Q08834 · MGT5A_RAT
- ProteinAlpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- GeneMgat5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids740 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:7615638, PubMed:8340368).
Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (By similarity).
Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration (PubMed:7615638).
MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity).
Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity).
Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (By similarity).
Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration (PubMed:7615638).
MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity).
Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity).
Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix.
Catalytic activity
- N4-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H+ + N4-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane | |
Molecular Function | acetylglucosaminyltransferase activity | |
Molecular Function | alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | protein phosphatase inhibitor activity | |
Biological Process | positive regulation of cell migration | |
Biological Process | positive regulation of receptor signaling pathway via STAT | |
Biological Process | protein N-linked glycosylation | |
Biological Process | protein N-linked glycosylation via asparagine |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ08834
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-13 | Cytoplasmic | ||||
Sequence: MAFFSPWKLSSQK | ||||||
Transmembrane | 14-30 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LGFFLVTFGFIWGMMLL | ||||||
Topological domain | 31-740 | Lumenal | ||||
Sequence: HFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVNGTGANSTNSTTAVPSLVSLEKINVADIINGVQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYGMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080524 | 1-740 | Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A | |||
Sequence: MAFFSPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVNGTGANSTNSTTAVPSLVSLEKINVADIINGVQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYGMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL | ||||||
Chain | PRO_0000445694 | 31-740 | Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A | |||
Sequence: HFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVNGTGANSTNSTTAVPSLVSLEKINVADIINGVQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYGMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 114 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 117 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 144↔182 | |||||
Sequence: CVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSC | ||||||
Disulfide bond | 155↔195 | |||||
Sequence: CEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWC | ||||||
Disulfide bond | 171↔337 | |||||
Sequence: CYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYGMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGC | ||||||
Glycosylation | 333 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 371↔625 | |||||
Sequence: CMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFC | ||||||
Glycosylation | 432 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 446 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 648↔723 | |||||
Sequence: CKQVCQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRIC | ||||||
Disulfide bond | 652↔725 | |||||
Sequence: CQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRICPC | ||||||
Disulfide bond | 659↔712 | |||||
Sequence: CEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSC | ||||||
Disulfide bond | 680↔701 | |||||
Sequence: CQSSELYKDILVPSFYPKSKHC | ||||||
Disulfide bond | 736↔739 | |||||
Sequence: CKDC |
Post-translational modification
N-glycosylated.
A secreted form is released from the membrane after cleavage by gamma-secretase.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in kidney (at protein level). Detected in kidney.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 212-740 | Sufficient for catalytic activity | ||||
Sequence: NSLAEIRTDFNILYGMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLICEPSFFQHLNKEKDLLKYKVICQSSELYKDILVPSFYPKSKHCVFQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL |
Sequence similarities
Belongs to the glycosyltransferase 18 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length740
- Mass (Da)84,562
- Last updated1995-02-01 v1
- ChecksumC0BD7F820FEA959C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5Y5S9 | A0A8I5Y5S9_RAT | Mgat5 | 741 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14284 EMBL· GenBank· DDBJ | AAA41665.1 EMBL· GenBank· DDBJ | mRNA |