ID   EOGT_BOVIN              Reviewed;         527 AA.
AC   A0JND3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) 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; BC126625; AAI26626.1; -; mRNA.
DR   RefSeq; NP_001071350.1; NM_001077882.1.
DR   RefSeq; XP_005222695.1; XM_005222638.3.
DR   RefSeq; XP_005222696.1; XM_005222639.3.
DR   RefSeq; XP_005222697.1; XM_005222640.3.
DR   RefSeq; XP_005222698.1; XM_005222641.3.
DR   AlphaFoldDB; A0JND3; -.
DR   SMR; A0JND3; -.
DR   STRING; 9913.ENSBTAP00000030725; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PaxDb; A0JND3; -.
DR   PRIDE; A0JND3; -.
DR   Ensembl; ENSBTAT00000030754; ENSBTAP00000030725; ENSBTAG00000022681.
DR   GeneID; 508782; -.
DR   KEGG; bta:508782; -.
DR   CTD; 285203; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022681; -.
DR   VGNC; VGNC:28515; EOGT.
DR   eggNOG; KOG4698; Eukaryota.
DR   GeneTree; ENSGT00940000156493; -.
DR   HOGENOM; CLU_039300_0_0_1; -.
DR   InParanoid; A0JND3; -.
DR   OMA; RFQTPQC; -.
DR   OrthoDB; 567582at2759; -.
DR   TreeFam; TF313716; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000022681; Expressed in neutrophil and 104 other tissues.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..527
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301969"
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;  61749 MW;  1BDB2867FD8D13A1 CRC64;
     MFMLLVFGAL LPEVPLSGQD KAPPQADGIS ATPLFNYASL RLPEEHIPFF LHNNRHIATV
     CRKDSHCPYK KYLENLKYCW GYEKSCRPEF RFGYPVCTYV DMGWTDTLES AQEIFWKQAD
     FGYAAERLEE LHVLCQPKEK NDSSLVCSRY LQYCRATNIY LDLRNIKRNH DRFKEDFVQS
     GEIGGYCKLD IRSLMSQGQR KSPLQSWFAE LQSYTELNFR PVEDAQCDIV IEKPTYFMKL
     DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YVVMWDTSSY GYGDLFSDTW KAFTDYDVIH
     LKTYDAKRVC FKEAIFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL HRLNITQEGP
     KGGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYKELGFL DQLRITHNTD
     IFIGMHGAGL THLLFLPDWA AVFELYNCGD ERCYLDLARL RGVHYITWRR QNKVFPQDKG
     HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD YVLQHPKWPF KKKHDEL