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Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

Galnt13

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei155SubstrateBy similarity1
Binding sitei185SubstrateBy similarity1
Metal bindingi208ManganeseBy similarity1
Metal bindingi210ManganeseBy similarity1
Binding sitei315SubstrateBy similarity1
Metal bindingi343ManganeseBy similarity1
Binding sitei346SubstrateBy similarity1
Binding sitei351SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Galnt13
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi735044. Galnt13.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini28 – 556LumenalSequence analysisAdd BLAST529

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591321 – 556Polypeptide N-acetylgalactosaminyltransferase 13Add BLAST556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi105 ↔ 338PROSITE-ProRule annotation
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi329 ↔ 407PROSITE-ProRule annotation
Disulfide bondi441 ↔ 458PROSITE-ProRule annotation
Disulfide bondi481 ↔ 496PROSITE-ProRule annotation
Disulfide bondi522 ↔ 539PROSITE-ProRule annotation
Glycosylationi551N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6UE39.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005335.
GenevisibleiQ6UE39. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000042772.

Structurei

3D structure databases

ProteinModelPortaliQ6UE39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini428 – 550Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 224Catalytic subdomain AAdd BLAST111
Regioni284 – 346Catalytic subdomain BAdd BLAST63

Domaini

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 similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ6UE39.
KOiK00710.
OMAiIMSDDLC.
OrthoDBiEOG091G085O.
PhylomeDBiQ6UE39.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6UE39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRLVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI
60 70 80 90 100
SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV
110 120 130 140 150
RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV
160 170 180 190 200
ILVDDASERD FLKLTLENYV KTLEVPVKII RMEERSGLIR ARLRGAAASK
210 220 230 240 250
GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG
260 270 280 290 300
SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN
310 320 330 340 350
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP
360 370 380 390 400
YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT
410 420 430 440 450
LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN
460 470 480 490 500
EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLSGP VIMLKCHHMR
510 520 530 540 550
GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR

NMTLGT
Length:556
Mass (Da):63,949
Last modified:July 5, 2004 - v1
Checksum:i5AEEB9F0F4ECD148
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY371923 mRNA. Translation: AAQ75749.1.
RefSeqiNP_954537.1. NM_199106.1.
XP_017447165.1. XM_017591676.1.
UniGeneiRn.39371.

Genome annotation databases

EnsembliENSRNOT00000048804; ENSRNOP00000042772; ENSRNOG00000005335.
GeneIDi311039.
KEGGirno:311039.
UCSCiRGD:735044. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY371923 mRNA. Translation: AAQ75749.1.
RefSeqiNP_954537.1. NM_199106.1.
XP_017447165.1. XM_017591676.1.
UniGeneiRn.39371.

3D structure databases

ProteinModelPortaliQ6UE39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000042772.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbiQ6UE39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000048804; ENSRNOP00000042772; ENSRNOG00000005335.
GeneIDi311039.
KEGGirno:311039.
UCSCiRGD:735044. rat.

Organism-specific databases

CTDi114805.
RGDi735044. Galnt13.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ6UE39.
KOiK00710.
OMAiIMSDDLC.
OrthoDBiEOG091G085O.
PhylomeDBiQ6UE39.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-RNO-913709. O-linked glycosylation of mucins.

Miscellaneous databases

PROiQ6UE39.

Gene expression databases

BgeeiENSRNOG00000005335.
GenevisibleiQ6UE39. RN.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLT13_RAT
AccessioniPrimary (citable) accession number: Q6UE39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.