Q59X23
Gene name |
PMT4 |
Protein name |
Dolichyl-phosphate-mannose--protein mannosyltransferase 4 |
Names |
Protein mannosyltransferase 4 |
Species |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
KEGG Pathway |
cal:CAALFM_C206100WA |
EC number |
2.4.1.109: 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 Q59X23
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q59X23-F1 | Predicted | AlphaFoldDB |
No variants for Q59X23
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q59X23 | |||||
No associated diseases with Q59X23
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.109 | 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 |
|---|---|
| dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex | A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p. |
| 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). |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| dolichyl-phosphate-mannose-protein mannosyltransferase activity | Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. |
| identical protein binding | Binding to an identical protein or proteins. |
| mannosyltransferase activity | Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall mannoprotein biosynthetic process | The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. |
| cellular response to neutral pH | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution. |
| filamentous growth | The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape. |
| filamentous growth of a population of unicellular organisms | The process in which a group of unicellular organisms grow in a threadlike, filamentous shape. |
| filamentous growth of a population of unicellular organisms in response to neutral pH | The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a neutral pH (pH close to 7) stimulus. |
| fungal-type cell wall organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
| negative regulation of proteolysis | Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein. |
| protein O-linked mannosylation | The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage. |
| regulation of endoplasmic reticulum unfolded protein response | Any process that modulates the frequency, rate or extent of endoplasmic reticulum unfolded protein response. |
| single-species biofilm formation on inanimate substrate | A process in which microorganisms of the same species attach to and grow on an inanimate surface such as a rock or pipe, and produce extracellular polymers that facilitate attachment and matrix formation, resulting in an alteration in the phenotype of the organisms with respect to growth rate and gene transcription. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQTLKKRGG | NSSGRKSPTT | SNIEFDDKKT | EFDLNAIVPP | KEPEYKYLAA | LTLVTLLAIY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TRFTKLGTPN | KVVFDEVHFG | KFASYYLERT | YFFDLHPPFA | KLLIAFVGWL | IGYDGKFKFE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AIGDSYIENN | VPYIAYRSLS | AIQGAAIVPI | MFLTMKTLGF | SVAACLFSSI | IVCFDNAQVT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSRLILLDAT | LILSVALTIF | SYSKFSTFRK | QSFSSKWWTW | LLATGVSLSC | VISTKYVGVF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TYLTIGIAVI | HELWILLDYR | KGLTLQEFAK | HFFARLWALI | IVPFCIYLYW | FYLHFAILTR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SGPGDAFMSS | EFQETLLESP | LAAHSKPVQY | FDQITIKHKD | TGAFLHSHQH | EYPLRYEDGR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ISSNGQQVTC | VVQENAANDP | NNQWEIVPTS | EGANKGTKVY | TNDIVRFRHV | GTGGYLLTHD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VASPLKPTNE | EFTVVYDDVA | QQRYNETLFR | LRLHVPGSNP | KKEKNKKEIK | TLATDLRILH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VDTVVAMWTH | NDELLPEWAF | NQQEVSGNKK | IPDKDNIWNF | DLITNLQSTD | PRNQYVPKKV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KTLPFLRKWW | ELQMLMFHHN | NQLSSEHPFA | TQPGEWPLAL | SGVSFYNDNT | EKKQIFFIGN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IIGFWLEVCF | LSIYIGILLA | DQITRRRNVH | VLSDRARSRL | YNTLGFLFVG | WAAHYLPFFL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| MNRQKFLHHY | LPAHLVAALF | SGGLVEFICS | NNSARPNGKP | VGVNKYKIIA | VVAACSTAII |
| 730 | 740 | 750 | |||
| WFFFYFRPLT | YGDVYLTPEE | VKARQWLDIK | LHYGK |