Galnt2 polypeptide N-acetylgalactosaminyltransferase 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Galnt2provided by MGI
Official Full Name: polypeptide N-acetylgalactosaminyltransferase 2provided by MGI
Primary source: MGI:MGI:894694
See related: Ensembl:ENSMUSG00000089704 AllianceGenome:MGI:894694
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Summary: Predicted to enable manganese ion binding activity and polypeptide N-acetylgalactosaminyltransferase activity. Predicted to be involved in protein O-linked glycosylation via serine; protein O-linked glycosylation via threonine; and protein maturation. Predicted to be located in Golgi stack and perinuclear region of cytoplasm. Predicted to be active in Golgi apparatus. Is expressed in several structures, including alimentary system; floor plate; lens; lung mesenchyme; and submandibular gland primordium. Human ortholog(s) of this gene implicated in congenital disorder of glycosylation type II. Orthologous to human GALNT2 (polypeptide N-acetylgalactosaminyltransferase 2). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in subcutaneous fat pad adult (RPKM 50.6), genital fat pad adult (RPKM 48.6) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 8 E2; 8 72.52 cM

Exon count:: 16

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	8	NC_000074.7 (124958133..125072461)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	8	NC_000074.6 (124231394..124345722)

Chromosome 8 - NC_000074.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The O-glycosylating enzyme GALNT2 acts as an oncogenic driver in non-small cell lung cancer.
Title: The O-glycosylating enzyme GALNT2 acts as an oncogenic driver in non-small cell lung cancer.
Morphological and molecular characterization of GALNT2-mediated adipogenesis.
Title: Morphological and molecular characterization of GALNT2-mediated adipogenesis.
GALNT2 regulates ANGPTL3 cleavage in cells and in vivo of mice.
Title: GALNT2 regulates ANGPTL3 cleavage in cells and in vivo of mice.
Investigated the effect of polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) on adipogenesis, lipid accumulation and insulin signaling in cultured mouse adipocytes.
Title: GALNT2 as a novel modulator of adipogenesis and adipocyte insulin signaling.
These results posit GALNT2 as a direct modulator of high density lipoprotein metabolism across mammals.
Title: Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.
These data suggest that the region responsible for the Mvwf1 regulatory switch lies within an approximately 30-kb genomic interval upstream of the B4galnt2 gene.
Title: The endothelial-specific regulatory mutation, Mvwf1, is a common mouse founder allele.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Gene trapped (2)
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:236032

Galnt2 (e-PCR), detects polymorphism
- UniSTS:495909

NoName (e-PCR)
- UniSTS:224852

AI480629 (e-PCR)
- UniSTS:159838

NoName (e-PCR)
- UniSTS:236031

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables carbohydrate binding	IEA Inferred from Electronic Annotation more info
enables manganese ion binding	ISO Inferred from Sequence Orthology more info
enables manganese ion binding	ISS Inferred from Sequence or Structural Similarity more info
enables polypeptide N-acetylgalactosaminyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables polypeptide N-acetylgalactosaminyltransferase activity	ISA Inferred from Sequence Alignment more info	PubMed
enables polypeptide N-acetylgalactosaminyltransferase activity	ISO Inferred from Sequence Orthology more info
enables polypeptide N-acetylgalactosaminyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in O-glycan processing	IEA Inferred from Electronic Annotation more info
involved_in protein O-linked glycosylation	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within protein O-linked glycosylation	ISA Inferred from Sequence Alignment more info	PubMed
involved_in protein O-linked glycosylation	ISO Inferred from Sequence Orthology more info
involved_in protein O-linked glycosylation	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein O-linked glycosylation via serine	IEA Inferred from Electronic Annotation more info
involved_in protein O-linked glycosylation via serine	ISO Inferred from Sequence Orthology more info
involved_in protein O-linked glycosylation via threonine	IEA Inferred from Electronic Annotation more info
involved_in protein O-linked glycosylation via threonine	ISO Inferred from Sequence Orthology more info
involved_in protein maturation	IEA Inferred from Electronic Annotation more info
involved_in protein maturation	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	IBA Inferred from Biological aspect of Ancestor more info
colocalizes_with Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in Golgi cisterna membrane	IEA Inferred from Electronic Annotation more info
located_in Golgi lumen	TAS Traceable Author Statement more info	PubMed
located_in Golgi stack	ISO Inferred from Sequence Orthology more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: polypeptide N-acetylgalactosaminyltransferase 2

Names: UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2; UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2; galNAc-T2; polypeptide GalNAc transferase 2; pp-GaNTase 2; ppGaNTase-T2; protein-UDP acetylgalactosaminyltransferase 2

NP_644678.2

EC 2.4.1.41

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_139272.2 → NP_644678.2 polypeptide N-acetylgalactosaminyltransferase 2

See identical proteins and their annotated locations for NP_644678.2

Status: VALIDATED

Source sequence(s)

BC053063, BC059818, BQ770019

Consensus CDS

CCDS22769.1

UniProtKB/Swiss-Prot

Q6PB93, Q7TSI5, Q8BL27, Q922K5, Q99ME1

UniProtKB/TrEMBL

Q3UA32

Related

ENSMUSP00000034458.9, ENSMUST00000034458.9

Conserved Domains (3) summary

cd02510
Location:138 → 433

pp-GalNAc-T; pp-GalNAc-T initiates the formation of mucin-type O-linked glycans

cd00161
Location:455 → 564

RICIN; Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ...

pfam00652
Location:445 → 562

Ricin_B_lectin; Ricin-type beta-trefoil lectin domain