ID A0A3Q0D4M8_MESAU Unreviewed; 1046 AA.
AC A0A3Q0D4M8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit {ECO:0000256|ARBA:ARBA00015782};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
DE AltName: Full=O-GlcNAc transferase subunit p110 {ECO:0000256|ARBA:ARBA00029769};
DE AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit {ECO:0000256|ARBA:ARBA00031470};
GN Name=Ogt {ECO:0000313|RefSeq:XP_021089270.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021089270.1};
RN [1] {ECO:0000313|RefSeq:XP_021089270.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26319212;
RA Ying B., Toth K., Spencer J.F., Aurora R., Wold W.S.;
RT "Transcriptome sequencing and development of an expression microarray
RT platform for liver infection in adenovirus type 5-infected Syrian golden
RT hamsters.";
RL Virology 485:305-312(2015).
RN [2] {ECO:0000313|RefSeq:XP_021089270.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000670};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000256|ARBA:ARBA00005386}.
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DR RefSeq; XP_021089270.1; XM_021233611.1.
DR AlphaFoldDB; A0A3Q0D4M8; -.
DR OrthoDB; 34780at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.720.150; -; 1.
DR Gene3D; 3.40.50.11380; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR Pfam; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 6.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_021089270.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_021089270.1}.
FT REPEAT 89..122
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 123..156
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 157..190
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 191..224
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 225..258
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 259..292
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 293..326
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 327..360
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 361..394
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 395..428
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 429..462
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 476..1016
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1046 AA; 116884 MW; D726C4FA1D9AD32E 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 SIVAEQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK
PPYEHPKDLK VSDGRLRVGY 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 KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY
LQMWEHYAAG NKPDHMIKPA EVTESA
//