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Reviewed, UniProtKB/Swiss-Prot Q8I136 (GALT4_CAEEL)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Polypeptide N-acetylgalactosaminyltransferase 4
      Short name=pp-GaNTase 4
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 4
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Gene names
Name: gly-4
ORF Names: Y116F11B.12
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Ref.1

Cofactor

Manganese By similarity.

Calcium 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

O163131EBI-314302,EBI-314267

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q8I136-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform b (identifier: Q8I136-2)

The sequence of this isoform differs from the canonical sequence as follows:
     453-453: E → D
     454-589: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Polypeptide N-acetylgalactosaminyltransferase 4
PRO_0000059147

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3120Signal-anchor for type II membrane protein Potential
Topological domain32 – 589558Lumenal Potential
Domain458 – 589132Ricin B-type lectin
Region150 – 255106Catalytic subdomain A
Region315 – 37763Catalytic subdomain B
Compositional bias37 – 7236Pro-rich

Amino acid modifications

Glycosylation5231N-linked (GlcNAc...) Potential
Disulfide bond471 ↔ 488 By similarity
Disulfide bond514 ↔ 531 By similarity
Disulfide bond553 ↔ 571 By similarity

Natural variations

Alternative sequence4531E → D in isoform b.
VSP_011236
Alternative sequence454 – 589136Missing in isoform b.
VSP_011237

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 108D621D91A329D2

FASTA58967,031
        10         20         30         40         50         60 
MLPRMLKMKT VGTVLAVIWL FGLAFIYVQS TSSSLRPPGR HPPPLPQLDP LIPQNPPQND 

        70         80         90        100        110        120 
EIRPKKSAPP IPTINLAEDT TIHERTEKDV TWKTFDVEKF LNKGKWHQGE DKYKANSFNQ 

       130        140        150        160        170        180 
EASDALNPTR KIPDSREPQC RDVDYSKVGM QPTTVIITYH NEARSSLLRT VFSVFNQSPE 

       190        200        210        220        230        240 
ELLLEIVLVD DNSQDVEIGK ELAQIQRITV LRNNQREGLI RSRVKGAQVA RAPVLTFLDS 

       250        260        270        280        290        300 
HIECNQKWLE PLLARIAENP KAVVAPIIDV INVDNFNYVG ASADLRGGFD WTLVFRWEFM 

       310        320        330        340        350        360 
NEQLRKERHA HPTAPIRSPT MAGGLFAISK EWFNELGTYD LDMEVWGGEN LEMSFRVWQC 

       370        380        390        400        410        420 
GGSLEIMPCS RVGHVFRKKH PYTFPGGSGN VFQKNTRRAA EVWMDEYKAI YLKNVPSARF 

       430        440        450        460        470        480 
VNFGDITDRL AIRDRLQCKS FKWYLENVYP QLEIPRKTPG KSFQMKIGNL CLDSMARKES 

       490        500        510        520        530        540 
EAPGLFGCHG TGGNQEWVFD QLTKTFKNAI SQLCLDFSSN TENKTVTMVK CENLRPDTMV 

       550        560        570        580 
VEKNGWLTQG GKCLTVNQGS GGDWLIYGAH CELNNGAQRW IFEKLDTYE 

« Hide

Isoform b.

Checksum: 572763F5D4D25B53
Show »

FASTA45351,879

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: 9525933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ENZYME ACTIVITY.
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: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: Bristol N2.

Cross-references

Sequence databases

AF031834 mRNA. Translation: AAC13670.1.
AL132943 Genomic DNA. Translation: CAB81985.3.
AL132943 Genomic DNA. Translation: CAC14394.1.
PIRT42244.
RefSeqNP_001024216.1.
UniGeneCel.19666

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8I136. 2 interactions.

Protein family/group databases

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

Proteomic databases

PRIDEQ8I136.

Genome annotation databases

EnsemblY116F11B.12. Caenorhabditis elegans. [Contig view]
GeneID180302.
KEGGcel:Y116F11B.12.

Organism-specific databases

WormBaseWBGene00001629. gly-4.
WormPepY116F11B.12a. CE26046. [WorfDB]
Y116F11B.12b. CE32074. [WorfDB]

Phylogenomic databases

OMAQ8I136. TIHERTE.

Enzyme and pathway databases

BRENDA2.4.1.41. 672.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
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]
PROSITEPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio908800.

Entry information

Entry nameGALT4_CAEEL
AccessionPrimary (citable) accession number: Q8I136
Secondary accession number(s): O61390
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents