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Q6UE39 (GLT13_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 13
EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 13
Short name=GalNAc-T13
Short name=pp-GaNTase 13
Protein-UDP acetylgalactosaminyltransferase 13
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Gene names
Name:Galnt13
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length556 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. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells By similarity.

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.

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 – 556556Polypeptide N-acetylgalactosaminyltransferase 13
PRO_0000059132

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2723Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 556529Lumenal Potential
Domain428 – 550123Ricin B-type lectin
Region114 – 224111Catalytic subdomain A
Region284 – 34663Catalytic subdomain B

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Disulfide bond441 ↔ 458 By similarity
Disulfide bond481 ↔ 496 By similarity
Disulfide bond522 ↔ 539 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6UE39 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5AEEB9F0F4ECD148

FASTA55663,949
        10         20         30         40         50         60 
MRRLVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM 

        70         80         90        100        110        120 
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV 

       130        140        150        160        170        180 
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII 

       190        200        210        220        230        240 
RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI 

       250        260        270        280        290        300 
SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 

       310        320        330        340        350        360 
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV 

       370        380        390        400        410        420 
INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD 

       430        440        450        460        470        480 
SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL 

       490        500        510        520        530        540 
CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS 

       550 
GSRSQQWLLR NMTLGT

« Hide

References

[1]Huang C.Q., Wu S.L., Liu S.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY371923 mRNA. Translation: AAQ75749.1.
IPIIPI00400577.
RefSeqNP_954537.1. NM_199106.1.
UniGeneRn.39371.

3D structure databases

ProteinModelPortalQ6UE39.
SMRQ6UE39. Positions 94-552.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000042772.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000048804; ENSRNOP00000042772; ENSRNOG00000005335.
GeneID311039.
KEGGrno:311039.
UCSCRGD:735044. rat.

Organism-specific databases

CTD114805.
RGD735044. Galnt13.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00700000104138.
HOVERGENHBG051699.
KOK00710.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ6UE39.

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]
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio662923.

Entry information

Entry nameGLT13_RAT
AccessionPrimary (citable) accession number: Q6UE39
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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