OGT1_PIG
ID OGT1_PIG Reviewed; 1046 AA.
AC Q27HV0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
DE EC=2.4.1.255 {ECO:0000250|UniProtKB:O15294};
DE AltName: Full=O-GlcNAc transferase subunit p110;
DE AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
DE Short=OGT;
GN Name=OGT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.G., Vallet J.L., Ford J.J., Rohrer G.A., Nonneman D.;
RT "Molecular cloning of swine OGT cDNA and mapping on chromosome X.";
RL Submitted (FEB-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 cytoplasmic and nuclear
CC proteins resulting in their modification with a beta-linked N-
CC acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number
CC of proteins including histone H2B, AKT1, ATG4B, EZH2, PFKL, KMT2E/MLL5,
CC MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-
CC talk between glycosylation and phosphorylation or by affecting
CC proteolytic processing. Probably by glycosylating KMT2E/MLL5,
CC stabilizes KMT2E/MLL5 by preventing its ubiquitination (By similarity).
CC Involved in insulin resistance in muscle and adipocyte cells via
CC glycosylating insulin signaling components and inhibiting the 'Thr-308'
CC phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating
CC insulin signaling (By similarity). Involved in glycolysis regulation by
CC mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its
CC activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required
CC for the regulation of the transcriptional activity of RRM1. Plays a key
CC role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112'
CC of histone H2B: recruited to CpG-rich transcription start sites of
CC active genes via its interaction with TET proteins (TET1, TET2 or
CC TET3). As part of the NSL complex indirectly involved in acetylation of
CC nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of
CC 'Ser-75' of EZH2 increases its stability, and facilitating the
CC formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian
CC oscillation of the clock genes and glucose homeostasis in the liver.
CC Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-
CC glycosylation, which prevents their ubiquitination and subsequent
CC degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of
CC genes in the negative loop of the circadian clock such as PER1/2 and
CC CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing
CC and transcriptional activity (By similarity). Regulates mitochondrial
CC motility in neurons by mediating glycosylation of TRAK1 (By
CC similarity). Glycosylates HOXA1 (By similarity). O-glycosylates FNIP1
CC (By similarity). Promotes autophagy by mediating O-glycosylation of
CC ATG4B (By similarity). {ECO:0000250|UniProtKB:O15294,
CC ECO:0000250|UniProtKB:P56558, ECO:0000250|UniProtKB:Q8CGY8}.
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 {ECO:0000250|UniProtKB:O15294}.
CC -!- SUBUNIT: Homotrimer, oligomerizes via TPR repeats 6 and 7.
CC Trimerization is not necessary for activity in vitro, however it
CC increases affinity for UDP-GlcNAc (By similarity). Component of a
CC THAP1/THAP3-HCFC1-OGT complex. Component of the NSL complex at least
CC composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT,
CC WDR5 and HCFC1. Interacts directly with HCFC1; the interaction O-
CC glycosylates HCFC1, regulates its proteolytic processing and
CC transcriptional activity and, in turn, stabilizes OGT in the nucleus.
CC Interacts (via TPRs 1-6) with SIN3A; the interaction mediates
CC transcriptional repression in parallel with histone deacetylase.
CC Interacts (via TPR 5-6) with TET1, TET2 and TET3 (By similarity).
CC Interacts (via TPR repeats 6 and 7) with ATXN10 (By similarity).
CC Interacts with histone H2B (By similarity). Interacts with ARNTL/BMAL1.
CC Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30,
CC RBBP4, OGT and TET1. Interacts with SINHCAF (By similarity). Component
CC of a complex composed of KMT2E/MLL5, OGT and USP7; the complex
CC stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and
CC proteosomal-mediated degradation. Interacts (via TRP repeats) with
CC KMT2E/MLL5 (via N-terminus). Interacts with USP7. Interacts with TRAK1;
CC this interaction is not required for glycosylation of TRAK1 by this
CC protein. Found in a complex with KIF5B, RHOT1, RHOT2 and TRAK1 (By
CC similarity). Interacts (via TPR repeats domain) with HOXA1; the
CC interaction takes place mainly in the nucleus (By similarity).
