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Q5NDL9 (EOGT_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length527 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
   Technical termComplete proteome
Reference proteome
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 – 1717 Potential
Chain18 – 527510EGF domain-specific O-linked N-acetylglucosamine transferase
PRO_0000301971

Regions

Motif295 – 2973Required for optimal activity By similarity
Motif524 – 5274Prevents secretion from ER Potential

Amino acid modifications

Glycosylation3541N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5NDL9 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: DA5DE507862BB6AA

FASTA52761,670
        10         20         30         40         50         60 
MLKLLVLGVL LHDVSLSGQD EAPPKADGIP GEPLFNYASI RLPEEHIPFF LHNNRHIATV 

        70         80         90        100        110        120 
CKKDSHCPYK KHLENLKYCW GYEKSCKPEF RFGYPVCTYI DMGWTDTLES AQDIFWKQAD 

       130        140        150        160        170        180 
FGYAGERLEE LHVLCQPEEP HDSSLLCSRY LQYCRAANLY LDLRNIKRNH DRFKEDFFQS 

       190        200        210        220        230        240 
GEIGGHCTLD TQTLLSEGQR KSPLQSWFAE LQSYTELNFR PIEDAKCDVV IEKPTYFMKL 

       250        260        270        280        290        300 
DAGVNMYHHF CDFVNLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW KAFTDYDVIH 

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

       370        380        390        400        410        420 
KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTLEVQIV DYKYKELGFL DQLRITHNTD 

       430        440        450        460        470        480 
IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG 

       490        500        510        520 
HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKRDEL 

« Hide

References

[1]"Phylogeny of xylosyltransferases."
Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V., Mollicone R., Oriol R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ868227 mRNA. Translation: CAI30562.1.
RefSeqNP_001009187.1. NM_001009187.1.
XP_005632096.1. XM_005632039.1.
XP_005632097.1. XM_005632040.1.
XP_005632098.1. XM_005632041.1.
UniGeneCfa.16220.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000009819.

Protein family/group databases

CAZyGT61. Glycosyltransferase Family 61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID494221.
KEGGcfa:494221.

Organism-specific databases

CTD285203.

Phylogenomic databases

eggNOGNOG320328.
HOGENOMHOG000033829.
HOVERGENHBG056678.
InParanoidQ5NDL9.
KOK18134.
OrthoDBEOG7D2FDQ.

Family and domain databases

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

Other

NextBio20865674.

Entry information

Entry nameEOGT_CANFA
AccessionPrimary (citable) accession number: Q5NDL9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 50 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