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Q8BYW9 (EOGT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EGF domain-specific O-linked N-acetylglucosamine transferase
EC=2.4.1.255
Alternative name(s):
Extracellular O-linked N-acetylglucosamine transferase
Gene names
Name:Eogt
Synonyms:Aer61, Eogt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. Ref.3

Catalytic activity

UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine. Ref.3

UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Tissue specificity

Widely expressed. Expressed in brain, heart, kidney, lung, skeletal muscles and thymus. Highest expression is observed in lung and the lowest in skeletal muscles. Ref.3

Sequence similarities

Belongs to the glycosyltransferase 61 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein O-linked glycosylation

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein N-acetylglucosaminyltransferase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 527508EGF domain-specific O-linked N-acetylglucosamine transferase
PRO_0000301972

Regions

Motif524 – 5274Prevents secretion from ER Potential

Amino acid modifications

Glycosylation3541N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8BYW9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 793D0E8F481AD5E4

FASTA52761,446
        10         20         30         40         50         60 
MLMLLVFGVL LHEVPLSGQD KAHSEADDAP GKALYDYSSL RLPAEHIPFF LHNNRHVASV 

        70         80         90        100        110        120 
CREDSHCPYK KHLENLNYCW GYEKSCAPEF RFGSPVCSYV DLGWTDTLES AQDMFWRQAD 

       130        140        150        160        170        180 
FGYARERLGE IRTICQPERA SDSSLVCSRY LQYCRATGLY LDLRNIKRNH DRFKEDFLQG 

       190        200        210        220        230        240 
GEIGGYCKLD SHALVSEGQR KSPLQSWFAE LQGYTQLNFR PIEDAKCDIV VEKPTYFMKL 

       250        260        270        280        290        300 
DAGINMYHHF CDFLNLYLTQ HVNNSFSTDV YIVMWDTSTY GYGDLFSDTW KAFTDYDVIH 

       310        320        330        340        350        360 
LKTYDSKKVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL HRLNITQEGP 

       370        380        390        400        410        420 
KDGKVRVTIL ARSTEYRKIL NQDELVNALK TVSTFEVRVV DYKYRELGFL DQLRITHNTD 

       430        440        450        460        470        480 
IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGIHYITWRK PSKVFPQDKG 

       490        500        510        520 
HHPTLGEHPK FTNYSFDVEE FMYLVLQAAE HVLQHPQWPF KKKHDEL

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.
[3]"O-linked-N-acetylglucosamine modification of mammalian Notch receptors by an atypical O-GlcNAc transferase Eogt1."
Sakaidani Y., Ichiyanagi N., Saito C., Nomura T., Ito M., Nishio Y., Nadano D., Matsuda T., Furukawa K., Okajima T.
Biochem. Biophys. Res. Commun. 419:14-19(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK037507 mRNA. Translation: BAC29821.1.
BC048939 mRNA. Translation: AAH48939.1.
IPIIPI00227372.
RefSeqNP_780522.1. NM_175313.4.
UniGeneMm.486365.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000061610.

Protein family/group databases

CAZyGT61. Glycosyltransferase Family 61.

PTM databases

PhosphoSiteQ8BYW9.

Proteomic databases

PaxDbQ8BYW9.
PRIDEQ8BYW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054344; ENSMUSP00000061610; ENSMUSG00000035245.
GeneID101351.
KEGGmmu:101351.
UCSCuc009dai.1. mouse.

Organism-specific databases

CTD285203.
MGIMGI:2141669. Eogt.

Phylogenomic databases

eggNOGNOG320328.
GeneTreeENSGT00390000008553.
HOGENOMHOG000033829.
HOVERGENHBG056678.
InParanoidQ8BYW9.
OMADSKRVCF.
OrthoDBEOG4XGZZQ.

Gene expression databases

ArrayExpressQ8BYW9.
BgeeQ8BYW9.
CleanExMM_A130022J15RIK.
GenevestigatorQ8BYW9.

Family and domain databases

InterProIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio354880.
SOURCESearch...

Entry information

Entry nameEOGT_MOUSE
AccessionPrimary (citable) accession number: Q8BYW9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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