ID   EOGT_CANLF              Reviewed;         527 AA.
AC   Q5NDL9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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; AJ868227; CAI30562.1; -; mRNA.
DR   RefSeq; NP_001009187.1; NM_001009187.1.
DR   RefSeq; XP_005632096.1; XM_005632039.2.
DR   AlphaFoldDB; Q5NDL9; -.
DR   SMR; Q5NDL9; -.
DR   STRING; 9615.ENSCAFP00000009819; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PaxDb; Q5NDL9; -.
DR   PRIDE; Q5NDL9; -.
DR   Ensembl; ENSCAFT00845019440; ENSCAFP00845015200; ENSCAFG00845010941.
DR   GeneID; 494221; -.
DR   KEGG; cfa:494221; -.
DR   CTD; 285203; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010941; -.
DR   VGNC; VGNC:40388; EOGT.
DR   eggNOG; KOG4698; Eukaryota.
DR   GeneTree; ENSGT00940000156493; -.
DR   InParanoid; Q5NDL9; -.
DR   Proteomes; UP000002254; Chromosome 20.
DR   Bgee; ENSCAFG00000006563; Expressed in keratinocyte and 48 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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: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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..527
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301971"
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;  61670 MW;  DA5DE507862BB6AA CRC64;
     MLKLLVLGVL LHDVSLSGQD EAPPKADGIP GEPLFNYASI RLPEEHIPFF LHNNRHIATV
     CKKDSHCPYK KHLENLKYCW GYEKSCKPEF RFGYPVCTYI DMGWTDTLES AQDIFWKQAD
     FGYAGERLEE LHVLCQPEEP HDSSLLCSRY LQYCRAANLY LDLRNIKRNH DRFKEDFFQS
     GEIGGHCTLD TQTLLSEGQR KSPLQSWFAE LQSYTELNFR PIEDAKCDVV IEKPTYFMKL
     DAGVNMYHHF CDFVNLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW KAFTDYDVIH
     LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL HRLNITQEGP
     KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTLEVQIV DYKYKELGFL DQLRITHNTD
     IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG
     HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKRDEL