ID   EOGT_XENLA              Reviewed;         525 AA.
AC   Q6GQ23;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 66.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC072925; AAH72925.1; -; mRNA.
DR   RefSeq; NP_001085557.1; NM_001092088.1.
DR   AlphaFoldDB; Q6GQ23; -.
DR   SMR; Q6GQ23; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   GlyCosmos; Q6GQ23; 1 site, No reported glycans.
DR   GeneID; 443983; -.
DR   KEGG; xla:443983; -.
DR   AGR; Xenbase:XB-GENE-994622; -.
DR   CTD; 443983; -.
DR   Xenbase; XB-GENE-994622; eogt.L.
DR   OrthoDB; 316918at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 443983; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR   InterPro; IPR049625; Glyco_transf_61_cat.
DR   InterPro; IPR007657; Glycosyltransferase_61.
DR   PANTHER; PTHR20961:SF124; EGF DOMAIN-SPECIFIC O-LINKED N-ACETYLGLUCOSAMINE TRANSFERASE; 1.
DR   PANTHER; PTHR20961; GLYCOSYLTRANSFERASE; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..525
FT                   /note="EGF domain-specific O-linked N-acetylglucosamine
FT                   transferase"
FT                   /id="PRO_0000301976"
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;  61182 MW;  71165EA2755AA496 CRC64;
     MVPLRLVLLL HIIHFSCENE VGSAANNGSA QLYNYRKIHL PDDHIPYYLH SNRHVAALCL
     QDLHCPYKQH LQNLNSCWGY EKTCAEGHRF GYPVCDQVDF GWAKTIEESQ QVFWRQADFG
     YVKERLAETQ ILCRPQEQGD SMLACSQNLQ HCRATNLYLD LRHPRRGQEN FKEDFLQEGE
     IGGHCDLDKQ ALLSQGAWKS PLQSWFAELQ SYSSFKFKPI EDAHCDIIIE KPTYFMKLDA
     GVNMYHHFCD FVNLYITQHV NNSFSTDINI VMWTTSVYGY GDLFSDTWKA FTDYEITHLK
     AYDNKRVCFK DAVFALLPRM RYGLFYNTPL ISHCHGSGLF RAFSQHVLHR LNITQHPATE
     AKIRVTILVR STEFRKILNL DELVQALEAV PTFQVKVVDY KYRVLGFLEQ LSITHNSDIF
     IGMHGAGLTH LLFLPDWAVV FELYNCEDAR CYLDLARLRG IQYMTWEKGD KVFPQDKGHH
     PNLGEHPKFT NYAFDVEEFL RLVQQGATYV SRHSKWPLRR TRDEL
//