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P34678 (GALT3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. 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:
Polypeptide N-acetylgalactosaminyltransferase 3

EC=2.4.1.41
Alternative name(s):
GalNAc-T1
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Short name=pp-GaNTase 3
Gene names
Name:gly-3
ORF Names:ZK688.8
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1

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.

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similarities

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

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 612612Polypeptide N-acetylgalactosaminyltransferase 3
PRO_0000059146

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 612578Lumenal Potential
Domain478 – 607130Ricin B-type lectin
Region169 – 279111Catalytic subdomain A
Region339 – 40163Catalytic subdomain B

Sites

Metal binding2631Manganese By similarity
Metal binding2651Manganese By similarity
Metal binding3981Manganese By similarity
Binding site2101Substrate By similarity
Binding site2401Substrate By similarity
Binding site3701Substrate By similarity
Binding site4011Substrate By similarity
Binding site4061Substrate By similarity

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Disulfide bond157 ↔ 393 By similarity
Disulfide bond384 ↔ 462 By similarity
Disulfide bond496 ↔ 513 By similarity
Disulfide bond536 ↔ 554 By similarity
Disulfide bond582 ↔ 595 By similarity

Sequences

Sequence LengthMass (Da)Tools
P34678 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 3031C2FE933F9858

FASTA61268,912
        10         20         30         40         50         60 
MLSVGGGRSA VCRAVIATSI VWLLIDVVIL FYYLDPSTSQ QQPFPEDNRI LNRARRIEPL 

        70         80         90        100        110        120 
PPAAQHDSDP DAHPIQPEKQ EKQVYPVDKE TANQLRKLME TQAFGPGYHG QGGTGVTVPE 

       130        140        150        160        170        180 
DKKTIKEKRF LENQFNVVAS EMISVNRTLP DYRSDACRTS GNNLKTAGMP KTSIIIVFHN 

       190        200        210        220        230        240 
EAWTTLLRTL HSVINRSPRH LLEEIILVDD KSDRDYLVKP LDSYIKMFPI PIHLVHLENR 

       250        260        270        280        290        300 
SGLIRARLTG SEMAKGKILL FLDAHVEVTD GWLEPLVSRV AEDRKRVVAP IIDVISDDTF 

       310        320        330        340        350        360 
EYVTASETTW GGFNWHLNFR WYAVPKRELN RRGSDRSMPI QTPTIAGGLF AIDKQFFYDI 

       370        380        390        400        410        420 
GSYDEGMQVW GGENLEISFR VWMCGGSLEI HPCSRVGHVF RKQTPYTFPG GTAKVIHHNA 

       430        440        450        460        470        480 
ARTAEVWMDE YKAFFYKMVP AARNVEAGDV SERKKLRETL QCKSFKWYLE NIYPEAPLPA 

       490        500        510        520        530        540 
DFRSLGAIVN RFTEKCVDTN GKKDGQAPGI QACHGAGGNQ AWSLTGKGEI RSDDLCLSSG 

       550        560        570        580        590        600 
HVYQIGSELK LERCSVSKIN VKHVFVFDDQ AGTLLHKKTG KCVTGADQRV TLDECGLGRK 

       610 
DQMWQLEGYQ SP 

« 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], ENZYME ACTIVITY.
Strain: Bristol N2.
[2]"2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans."
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L. expand/collapse author list , Gardner A., Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., Wohldman P.
Nature 368:32-38(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031833 mRNA. Translation: AAC13669.1.
FO080277 Genomic DNA. Translation: CCD62541.1.
PIRA88515.
T42243.
RefSeqNP_498722.1. NM_066321.5.
UniGeneCel.17588.

3D structure databases

ProteinModelPortalP34678.
SMRP34678. Positions 110-611.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.ZK688.8.1.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbP34678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaZK688.8; ZK688.8; WBGene00001628.
GeneID176112.
KEGGcel:CELE_ZK688.8.
UCSCZK688.8.1. c. elegans.

Organism-specific databases

CTD176112.
WormBaseZK688.8; CE29649; WBGene00001628; gly-3.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000038227.
InParanoidP34678.
KOK00710.
OMACRAVIAT.
OrthoDBEOG7J9VP2.
PhylomeDBP34678.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio891164.
PROP34678.

Entry information

Entry nameGALT3_CAEEL
AccessionPrimary (citable) accession number: P34678
Secondary accession number(s): Q9U003
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 27, 2002
Last modified: June 11, 2014
This is version 120 of the entry and version 2 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