Q09200 · B4GN1_MOUSE
- ProteinBeta-1,4 N-acetylgalactosaminyltransferase 1
- GeneB4galnt1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids533 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of gangliosides GM2, GD2 and GA2.
Involved in the biosynthesis of gangliosides GM2, GD2, GT2 and GA2 from GM3, GD3, GT3 and GA3, respectively.
Catalytic activity
- a ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GM2 (d18:1(4E)) + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GD2 (d18:1(4E)) + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GM2 + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GD2 + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GalNAc-GD1a + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GT2 (d18:1(4E)) + H+ + UDPThis reaction proceeds in the forward direction.
- a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GA2 (d18:1(4E)) + H+ + UDPThis reaction proceeds in the forward direction.
- a neolactoside IV3-alpha-NeuGc-nLc4Cer + UDP-N-acetyl-alpha-D-galactosamine = a neolactoside IV4-beta-GalNAc-IV3-alpha-NeuGc-nLc4Cer + H+ + UDPThis reaction proceeds in the forward direction.
Pathway
Sphingolipid metabolism.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity | |
Molecular Function | acetylgalactosaminyltransferase activity | |
Biological Process | determination of adult lifespan | |
Biological Process | ganglioside biosynthetic process | |
Biological Process | glycosphingolipid biosynthetic process | |
Biological Process | glycosphingolipid metabolic process | |
Biological Process | limb development | |
Biological Process | lipid glycosylation | |
Biological Process | lipid storage | |
Biological Process | motor behavior | |
Biological Process | nerve development | |
Biological Process | spermatogenesis | |
Biological Process | vacuole organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-1,4 N-acetylgalactosaminyltransferase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ09200
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MRLDRRA | ||||||
Transmembrane | 8-25 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LYALVLLLACASLGLLYS | ||||||
Topological domain | 26-533 | Lumenal | ||||
Sequence: STRNAPSLPNPLALWSPPQGPPRLDLLDLAPEPRYAHIPVRIKEQVVGLLAQNNCSCESKGGSLPLPFLRQVRAVDLTKAFDAEELRAVSVAREQEYQAFLARSRSLADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQEASVQEIYQVNLSASLGTWDVAGEVTGVTLTGEGQPDLTLASPVLDKLNRQLQLVTYSSRSYQANTADTVRFSTKGHEVAFTILVRHPPNPRLYPPSSLPQGAEYNISALVTIATKTFLRYDRLRTLIASIRRFYPTVTIVIADDSDKPERISDPHVEHYFMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLEKLVDVLEKTPLDLVGGAVREISGYATTYRQLLSVEPGAPGLGNCFRQKQGFHHELVGFPSCVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGFLRVGSCSDVVVDHASKVKLPWTAKDPGAETYARYRYPGSLDQSQVAKHRLLFFKHRLQCMTAE |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype, excepting a slight decrease in neural conduction velocity from the tibial nerve to the somatosensory cortex (PubMed:8855236).
Mutant mice display impaired motor coordination and balance (PubMed:15953602).
Sciatic nerves from over three month old mutant mice show signs of Wallerian degeneration, with redundant myelin, degeneration of myelinated fibers, axon dysmyelination, and an apparent decrease in the diameter of myelinated axons (PubMed:15953602).
The distances between neurofilaments in myelinated axons from over 3 month old mice are shorter than normal (PubMed:15953602).
Mice are less sensitive to C.botulinum neurotoxin type C (BoNT/C), C.botulinum neurotoxin type D (BoNT/D, botD) and C.botulinum neurotoxin type F (BoNT/F, botF) (PubMed:21483489).
Mutant mice display impaired motor coordination and balance (PubMed:15953602).
Sciatic nerves from over three month old mutant mice show signs of Wallerian degeneration, with redundant myelin, degeneration of myelinated fibers, axon dysmyelination, and an apparent decrease in the diameter of myelinated axons (PubMed:15953602).
The distances between neurofilaments in myelinated axons from over 3 month old mice are shorter than normal (PubMed:15953602).
Mice are less sensitive to C.botulinum neurotoxin type C (BoNT/C), C.botulinum neurotoxin type D (BoNT/D, botD) and C.botulinum neurotoxin type F (BoNT/F, botF) (PubMed:21483489).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059101 | 1-533 | Beta-1,4 N-acetylgalactosaminyltransferase 1 | |||
Sequence: MRLDRRALYALVLLLACASLGLLYSSTRNAPSLPNPLALWSPPQGPPRLDLLDLAPEPRYAHIPVRIKEQVVGLLAQNNCSCESKGGSLPLPFLRQVRAVDLTKAFDAEELRAVSVAREQEYQAFLARSRSLADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQEASVQEIYQVNLSASLGTWDVAGEVTGVTLTGEGQPDLTLASPVLDKLNRQLQLVTYSSRSYQANTADTVRFSTKGHEVAFTILVRHPPNPRLYPPSSLPQGAEYNISALVTIATKTFLRYDRLRTLIASIRRFYPTVTIVIADDSDKPERISDPHVEHYFMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLEKLVDVLEKTPLDLVGGAVREISGYATTYRQLLSVEPGAPGLGNCFRQKQGFHHELVGFPSCVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGFLRVGSCSDVVVDHASKVKLPWTAKDPGAETYARYRYPGSLDQSQVAKHRLLFFKHRLQCMTAE | ||||||
Glycosylation | 79 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 80 | Interchain (with C-412) | ||||
Sequence: C | ||||||
Disulfide bond | 82 | Interchain (with C-529) | ||||
Sequence: C | ||||||
Glycosylation | 179 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 274 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 412 | Interchain (with C-80) | ||||
Sequence: C | ||||||
Disulfide bond | 429↔476 | |||||
Sequence: CVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGFLRVGSC | ||||||
Disulfide bond | 529 | Interchain (with C-82) | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Most abundant in brain, liver, lung, spleen and testis.
Developmental stage
Highest at day 7 of embryonic development after which it declines to its lowest levels at day 11 before increasing again.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length533
- Mass (Da)59,212
- Last updated1995-11-01 v1
- Checksum6A15D81D2A68A28F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2P6F0 | A0A1W2P6F0_MOUSE | B4galnt1 | 192 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 73 | in Ref. 2; AAA85496 | ||||
Sequence: G → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L25885 EMBL· GenBank· DDBJ | AAA65027.1 EMBL· GenBank· DDBJ | mRNA | ||
U18975 EMBL· GenBank· DDBJ | AAA85496.1 EMBL· GenBank· DDBJ | mRNA | ||
BC036996 EMBL· GenBank· DDBJ | AAH36996.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057199 EMBL· GenBank· DDBJ | AAH57199.1 EMBL· GenBank· DDBJ | mRNA |