EOGT_MOUSE
ID EOGT_MOUSE Reviewed; 527 AA.
AC Q8BYW9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=EGF domain-specific O-linked N-acetylglucosamine transferase;
DE EC=2.4.1.255 {ECO:0000269|PubMed:22310717};
DE AltName: Full=Extracellular O-linked N-acetylglucosamine transferase;
DE Flags: Precursor;
GN Name=Eogt; Synonyms=Aer61, Eogt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=22310717; DOI=10.1016/j.bbrc.2012.01.098;
RA Sakaidani Y., Ichiyanagi N., Saito C., Nomura T., Ito M., Nishio Y.,
RA Nadano D., Matsuda T., Furukawa K., Okajima T.;
RT "O-linked-N-acetylglucosamine modification of mammalian Notch receptors by
RT an atypical O-GlcNAc transferase Eogt1.";
RL Biochem. Biophys. Res. Commun. 419:14-19(2012).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=23522784; DOI=10.1016/j.ajhg.2013.02.012;
RA Shaheen R., Aglan M., Keppler-Noreuil K., Faqeih E., Ansari S., Horton K.,
RA Ashour A., Zaki M.S., Al-Zahrani F., Cueto-Gonzalez A.M., Abdel-Salam G.,
RA Temtamy S., Alkuraya F.S.;
RT "Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive
RT Adams-Oliver syndrome.";
RL Am. J. Hum. Genet. 92:598-604(2013).
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:0000269|PubMed:22310717}.
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:0000269|PubMed:22310717};
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:0000269|PubMed:22310717};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC kidney, lung, skeletal muscles and thymus. Highest expression is
CC observed in lung and the lowest in skeletal muscles.
CC {ECO:0000269|PubMed:22310717}.
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic day (E) 10.5 in the growing
CC edge of the limb buds. At 11.5 dpc, enriched in the apical ectodermal
CC ridge of the limbs. By 12.5 dpc, expression assumes a digit-
CC condensation pattern in the 4 limbs. {ECO:0000269|PubMed:23522784}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
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DR EMBL; AK037507; BAC29821.1; -; mRNA.
DR EMBL; BC048939; AAH48939.1; -; mRNA.
DR CCDS; CCDS20383.1; -.
DR RefSeq; NP_780522.1; NM_175313.4.
DR RefSeq; XP_006505321.1; XM_006505258.3.
DR AlphaFoldDB; Q8BYW9; -.
DR SMR; Q8BYW9; -.
DR BioGRID; 221637; 2.
DR IntAct; Q8BYW9; 1.
DR MINT; Q8BYW9; -.
DR STRING; 10090.ENSMUSP00000061610; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyConnect; 2279; 2 N-Linked glycans (1 site).
DR GlyGen; Q8BYW9; 1 site, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8BYW9; -.
DR EPD; Q8BYW9; -.
DR MaxQB; Q8BYW9; -.
DR PaxDb; Q8BYW9; -.
DR PeptideAtlas; Q8BYW9; -.
DR PRIDE; Q8BYW9; -.
DR ProteomicsDB; 277879; -.
DR Antibodypedia; 15479; 49 antibodies from 17 providers.
DR Ensembl; ENSMUST00000054344; ENSMUSP00000061610; ENSMUSG00000035245.
DR GeneID; 101351; -.
DR KEGG; mmu:101351; -.
DR UCSC; uc009dai.1; mouse.
DR CTD; 285203; -.
DR MGI; MGI:2141669; Eogt.
DR VEuPathDB; HostDB:ENSMUSG00000035245; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000156493; -.
DR HOGENOM; CLU_039300_0_0_1; -.
DR InParanoid; Q8BYW9; -.
DR OMA; RFQTPQC; -.
DR OrthoDB; 567582at2759; -.
DR PhylomeDB; Q8BYW9; -.
DR TreeFam; TF313716; -.
DR BRENDA; 2.4.1.255; 3474.
DR BioGRID-ORCS; 101351; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Eogt; mouse.
DR PRO; PR:Q8BYW9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BYW9; protein.
DR Bgee; ENSMUSG00000035245; Expressed in embryonic post-anal tail and 271 other tissues.
DR ExpressionAtlas; Q8BYW9; baseline and differential.
DR Genevisible; Q8BYW9; MM.
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; IDA: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; IDA: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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..527
FT /note="EGF domain-specific O-linked N-acetylglucosamine
FT transferase"
FT /id="PRO_0000301972"
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; 61446 MW; 793D0E8F481AD5E4 CRC64;
MLMLLVFGVL LHEVPLSGQD KAHSEADDAP GKALYDYSSL RLPAEHIPFF LHNNRHVASV
CREDSHCPYK KHLENLNYCW GYEKSCAPEF RFGSPVCSYV DLGWTDTLES AQDMFWRQAD
FGYARERLGE IRTICQPERA SDSSLVCSRY LQYCRATGLY LDLRNIKRNH DRFKEDFLQG
GEIGGYCKLD SHALVSEGQR KSPLQSWFAE LQGYTQLNFR PIEDAKCDIV VEKPTYFMKL
DAGINMYHHF CDFLNLYLTQ HVNNSFSTDV YIVMWDTSTY GYGDLFSDTW KAFTDYDVIH
LKTYDSKKVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL HRLNITQEGP
KDGKVRVTIL ARSTEYRKIL NQDELVNALK TVSTFEVRVV DYKYRELGFL DQLRITHNTD
IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGIHYITWRK PSKVFPQDKG
HHPTLGEHPK FTNYSFDVEE FMYLVLQAAE HVLQHPQWPF KKKHDEL
