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Q6DJR8 (GLT11_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 11

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name=GalNAc-T11
Short name=pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene names
Name:galnt11
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis) [Reference proteome]
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Ref.2

Catalytic activity

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

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with notch1. Ref.2

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.

Disruption phenotype

Aberrant left-right patterning resulting in abnormal cardiac loops, including leftward and symmetric/midline loops. Ref.2

Sequence similarities

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

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence AAH75106.1 differs from that shown. Reason: Frameshift at position 39.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Polypeptide N-acetylgalactosaminyltransferase 11
PRO_0000425208

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 601573Lumenal Potential
Domain469 – 600132Ricin B-type lectin
Region143 – 254112Catalytic subdomain A By similarity
Region312 – 37463Catalytic subdomain B By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Disulfide bond486 ↔ 505 By similarity
Disulfide bond529 ↔ 546 By similarity
Disulfide bond571 ↔ 589 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6DJR8 [UniParc].

Last modified January 22, 2014. Version 2.
Checksum: 1FA0294A3CEEA236

FASTA60168,383
        10         20         30         40         50         60 
MGSAALRCFC YGCLFTSVTW TLLLFIYFNF SEESQGFRHV PVKGLEPYKP LPKKIYPRFS 

        70         80         90        100        110        120 
RDSMGQHSDP RKGHNGNQLE TEANADLSPE LGMIFNEQDQ DVRDVGYQKH AFNLLISNRL 

       130        140        150        160        170        180 
GYHRDVPDTR DSKCAKKTYP PDLPMASIVI CFYNEAFSAL LRTVHSVLDR TPAQLLHEII 

       190        200        210        220        230        240 
LVDDNSELDD LKKDLDGYMQ ENLSKKVKLV RNKQREGLIR GRMVGASHAT GDVLVFLDSH 

       250        260        270        280        290        300 
CEVNEMWLQP LLAPIKENPR TVVCPVIDII SADTLIYSSS PVVRGGFNWG LHFKWDPVPL 

       310        320        330        340        350        360 
AELGGPEGFS APFRSPTMAG GLFAMDREYF NMLGQYDSGM DIWGGENLEI SFRIWMCGGS 

       370        380        390        400        410        420 
LLIVPCSRVG HIFRKRRPYG SPGGHDTMAH NSLRLAHVWM DEYKDQYFAL RPELRNRDFG 

       430        440        450        460        470        480 
DIRERLALRR RLNCKSFKWY LDNIYPEMQV SGPNAKPQPP VFMNKGQKRP KILQRGRLIN 

       490        500        510        520        530        540 
MQTNRCLVAQ GHPSQKGGLV VAKECDYNDS EQVWSYNEEH ELILSNLLCL DMSETRSSDP 

       550        560        570        580        590        600 
PRLMKCHGSG GSQQWVFGKS NRLYQVSVGQ CLKLVDPMSR KGYVSMAICD GSPSQQWHLE 


N 

« Hide

References

« Hide 'large scale' references
[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[2]"The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH NOTCH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC075106 mRNA. Translation: AAH75106.1. Frameshift.
RefSeqNP_001006904.1. NM_001006903.1.
UniGeneStr.1760.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID448751.
KEGGxtr:448751.

Organism-specific databases

CTD63917.
XenbaseXB-GENE-981830. galnt11.

Phylogenomic databases

HOVERGENHBG051699.
KOK00710.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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...

Entry information

Entry nameGLT11_XENTR
AccessionPrimary (citable) accession number: Q6DJR8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: January 22, 2014
Last modified: July 9, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways