Q5REP8
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 |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100190826 |
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 Q5REP8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5REP8-F1 | Predicted | AlphaFoldDB |
No variants for Q5REP8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5REP8 | |||||
No associated diseases with Q5REP8
No regional properties for Q5REP8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5REP8 | |||
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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| metal ion binding | Binding to a metal ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
3 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRLRNGTVAT | ALAFITSFLT | LSWYTTWQNG | KEKLIAYQRE | FLALKERLRI | AEHRISQRSS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELNTIVQQFK | RVGAETNGSK | DALNKFSDNT | LKLLKELTSK | KSLQVPSIYY | HLPHLLKNEG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLQPAVQIGN | GRTGVSIVMG | IPTVKREVKS | YLIETLHSLI | DNLYPEEKLD | CVIVVFIGET |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DIDYVHGVVA | NLEKEFSKEI | SSGLVEVISP | PESYYPDLTN | LKETFGDSKE | RVRWRTKQNL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYCFLMMYAQ | EKGIYYIQLE | DDIIVKQNYF | NTIKNFALQL | SSEEWMILEF | SQLGFIGKMF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QAPDLTLIVE | FIFMFYKEKP | IDWLLDHILW | VKVCNPEKDA | KHCDRQKANL | RIHFRPSLFQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HVGLHSSLSG | KIQKLTDKDY | MKPLLLKIHV | NPPAEVSTSL | KVYQGHTLEK | TYMGEDFFWA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ITPIAGDYIL | FKFDKPVNVE | SYLFHSGNQE | HPGDILLNTT | VEVLPFKSEG | LEISKETKDK |
| 490 | 500 | 510 | 520 | 530 | |
| RLEDGYFRIG | KFENGVAEGM | VDPSLNPISA | FRLSVIQNSA | VWAILNEIHI | KKATN |