OGT1_CAEEL
ID OGT1_CAEEL Reviewed; 1151 AA.
AC O18158; Q21232;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase;
DE EC=2.4.1.255 {ECO:0000250|UniProtKB:O15294};
DE AltName: Full=O-GlcNAc;
DE AltName: Full=OGT;
GN Name=ogt-1; ORFNames=K04G7.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 321-340 AND 1060-1076, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9083068; DOI=10.1074/jbc.272.14.9316;
RA Lubas W.A., Frank D.W., Krause M., Hanover J.A.;
RT "O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein
RT containing tetratricopeptide repeats.";
RL J. Biol. Chem. 272:9316-9324(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=24706800; DOI=10.1073/pnas.1322396111;
RA Radermacher P.T., Myachina F., Bosshardt F., Pandey R., Mariappa D.,
RA Mueller H.A., Lehner C.F.;
RT "O-GlcNAc reports ambient temperature and confers heat resistance on
RT ectotherm development.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5592-5597(2014).
CC -!- FUNCTION: Addition of nucleotide-activated sugars directly onto the
CC polypeptide through O-glycosidic linkage with the hydroxyl of serine or
CC threonine. {ECO:0000250|UniProtKB:O15294}.
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:O15294};
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:O15294};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:9083068}.
CC -!- DOMAIN: The TPR repeat domain mediates recognition of protein
CC substrates. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lack O-GlcNAc post-translational
CC modification and brood size decreases with increasing ambient
CC temperature. {ECO:0000269|PubMed:24706800}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; U77412; AAB63465.1; -; mRNA.
DR EMBL; FO080149; CCD61614.1; -; Genomic_DNA.
DR PIR; E88499; E88499.
DR RefSeq; NP_001040860.1; NM_001047395.3.
DR AlphaFoldDB; O18158; -.
DR SMR; O18158; -.
DR BioGRID; 41212; 8.
DR DIP; DIP-26521N; -.
DR IntAct; O18158; 1.
DR STRING; 6239.K04G7.3a; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR iPTMnet; O18158; -.
DR EPD; O18158; -.
DR PaxDb; O18158; -.
DR PeptideAtlas; O18158; -.
DR EnsemblMetazoa; K04G7.3a.1; K04G7.3a.1; WBGene00003858.
DR GeneID; 176000; -.
DR KEGG; cel:CELE_K04G7.3; -.
DR UCSC; K04G7.3a; c. elegans.
DR CTD; 176000; -.
DR WormBase; K04G7.3a; CE25042; WBGene00003858; ogt-1.
DR eggNOG; KOG4626; Eukaryota.
DR InParanoid; O18158; -.
DR OMA; HAYSEKL; -.
DR OrthoDB; 142546at2759; -.
DR PhylomeDB; O18158; -.
DR SignaLink; O18158; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:O18158; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003858; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O18158; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IMP:WormBase.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IMP:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:WormBase.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:WormBase.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:WormBase.
DR GO; GO:0009100; P:glycoprotein metabolic process; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IMP:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:WormBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR037919; OGT.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44366; PTHR44366; 1.
DR Pfam; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 12.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycosyltransferase; Nucleus;
KW Reference proteome; Repeat; TPR repeat; Transferase.
FT CHAIN 1..1151
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000191775"
FT REPEAT 125..158
FT /note="TPR 1"
FT REPEAT 193..226
FT /note="TPR 2"
FT REPEAT 227..260
FT /note="TPR 3"
FT REPEAT 261..294
FT /note="TPR 4"
FT REPEAT 295..328
FT /note="TPR 5"
FT REPEAT 329..362
FT /note="TPR 6"
FT REPEAT 363..396
FT /note="TPR 7"
FT REPEAT 397..430
FT /note="TPR 8"
FT REPEAT 431..464
FT /note="TPR 9"
FT REPEAT 465..498
FT /note="TPR 10"
FT REPEAT 499..532
FT /note="TPR 11"
FT REPEAT 533..566
FT /note="TPR 12"
FT REPEAT 567..577
FT /note="TPR 13; truncated"
FT MOTIF 591..607
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 612
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 954
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 957
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 1010..1013
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 1016..1019
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 1034..1036
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 1040
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT CONFLICT 129
FT /note="T -> A (in Ref. 1; AAB63465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1151 AA; 128012 MW; D1CE2A19401CC44F CRC64;
MEKPNYFQSY NKVIGATGEQ LAPGAVPPHP VLAPSIAPGG VAGVSAANMA NIMQTPGFAN
LVQQAIRTQL ENQAAQQLAV NQQFQLNGAT AVQQQLLLTP QQSLAQPIAL APQPTVVLNG
VSETLKKVTE LAHRQFQSGN YVEAEKYCNL VFQSDPNNLP TLLLLSAINF QTKNLEKSMQ
YSMLAIKVNN QCAEAYSNLG NYYKEKGQLQ DALENYKLAV KLKPEFIDAY INLAAALVSG
GDLEQAVTAY FNALQINPDL YCVRSDLGNL LKAMGRLEEA KVCYLKAIET QPQFAVAWSN
LGCVFNSQGE IWLAIHHFEK AVTLDPNFLD AYINLGNVLK EARIFDRAVS AYLRALNLSG
NHAVVHGNLA CVYYEQGLID LAIDTYKKAI DLQPHFPDAY CNLANALKEK GSVVEAEQMY
MKALELCPTH ADSQNNLANI KREQGKIEDA TRLYLKALEI YPEFAAAHSN LASILQQQGK
LNDAILHYKE AIRIAPTFAD AYSNMGNTLK EMGDSSAAIA CYNRAIQINP AFADAHSNLA
SIHKDAGNMA EAIQSYSTAL KLKPDFPDAY CNLAHCHQII CDWNDYDKRV RKLVQIVEDQ
LCKKRLPSVH PHHSMLYPLS HAARIAIAAK HASLCFDKVH VQMLGKTPLI HADRFSVQNG
QRLRIGYVSS DFGNHPTSHL MQSIPGMHDR SRVEVFCYAL SVNDGTNFRS KLMNESEHFV
DLSQIPCNGK AAEKIAQDGI HILINMNGYT KGARNEIFAL RPAPIQVMWL GYPSTSGATF
MDYIITDAVT SPLRLANAFT EKLAYMPHTF FIGDHAQMLR HLTDKVVVKD KETTERDSCL
IMNTANMDPI LAKSEIKEQV LDTEVVSGPN KELVRAEMVL PVLEVPTEPI KQMIMTGQMT
MNVMEDMNVQ NGLGQSQMHH KAATGEEIPN SVLLTSRAQY QLPDDAIVFC NFNQLYKIDP
STLDMWIKIL ENVPKSILWL LRFPYQGEEH IRKYCVERGL DPSRIVFSNV AAKEEHVRRG
QLADVCLDTP LCNGHTTGMD ILWTGTPMVT MPLESLASRV ATSQLYALGV PELVAKTRQE
YVSIAVRLGT DADHLANMRA KVWMARTSST LFDVKQYCHD MEDLLGQMWK RYESGMPIDH
ITNNTETPHG L
