Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6GQ23 (EOGT_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

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.

Sequence similarities

Belongs to the glycosyltransferase 61 family.

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein N-acetylglucosaminyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 525501EGF domain-specific O-linked N-acetylglucosamine transferase
PRO_0000301976

Regions

Motif522 – 5254Prevents secretion from ER Potential

Amino acid modifications

Glycosylation3521N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6GQ23 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 71165EA2755AA496

FASTA52561,182
        10         20         30         40         50         60 
MVPLRLVLLL HIIHFSCENE VGSAANNGSA QLYNYRKIHL PDDHIPYYLH SNRHVAALCL 

        70         80         90        100        110        120 
QDLHCPYKQH LQNLNSCWGY EKTCAEGHRF GYPVCDQVDF GWAKTIEESQ QVFWRQADFG 

       130        140        150        160        170        180 
YVKERLAETQ ILCRPQEQGD SMLACSQNLQ HCRATNLYLD LRHPRRGQEN FKEDFLQEGE 

       190        200        210        220        230        240 
IGGHCDLDKQ ALLSQGAWKS PLQSWFAELQ SYSSFKFKPI EDAHCDIIIE KPTYFMKLDA 

       250        260        270        280        290        300 
GVNMYHHFCD FVNLYITQHV NNSFSTDINI VMWTTSVYGY GDLFSDTWKA FTDYEITHLK 

       310        320        330        340        350        360 
AYDNKRVCFK DAVFALLPRM RYGLFYNTPL ISHCHGSGLF RAFSQHVLHR LNITQHPATE 

       370        380        390        400        410        420 
AKIRVTILVR STEFRKILNL DELVQALEAV PTFQVKVVDY KYRVLGFLEQ LSITHNSDIF 

       430        440        450        460        470        480 
IGMHGAGLTH LLFLPDWAVV FELYNCEDAR CYLDLARLRG IQYMTWEKGD KVFPQDKGHH 

       490        500        510        520 
PNLGEHPKFT NYAFDVEEFL RLVQQGATYV SRHSKWPLRR TRDEL 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Gastrula.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC072925 mRNA. Translation: AAH72925.1.
RefSeqNP_001085557.1. NM_001092088.1.
UniGeneXl.7160.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT61. Glycosyltransferase Family 61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID443983.
KEGGxla:443983.

Organism-specific databases

CTD285203.
XenbaseXB-GENE-994622. eogt.

Phylogenomic databases

HOVERGENHBG056678.

Family and domain databases

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

Entry information

Entry nameEOGT_XENLA
AccessionPrimary (citable) accession number: Q6GQ23
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2004
Last modified: November 28, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families