ID   EOGT_PANTR              Reviewed;         527 AA.
AC   Q5NDL1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
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; AJ868235; CAI30570.1; -; mRNA.
DR   RefSeq; NP_001009171.1; NM_001009171.1.
DR   RefSeq; XP_009444097.1; XM_009445822.2.
DR   RefSeq; XP_009444098.1; XM_009445823.2.
DR   RefSeq; XP_009444099.1; XM_009445824.2.
DR   AlphaFoldDB; Q5NDL1; -.
DR   SMR; Q5NDL1; -.
DR   STRING; 9598.ENSPTRP00000026055; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PaxDb; Q5NDL1; -.
DR   Ensembl; ENSPTRT00000028239; ENSPTRP00000026055; ENSPTRG00000015092.
DR   GeneID; 494220; -.
DR   KEGG; ptr:494220; -.
DR   CTD; 285203; -.
DR   VGNC; VGNC:9671; EOGT.
DR   eggNOG; KOG4698; Eukaryota.
DR   GeneTree; ENSGT00940000156493; -.
DR   HOGENOM; CLU_039300_0_0_1; -.
DR   InParanoid; Q5NDL1; -.
DR   OMA; RFQTPQC; -.
DR   OrthoDB; 567582at2759; -.
DR   TreeFam; TF313716; -.
DR   Proteomes; UP000002277; Chromosome 3.
DR   Bgee; ENSPTRG00000015092; Expressed in colon and 21 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_0000301973"
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;  62044 MW;  B742A488D7ED56B6 CRC64;
     MLMLFVFGVL LHEVSLSGQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF LHNNRHIATV
     CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV DMGWTDTLES AEDIFWKQAD
     FGYARERLEE MHVLCQPKET SDSSLVCSRY LQYCRATNLY LDLRNIKRNH DRFMEDFFQS
     GEIGGHCKLD IRTLMSEGQR KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL
     DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH
     LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL HRLNITQEGP
     KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYRELGFL DQLRITHNTD
     IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG
     HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKHDEL