ID   EOGT_CHICK              Reviewed;         535 AA.
AC   Q5NDL3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-70.
RC   TISSUE=Abdominal adipose tissue;
RX   PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA   Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA   Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT   "A comprehensive collection of chicken cDNAs.";
RL   Curr. Biol. 12:1965-1969(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-535.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC       {ECO:0000305}.
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DR   EMBL; BU415425; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AJ868233; CAI30568.1; -; mRNA.
DR   RefSeq; NP_001026580.1; NM_001031409.1.
DR   AlphaFoldDB; Q5NDL3; -.
DR   SMR; Q5NDL3; -.
DR   STRING; 9031.ENSGALP00000021829; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PaxDb; Q5NDL3; -.
DR   GeneID; 426961; -.
DR   KEGG; gga:426961; -.
DR   CTD; 285203; -.
DR   VEuPathDB; HostDB:geneid_426961; -.
DR   eggNOG; KOG4698; Eukaryota.
DR   InParanoid; Q5NDL3; -.
DR   OrthoDB; 567582at2759; -.
DR   PhylomeDB; Q5NDL3; -.
DR   PRO; PR:Q5NDL3; -.
DR   Proteomes; UP000000539; Unplaced.
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.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..535
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301975"
FT   MOTIF           303..305
FT                   /note="Required for optimal activity"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   535 AA;  62868 MW;  2F0EC0F588B4BB3B CRC64;
     MFILLMFVLL LQEILANSRD ENLTELNSVL EEPTYSYRAI NLPAEHIPYF LHNNRHIAGI
     CKQDSRCPYK VGFYFVLHKY LKKLKSCWGY EKSCKSDYRF SYPVCDYVES GWANDIETAQ
     QIFWKQADFG YIRERLNEMK THCKPTVTGD SSLTCSQFLQ HCRATNLYID LRTAKRNHER
     FKEDFFQKGE IGGHCTLDVK AFLAEGQRKS PLQSWFAELQ TFTSLNFRPL DDGKCDIVIE
     KPTYFMKLDA GVNMYHHFCD FVNLYITQHI NNSFSTDVNI VMWDTSSYGY GDLFSETWKA
     FTDYDIIYLK TFDSKRVCFK EAVFSLLPRM RYGLFYNTPL ISGCHGTGLF RAFSQHVLHR
     LNITQEGPKD GKIRVTILAR STDYRKILNQ NELVNALKTV STLEVKVVDY KYKELEFSEQ
     LRITHNSDIF IGMHGAGLTH LLFLPDWAVV FELYNCEDER CYLDLARLRG IHYITWRKRN
     KVFPQDQGHH PTLGEHPKFT NYSFDVEEFM YLVLLAANHV SQHSKWPFRV KHDEF