CC Interacts with NSD2 (By similarity). {ECO:0000250|UniProtKB:O15294,
CC ECO:0000250|UniProtKB:P56558, ECO:0000250|UniProtKB:Q8CGY8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15294}. Nucleus
CC {ECO:0000250|UniProtKB:O15294}. Cell membrane
CC {ECO:0000250|UniProtKB:O15294}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P56558}. Cell projection
CC {ECO:0000250|UniProtKB:P56558}. Note=Mostly in the nucleus. Retained in
CC the nucleus via interaction with HCFC1. After insulin induction,
CC translocated from the nucleus to the cell membrane via
CC phosphatidylinositide binding. Colocalizes with AKT1 at the plasma
CC membrane (By similarity). TRAK1 recruits this protein to mitochondria.
CC In the absence of TRAK1, localizes in cytosol and nucleus (By
CC similarity). {ECO:0000250|UniProtKB:O15294,
CC ECO:0000250|UniProtKB:P56558}.
CC -!- DOMAIN: The TPR repeat domain is required for substrate binding and
CC oligomerization. {ECO:0000250|UniProtKB:O15294}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
CC regulates its activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; DQ400859; ABD61726.1; -; mRNA.
DR RefSeq; NP_001034837.1; NM_001039748.2.
DR AlphaFoldDB; Q27HV0; -.
DR SMR; Q27HV0; -.
DR STRING; 9823.ENSSSCP00000013198; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR PaxDb; Q27HV0; -.
DR PeptideAtlas; Q27HV0; -.
DR PRIDE; Q27HV0; -.
DR GeneID; 664652; -.
DR KEGG; ssc:664652; -.
DR CTD; 8473; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG4626; Eukaryota.
DR InParanoid; Q27HV0; -.
DR UniPathway; UPA00378; -.
DR ChiTaRS; EOGT; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS: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; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 12.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Biological rhythms; Cell membrane; Cell projection;
KW Chromatin regulator; Cytoplasm; Glycoprotein; Glycosyltransferase;
KW Lipid-binding; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT CHAIN 2..1046
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase 110 kDa subunit"
FT /id="PRO_0000289993"
FT REPEAT 21..54
FT /note="TPR 1"
FT REPEAT 89..122
FT /note="TPR 2"
FT REPEAT 123..156
FT /note="TPR 3"
FT REPEAT 157..190
FT /note="TPR 4"
FT REPEAT 191..224
FT /note="TPR 5"
FT REPEAT 225..258
FT /note="TPR 6"
FT REPEAT 259..292
FT /note="TPR 7"
FT REPEAT 293..326
FT /note="TPR 8"
FT REPEAT 327..360
FT /note="TPR 9"
FT REPEAT 361..394
FT /note="TPR 10"
FT REPEAT 395..428
FT /note="TPR 11"
FT REPEAT 429..462
FT /note="TPR 12"
FT REPEAT 463..473
FT /note="TPR 13; truncated"
FT REGION 991..1010
FT /note="Required for phosphatidylinositol 3,4,5-triphosphate
FT binding"
FT MOTIF 487..503
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 508
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 849
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 852
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 906..908
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 911..914
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 930..932
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 935
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT MOD_RES 3
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CGY8"
FT MOD_RES 4
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CGY8"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT MOD_RES 989
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P56558"
FT CARBOHYD 3
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1046 AA; 116923 MW; A9296D28DDF12A8C CRC64;
MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL
LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP
DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY
LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI
FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF
AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR
AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT
DYDERMKKLV SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK
PPYEHPKDLK LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA
MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV
IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADSSNT ALNMPVIPMN
TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED
AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL
TCLGCLELIA KNRQEFEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY
LQMWEHYAAG NKPDHMIKPV EVTESA
