferases.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000250|UniProtKB:Q8BYW9}.
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:0000250|UniProtKB:Q8BYW9};
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:0000250|UniProtKB:Q8BYW9};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ868236; CAI30571.1; -; mRNA.
DR   RefSeq; NP_001009502.1; NM_001009502.1.
DR   RefSeq; XP_008761369.1; XM_008763147.2.
DR   RefSeq; XP_017448256.1; XM_017592767.1.
DR   AlphaFoldDB; Q5NDL0; -.
DR   SMR; Q5NDL0; -.
DR   STRING; 10116.ENSRNOP00000034561; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   GlyGen; Q5NDL0; 1 site.
DR   PhosphoSitePlus; Q5NDL0; -.
DR   jPOST; Q5NDL0; -.
DR   PaxDb; Q5NDL0; -.
DR   PRIDE; Q5NDL0; -.
DR   GeneID; 494219; -.
DR   KEGG; rno:494219; -.
DR   UCSC; RGD:1359357; rat.
DR   CTD; 285203; -.
DR   RGD; 1359357; Eogt.
DR   eggNOG; KOG4698; Eukaryota.
DR   HOGENOM; CLU_039300_0_0_1; -.
DR   InParanoid; Q5NDL0; -.
DR   PhylomeDB; Q5NDL0; -.
DR   TreeFam; TF313716; -.
DR   PRO; PR:Q5NDL0; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000024533; Expressed in lung and 19 other tissues.
DR   ExpressionAtlas; Q5NDL0; baseline and differential.
DR   Genevisible; Q5NDL0; RN.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097370; P:protein O-GlcNAcylation via threonine; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISS: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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..527
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301974"
FT   MOTIF           295..297
FT                   /note="Required for optimal activity"
FT                   /evidence="ECO:0000250"
FT   MOTIF           524..527
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   527 AA;  61524 MW;  CB8678AFF3B00870 CRC64;
     MLMLLVFGVL LHEVPLSGQD EAHPEADRVP GEALYDYSSL RLPEEHIPFF LHSNRHVASV
     CREDSHCPYK KHLESLNSCW GYEKSCTPES RFGSPICSYV DLGWTDTLES AQDMFWKQAD
     FGYARERLEE IRMFCRPESA SDSSLLCSRY LQYCRATGLY LDLRNIKRNH DRFKEDFLQG
     GDIGGYCKLD RHALVSEGQR KSPLQSWFAE LQGYTQLNFR PIEDAKCDIV VEKPTYFMKL
     DAGINMYHHF CDFLNLYLTQ HINNSFSTDV YIVMWDTSSY GYGDLFSDTW KAFTDYDVIH
     LKTYDSKKVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL HRLNISQEGP
     KDGKLRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVRVV DYKYRELGFL DQLRITHNTD
     IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGIYYITWQK PSKVFPQDKG
     HHPTLGEHPK FTNYSFDVEE FMYLVLQAAE HVLQHPQWPL KKNHDEL