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Reviewed, UniProtKB/Swiss-Prot Q9U2C4 (GALT9_CAEEL)

Last modified June 16, 2009. Version 55. 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable N-acetylgalactosaminyltransferase 9
    EC=2.4.1.-
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 9
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
      Short name=pp-GaNTase 9
Gene names
Name: gly-9
ORF Names: Y47D3A.23
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide 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.

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.

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q9U2C4-1)

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: Q9U2C4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-254: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Probable N-acetylgalactosaminyltransferase 9
PRO_0000059152

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3018Signal-anchor for type II membrane protein Potential
Topological domain31 – 579549Lumenal Potential
Domain450 – 574125Ricin B-type lectin
Region133 – 243111Catalytic subdomain A
Region302 – 36463Catalytic subdomain B

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Disulfide bond464 ↔ 483 By similarity
Disulfide bond507 ↔ 520 By similarity
Disulfide bond545 ↔ 562 By similarity

Natural variations

Alternative sequence1 – 254254Missing in isoform b.
VSP_020151

Experimental info

Sequence conflict2031V → D in AAC13679. Ref.1

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Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 2F50B222CFB13597

FASTA57966,430
        10         20         30         40         50         60 
MLRYIIPRKK GTFVIAAFLT VAFFCIVAYH RNDRRRTKFQ FPDIEKYAEE LVRLPETWNG 

        70         80         90        100        110        120 
ELHQIPNYTA PREGPGEKGK PVVLTGKDAE LGQADMKKWF MNVHASDKIS LDRDVPDPRI 

       130        140        150        160        170        180 
QACKDIKYDY AALPKTSVII IFTDEAWTPL LRTVHSVINR SPPELLQEVI LLDDNSKRQE 

       190        200        210        220        230        240 
LQEPLDEHIK RFGGKVRLIR KHVRHGLIRA KLAGAREAVG DIIVFLDSHC EANHGWLEPI 

       250        260        270        280        290        300 
VQRISDERTA IVCPMIDSIS DNTLAYHGDW SLSTGGFSWA LHFTWEGLSE EEQKRRTKPT 

       310        320        330        340        350        360 
DYIRSPTMAG GLLAANREYF FEVGGYDEEM DIWGGENLEI SFRAWMCGGS IEFIPCSHVG 

       370        380        390        400        410        420 
HIFRAGHPYN MTGRNNNKDV HGTNSKRLAE VWMDDYKRLY YMHREDLRTK DVGDLTARHE 

       430        440        450        460        470        480 
LRKRLNCKPF KWFLDNIAKG KFIMDEDVVA YGALHTVVSG TRMCTDTLQR DEKMSQLLGV 

       490        500        510        520        530        540 
FHCQGKGSSP QLMSLSKEGN LRRENTCASE ENGNIRMKTC SKKAQFNERW AYENKMIRNL 

       550        560        570 
KSGKCMSTAN LKPGDNAIVV ECDEKDEHQK WNFIDPAKA

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Isoform b.

Checksum: 10091A101BC8CB0A
Show »

FASTA32537,284

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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).
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.

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Cross-references

Sequence databases

AF031843 mRNA. Translation: AAC13679.1.
AL117202 Genomic DNA. Translation: CAB57897.1.
AL117202 Genomic DNA. Translation: CAI46621.1.
PIRT31549.
RefSeqNP_001022876.1.
UniGeneCel.19662

3D structure databases

ModBaseSearch...

Protein family/group databases

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

Proteomic databases

PRIDEQ9U2C4.

Genome annotation databases

EnsemblY47D3A.23. Caenorhabditis elegans. [Contig view]
GeneID176557.
KEGGcel:Y47D3A.23.
NMPDRfig|6239.3.peg.11654.

Organism-specific databases

WormBaseWBGene00012934. gly-9.
WormPepY47D3A.23a. CE24334. [WorfDB]
Y47D3A.23b. CE37859. [WorfDB]

Phylogenomic databases

OMAQ9U2C4. HREDLRT.

Gene expression databases

ArrayExpressQ9U2C4.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio893070.

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Entry information

Entry nameGALT9_CAEEL
AccessionPrimary (citable) accession number: Q9U2C4
Secondary accession number(s): O61398, Q5GMH7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

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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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents