O19071
Gene name |
MGAT2 (GNT2) |
Protein name |
Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase |
Names |
Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, GNT-II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II |
Species |
Sus scrofa (Pig) |
KEGG Pathway |
ssc:100151745 |
EC number |
2.4.1.143: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O19071
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O19071-F1 | Predicted | AlphaFoldDB |
No variants for O19071
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O19071 | |||||
No associated diseases with O19071
No regional properties for O19071
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for O19071 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.143 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| Golgi stack | The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity | Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| oligosaccharide biosynthetic process | The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. |
| protein N-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. |
| protein N-linked glycosylation via asparagine | The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q10469 | MGAT2 | Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Homo sapiens (Human) | PR |
| Q921V5 | Mgat2 | Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Mus musculus (Mouse) | PR |
| Q09326 | Mgat2 | Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRFRIYKRKV | LILTFVVAAC | GFVLWSSNGR | QRKNEALAPP | LLDAEPVRGA | GARAGDHPAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SVGIRRGSND | SAAPLVAAAP | QPEVDNLTLR | YRSLVYQLNF | DQTLRNVDKV | SSWVPRELVL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VVQVHNRAEY | LKLLLDSLRK | AQGIDNVLVI | FSHDFWSTEI | NQLIAGVDFC | PVLQVFFPFS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IQLYPNEFPG | TDPRDCPRDL | EKNAALKMGC | INAEYPDSFG | HYREAKFSQT | KHHWWWKLHF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VWERVKVLRD | YAGLILFLEE | DHYVAPDFYH | VFKKMWNLKQ | QECPECDVLS | LGTYTTVRSF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RDVADKVDVK | TWKSTEHNMG | LALTRDAYQK | LIECTDTFCT | YDDYNWDWTL | QYLTVSCLPK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FWKVLVPQVP | RIFHAGDCGM | HHKKTCRPST | QSAQIESLLN | SNKQYMFPET | LTISEKLTAA |
| 430 | 440 | ||||
| LSPPRKNGGW | GDIRDHELCK | SYRRLQ |