ID   EOGT_XENTR              Reviewed;         525 AA.
AC   Q08CY9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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; BC124028; AAI24029.1; -; mRNA.
DR   RefSeq; NP_001072691.1; NM_001079223.1.
DR   AlphaFoldDB; Q08CY9; -.
DR   SMR; Q08CY9; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PRIDE; Q08CY9; -.
DR   DNASU; 780148; -.
DR   Ensembl; ENSXETT00000035246; ENSXETP00000035246; ENSXETG00000016165.
DR   GeneID; 780148; -.
DR   KEGG; xtr:780148; -.
DR   CTD; 285203; -.
DR   Xenbase; XB-GENE-994619; eogt.
DR   InParanoid; Q08CY9; -.
DR   OrthoDB; 567582at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000016165; Expressed in 2-cell stage embryo and 12 other tissues.
DR   ExpressionAtlas; Q08CY9; baseline.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..525
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301977"
FT   MOTIF           293..295
FT                   /note="Required for optimal activity"
FT                   /evidence="ECO:0000250"
FT   MOTIF           522..525
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   525 AA;  61427 MW;  DC8F270FDCAE2F88 CRC64;
     MVPLWLLLLF HVIHFSHGNE IDSAASNGSA LSYHYGKLYL PDDHIPYYLH SNRHIAALCR
     RDPHCPFKQH LQNLNSCWGY EKSCTKGHGY SYPVCDQVDF GWAKTIEESQ EVFWKQADFG
     YVKERLAETQ ILCRPQEQGD SMLACSRNLQ HCRATNLYLD LRNPRRGQEN FKEDFLQEGE
     IGGRCNLDKQ ALLSQGAWKS PLQSWFAELQ SYSSLTFKPV EDAHCDIIID KPTYFMKLDA
     GVNMYHHFCD FVNLYITQHV NNSFSTDINI VMWTTSVYGY GDLFSDTWKA FTDYDITHLK
     AYDNKRVCFK DAVFALLPRM RYGLFYNTPL ISNCHGSGLF RAFSQHVLHR LNITQQLPKE
     AKIRITILVR STEFRKILNL DELVHALEAE PTFQVKVVDY KYRVLGFLEQ LEITHNSDIF
     IGMHGAGLTH LLFLPDWAVV FELYNCEDER CYLDLARLRG IRYMTWENRD KVFPQDKGHH
     PNLGEHPKFT NYAFDVEEFL RLVRQAAKNV SRHSKWPFRR TRDEL