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Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

Galnt13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. Probably responsible for the synthesis of Tn antigen in neuronal cells.2 Publications

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

  • protein O-linked glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2139447. 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

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. It however abolishes Tn antigen in neuronal cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591311 – 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

PaxDbiQ8CF93.
PRIDEiQ8CF93.

PTM databases

iPTMnetiQ8CF93.
PhosphoSitePlusiQ8CF93.

Expressioni

Tissue specificityi

Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level.2 Publications

Gene expression databases

BgeeiENSMUSG00000060988.
ExpressionAtlasiQ8CF93. baseline and differential.
GenevisibleiQ8CF93. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063464.

Structurei

3D structure databases

ProteinModelPortaliQ8CF93.
SMRiQ8CF93.
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.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8CF93.
KOiK00710.
OMAiIMSDDLC.
OrthoDBiEOG091G085O.
TreeFamiTF313267.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CF93-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRRFVYCKVV 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):63,983
Last modified:March 1, 2003 - v1
Checksum:i593934CFD0AED148
GO
Isoform 2 (identifier: Q8CF93-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     466-466: V → VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV

Note: No experimental confirmation available.
Show »
Length:592
Mass (Da):67,796
Checksum:i54A13935542D268C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti457N → K in BAC32353 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011220466V → VHDLCLSAPSLGVGAEECCS NHPLYGLVYTPTINEQV in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082928 mRNA. Translation: BAC54546.1.
AK038387 mRNA. Translation: BAC29981.1.
AK045417 mRNA. Translation: BAC32353.1.
CCDSiCCDS16041.1. [Q8CF93-1]
RefSeqiNP_766618.2. NM_173030.2. [Q8CF93-1]
XP_006498154.1. XM_006498091.2. [Q8CF93-1]
XP_006498155.1. XM_006498092.2. [Q8CF93-1]
UniGeneiMm.330227.

Genome annotation databases

EnsembliENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
GeneIDi271786.
KEGGimmu:271786.
UCSCiuc008jrq.1. mouse. [Q8CF93-1]
uc012bvm.1. mouse. [Q8CF93-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082928 mRNA. Translation: BAC54546.1.
AK038387 mRNA. Translation: BAC29981.1.
AK045417 mRNA. Translation: BAC32353.1.
CCDSiCCDS16041.1. [Q8CF93-1]
RefSeqiNP_766618.2. NM_173030.2. [Q8CF93-1]
XP_006498154.1. XM_006498091.2. [Q8CF93-1]
XP_006498155.1. XM_006498092.2. [Q8CF93-1]
UniGeneiMm.330227.

3D structure databases

ProteinModelPortaliQ8CF93.
SMRiQ8CF93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063464.

Protein family/group databases

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

PTM databases

iPTMnetiQ8CF93.
PhosphoSitePlusiQ8CF93.

Proteomic databases

PaxDbiQ8CF93.
PRIDEiQ8CF93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
GeneIDi271786.
KEGGimmu:271786.
UCSCiuc008jrq.1. mouse. [Q8CF93-1]
uc012bvm.1. mouse. [Q8CF93-2]

Organism-specific databases

CTDi114805.
MGIiMGI:2139447. Galnt13.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8CF93.
KOiK00710.
OMAiIMSDDLC.
OrthoDBiEOG091G085O.
TreeFamiTF313267.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiGalnt13. mouse.
PROiQ8CF93.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000060988.
ExpressionAtlasiQ8CF93. baseline and differential.
GenevisibleiQ8CF93. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q8CF93
Secondary accession number(s): Q8BLE4, Q8BYT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was initially wrongly assigned as Galnt8.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.