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Reviewed, UniProtKB/Swiss-Prot O45947 (GLT10_CAEEL)

Last modified November 4, 2008. Version 59. 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

Names and origin

Protein namesRecommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase 10
      Short name=pp-GaNTase 10
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene names
Name: gly-10
ORF Names: Y45F10D.3
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May catalyze 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 By similarity.

Catalytic activity

UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane proteinBy 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: O45947-1)

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.
Notes: No experimental confirmation available.
Isoform b (identifier: O45947-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684Putative polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000059153

Regions

Topological domain1 – 7474Cytoplasmic Potential
Transmembrane75 – 9521Signal-anchor for type II membrane protein Potential
Topological domain96 – 684589Lumenal Potential
Domain581 – 684104Ricin B-type lectin
Region218 – 330113Catalytic subdomain A
Region386 – 44863Catalytic subdomain B
Region448 – 46114Flexible loop By similarity

Sites

Metal binding3141Manganese By similarity
Metal binding3161Manganese By similarity
Metal binding4451Manganese By similarity
Binding site2591Substrate By similarity
Binding site3141Substrate By similarity

Amino acid modifications

Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Ref.3
Disulfide bond209 ↔ 440 By similarity
Disulfide bond431 ↔ 509 By similarity
Disulfide bond594 ↔ 611 By similarity
Disulfide bond637 ↔ 653 By similarity

Natural variations

Alternative sequence1 – 6262Missing in isoform b.
VSP_032724

Sequences

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

Last modified April 8, 2008. Version 3.
Checksum: 59B9B3F84C2B3445

FASTA68478,971
        10         20         30         40         50         60 
MVAICIKIGE RERKRVHIML LAYTWKTRVS SHQCNKSPIF GLFAIQFSNI CSNLLLLQQK 

        70         80         90        100        110        120 
LSMGLSRYLS RRHHWVIQYC GLLLFLYLIY SYVATSNDGP NLHEDIPVFQ GQGKDRANPN 

       130        140        150        160        170        180 
PPAALGDEAL DPFEKYRGHE KIKWEDEAAY EKEKRREGPG EWGKPVKLPE DKEVEKEALS 

       190        200        210        220        230        240 
LYKANGYNAY ISDMISLNRS IKDIRHKECK NMMYSAKLPT VSVIFPFHEE HNSTLLRSVY 

       250        260        270        280        290        300 
SVINRSPPEL LKEIILVDDF SEKPALRQPL EDFLKKNKID HIVKVLRTKK REGLIRGRQL 

       310        320        330        340        350        360 
GAQDATGEIL IFLDAHSEAN YNWLPPLLDP IAEDYRTVVC PFVDVIDCET YEVRPQDEGA 

       370        380        390        400        410        420 
RGSFDWAFNY KRLPLTKKDR ESPTKPFNSP VMAGGYFAIS AKWFWELGGY DEGLDIWGGE 

       430        440        450        460        470        480 
QYELSFKVWQ CHGRMVDAPC SRVAHIYRCK YAPFKNAGMG DFVSRNYKRV AEVWMDDYKE 

       490        500        510        520        530        540 
TLYKHRPGVG NADAGDLKLM KGIREKLQCK SFDWFMKEIA FDQDKYYPAV EPKASAEGEI 

       550        560        570        580        590        600 
RNVGTNFCID TQFKEQNQRF GLRKCTSDDK DGGGEQDLRL TRWHDIRPKG RKICFDCSTS 

       610        620        630        640        650        660 
VDKAPVILFD CHSMKGNQLF KYRVAQKQIY HPISGQCLTA DENGKGFLHM KKCDSSSDLQ 

       670        680 
KWAWQTVDNE LLETRQANEA KEQE 

« Hide

Isoform b.

Checksum: F8A3A21159C7E452
Show »

62271,812

References

« Hide 'large scale' references
[1]"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.
[2]"The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation."
Wang H., Spang A., Sullivan M.A., Hryhorenko J., Hagen F.K.
Mol. Biol. Cell 16:4202-4213(2005) [PubMed: 15987734] [Abstract]
Cited for: IDENTIFICATION.
[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: 17761667] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, MASS SPECTROMETRY.

Cross-references

Sequence databases

AL021492 Genomic DNA. Translation: CAA16378.1.
AL021492 Genomic DNA. Translation: CAJ76949.1.
PIRT26930.
RefSeqNP_001041036.1.
UniGeneCel.6680

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblY45F10D.3. Caenorhabditis elegans. [Contig view]
GeneID178343.
KEGGcel:Y45F10D.3.

Organism-specific databases

WormBaseWBGene00012884. Y45F10D.3.
WormPepY45F10D.3a. CE16642. [WorfDB]
Y45F10D.3b. CE39841. [WorfDB]

Gene expression databases

ArrayExpressO45947.

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

NextBio900740.

Entry information

Entry nameGLT10_CAEEL
AccessionPrimary (citable) accession number: O45947
Secondary accession number(s): Q2HQM0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: April 8, 2008
Last modified: November 4, 2008
This is version 59 of the entry and version 3 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents