alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4E isoform X1 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PGAP4-like super family | cl04660 | Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ... |
71-295 | 4.78e-51 | |||||
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4. The actual alignment was detected with superfamily member pfam04666: Pssm-ID: 471077 Cd Length: 278 Bit Score: 174.03 E-value: 4.78e-51
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| Name | Accession | Description | Interval | E-value | |||||
| Glyco_transf_54 | pfam04666 | N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ... |
71-295 | 4.78e-51 | |||||
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein. Pssm-ID: 461384 Cd Length: 278 Bit Score: 174.03 E-value: 4.78e-51
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| PGAP4-like | cd21105 | Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ... |
49-210 | 5.91e-06 | |||||
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4. Pssm-ID: 409189 Cd Length: 364 Bit Score: 48.14 E-value: 5.91e-06
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| Name | Accession | Description | Interval | E-value | |||||
| Glyco_transf_54 | pfam04666 | N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ... |
71-295 | 4.78e-51 | |||||
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein. Pssm-ID: 461384 Cd Length: 278 Bit Score: 174.03 E-value: 4.78e-51
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| PGAP4-like | cd21105 | Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ... |
49-210 | 5.91e-06 | |||||
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4. Pssm-ID: 409189 Cd Length: 364 Bit Score: 48.14 E-value: 5.91e-06
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| PGAP4-like_fungal | cd22189 | uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ... |
73-193 | 5.12e-04 | |||||
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This subfamily contains uncharacterized fungal proteins with similarity to animal post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. Proteins from this subfamily contain the putative catalytic site of PGAP4 and may have similar activities. Pssm-ID: 409190 Cd Length: 375 Bit Score: 42.15 E-value: 5.12e-04
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