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O45293 (GALT8_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Probable N-acetylgalactosaminyltransferase 8

EC=2.4.1.-
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 8
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Short name=pp-GaNTase 8
Gene names
Name:gly-8
ORF Names:Y66A7A.6
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potential glycopeptide transferase involved in O-linked oligosaccharide biosynthesis By similarity. In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Caution

In contrast to other members of the family, it lacks the C-terminal ricin B-type lectin domain, which usually contributes to the glycopeptide specificity. It instead contains a motif that may retain its secretion form the endoplasmic reticulum.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Probable N-acetylgalactosaminyltransferase 8
PRO_0000059151

Regions

Topological domain1 – 33Cytoplasmic Potential
Transmembrane4 – 2421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 421397Lumenal Potential
Region106 – 219114Catalytic subdomain A
Region277 – 33963Catalytic subdomain B
Motif418 – 4214Prevents secretion from ER Potential

Sites

Metal binding2031Manganese By similarity
Metal binding2051Manganese By similarity
Metal binding3361Manganese By similarity
Binding site1471Substrate By similarity
Binding site1801Substrate By similarity
Binding site2041Substrate By similarity
Binding site3081Substrate By similarity
Binding site3391Substrate By similarity
Binding site3441Substrate By similarity

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Ref.3
Glycosylation581N-linked (GlcNAc...) Ref.3
Disulfide bond98 ↔ 331 By similarity
Disulfide bond322 ↔ 399 By similarity

Sequences

Sequence LengthMass (Da)Tools
O45293 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 3FA38E18702D087D

FASTA42148,358
        10         20         30         40         50         60 
MRRHVVLSIF VFAGIVFAAE EAEKLPKCEH VDPYENLEGW LDLKPLTERK CNHTLKENLT 

        70         80         90        100        110        120 
EAESKKSEWG IKSFAFDALS SEKLGPNRNV GKQAHKLCEE EKYDASYSTS VVVIHHNEAL 

       130        140        150        160        170        180 
STILRMINGI IEFTPKSLLK EIVLYEDASE EDHVLTKHLE KFAKIKGLED KLIIKRSEYR 

       190        200        210        220        230        240 
QGLIRAKVHA SRLATGEVIV FMDSHCEVAE RWLEPLLQPI KEDPKSIVLP VVDLINPVSF 

       250        260        270        280        290        300 
DYSPSMVAKS GFDWGFTFKW IYLPWEYFET PENNVKPFNS PAMPGGLLAM RKEYFVELGE 

       310        320        330        340        350        360 
YDMGMEIWGS ENIELSLKAW LCGGRVVVAP CSRVGHVFRM RRPYTSKPGM DTALYNAVRV 

       370        380        390        400        410        420 
AKTWLGEYES KFFAVKPRGA KMVFGDLTEP MQVKDRLKCK DMKWFIENVY PELEPKVHDE 


L 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans."
Hagen F.K., Nehrke K.
J. Biol. Chem. 273:8268-8277(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-58, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031842 mRNA. Translation: AAC13678.1.
AL590342 Genomic DNA. Translation: CAC35860.1.
PIRT42252.
RefSeqNP_499504.1. NM_067103.4.
UniGeneCel.19663.

3D structure databases

ProteinModelPortalO45293.
SMRO45293. Positions 76-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41776. 2 interactions.
DIPDIP-24790N.
MINTMINT-1070872.
STRING6239.Y66A7A.6.1.

Protein family/group databases

CAZyGT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbO45293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY66A7A.6.1; Y66A7A.6.1; WBGene00001633.
Y66A7A.6.2; Y66A7A.6.2; WBGene00001633.
GeneID176595.
KEGGcel:CELE_Y66A7A.6.
UCSCY66A7A.6.1. c. elegans.

Organism-specific databases

CTD176595.
WormBaseY66A7A.6; CE15691; WBGene00001633; gly-8.

Phylogenomic databases

eggNOGNOG295988.
GeneTreeENSGT00670000097647.
HOGENOMHOG000038227.
InParanoidO45293.
OMAPENNVKP.
PhylomeDBO45293.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio893222.
PROO45293.

Entry information

Entry nameGALT8_CAEEL
AccessionPrimary (citable) accession number: O45293
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase