Q7S4Z3
Gene name |
gim-1 (gpi14, NCU06057) |
Protein name |
GPI mannosyltransferase 1 |
Names |
GPI mannosyltransferase I, GPI-MT-I, Glycosylphosphatidylinositol-anchor biosynthesis protein 14 |
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU06057 |
EC number |
|
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 Q7S4Z3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7S4Z3-F1 | Predicted | AlphaFoldDB |
No variants for Q7S4Z3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7S4Z3 | |||||
No associated diseases with Q7S4Z3
No regional properties for Q7S4Z3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q7S4Z3 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| glycosylphosphatidylinositol-mannosyltransferase I complex | A protein complex that is involved in the transfer of the four mannoses in the GPI-anchor precursor. In yeast S. cerevisiae this complex consists of Pbn1p and Gpi14p and in rat this complex consists of PIG-X and PIG-M. |
| 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-1,4-mannosyltransferase activity | Catalysis of the transfer of a mannose residue to an oligosaccharide, forming an alpha-(1->4) linkage. |
| glycolipid mannosyltransferase activity | Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-D-mannosyl-D-mannose linkage. |
| mannosyltransferase activity | Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| GPI anchor biosynthetic process | The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATTSPAAPR | PKSKSSSLLS | TLFSRPLPLY | VSAFLLRIVL | LLYGLWQDAN | SPLKYTDIDY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LVFTDAARFV | SRGESPYARE | TYRYTPILAW | LLLPTTWTAG | AQWGPWAAKV | INVAWFSFGK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLFAAADLVA | GWLIEQVLVM | GKDFPSSAAK | GKEKDTEKTK | EGGKKGPSVT | ASTGMDPSRA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RAFAAIWLLN | PMVATISTRG | SSEGLLGVLV | MALLWAVLSR | RITLAGLLLG | FSVHFKIYPF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IYAPAIVWWM | DQERLSGVRA | GGGGGGGGQK | KTSSSFRKTL | TRFLTLPRLL | LAFTSLATFL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLNFLMYRLY | GHPFLQETYL | HHVTRIDHRH | NFSPYNTQLY | LSSASVSPSH | SAAEPKFKIE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SLAFLPQLVL | STILIPLTLA | KKDLPTSLLA | QTFAFVTFNK | VCTSQYFLWY | LVLLPLYLPR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SSFWTSKRMG | LVALGLWVLG | QALWLQQAYE | LEFLGRSTFL | PGLWMASLGF | FVVNCWILGV |
| IVGDGGR |