Q5M854
PR
Gene name |
Mgat4a |
Protein name |
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A |
Names |
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa, GlcNAc-T IVa, GnT-IVa, N-acetylglucosaminyltransferase IVa, UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:367252 |
EC number |
2.4.1.145: 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 Q5M854
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5M854-F1 | Predicted | AlphaFoldDB |
No variants for Q5M854
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5M854 | |||||
No associated diseases with Q5M854
No regional properties for Q5M854
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5M854 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.145 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum-Golgi intermediate compartment | A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| 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. |
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetylglucosaminyltransferase activity | Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar. |
| alanine-glyoxylate transaminase activity | Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine. |
| alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity | Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R. |
| glycosyltransferase activity | Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor). |
| metal ion binding | Binding to a metal ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| glyoxylate metabolic process | The chemical reactions and pathways involving glyoxylate, the anion of glyoxylic acid, HOC-COOH. |
| N-glycan processing | The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
| 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. |
2 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRLRNGTVAT | ALVFVTSFLT | LSWYTTWQNG | KEKLIAYQRE | FLALKERLRV | AEHRISQRSS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELNTIVQQFR | RAGAETNGNN | TIKLLKELTS | KKSLQVPSIY | YHLPHLLQNE | RSLQPAVQIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGRTGVSIVM | GIPTVKREVK | SYLIETLHSL | IDNLYPEEKL | DCVIVVFIGE | TDLDYVHSVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ANLEKEFSRE | ISSGLLEVIS | PPESYYPDLT | NLKETFGDSK | ERVRWRTKQN | LDYCFLMMYA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QEKGIYYIQL | EDDIIVKQNY | FNTIKNFALQ | LSSEEWMILE | FSQLGFIGKM | FQAPDLALVV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EFILMFYKEK | PIDWLLDHIL | WVKVCNPEKD | AKHCDRQKAN | LRIRFRPSLF | QHVGLHSSLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GKIQKLTDKD | YMKPLLLKIH | VNPPAEVSTS | LKVYQGHTLE | KTYMGEDFFW | AITPTAGDYI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LFKFDKPVNV | ESYLFHSGNQ | EHPGDILLNT | TVEVLPLKSD | SLEISKETKD | KRLEDGYFRI |
| 490 | 500 | 510 | 520 | ||
| GKFEYGVAEG | IVDPGLNPIS | AFRLSVIQNS | AVWAILNEIH | IKKVTS |