P31382
Gene name |
PMT2 |
Protein name |
Dolichyl-phosphate-mannose--protein mannosyltransferase 2 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YAL023C |
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
5 structures for P31382
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6P25 | EM | 320 A | B | 1-759 | PDB |
| 6P28 | X-ray | 135 A | A | 337-532 | PDB |
| 6P2R | EM | 320 A | B | 1-759 | PDB |
| 6ZQP | X-ray | 160 A | A | 339-533 | PDB |
| AF-P31382-F1 | Predicted | AlphaFoldDB |
4 variants for P31382
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s01-108458 | 32 | S>N | No | SGRP | |
| s01-108392 | 54 | A>V | No | SGRP | |
| s01-107246 | 436 | V>G | No | SGRP | |
| s01-107088 | 489 | G>S | No | SGRP |
No associated diseases with P31382
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 | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex | A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt2p. |
| dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex | A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt2p. |
| 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 membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| 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. |
1 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. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| ER-associated misfolded protein catabolic process | The chemical reactions and pathways resulting in the breakdown of misfolded proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation. |
| fungal-type cell wall biogenesis | A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin. |
| protein exit from endoplasmic reticulum | The directed movement of proteins from the endoplasmic reticulum. |
| protein O-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan. |
| 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. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P47190 | PMT3 | Dolichyl-phosphate-mannose--protein mannosyltransferase 3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P46971 | PMT4 | Dolichyl-phosphate-mannose--protein mannosyltransferase 4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q9UKY4 | POMT2 | Protein O-mannosyl-transferase 2 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSSSSTGYS | KNNAAHIKQE | NTLRQRESSS | ISVSEELSSA | DERDAEDFSK | EKPAAQSSLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RLESVVMPVI | FTALALFTRM | YKIGINNHVV | WDEAHFGKFG | SYYLRHEFYH | DVHPPLGKML |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VGLSGYLAGY | NGSWDFPSGE | IYPDYLDYVK | MRLFNASFSA | LCVPLAYFTA | KAIGFSLPTV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WLMTVLVLFE | NSYSTLGRFI | LLDSMLLFFT | VASFFSFVMF | HNQRSKPFSR | KWWKWLLITG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ISLGCTISVK | MVGLFIITMV | GIYTVIDLWT | FLADKSMSWK | TYINHWLARI | FGLIIVPFCI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FLLCFKIHFD | LLSHSGTGDA | NMPSLFQARL | VGSDVGQGPR | DIALGSSVVS | IKNQALGGSL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LHSHIQTYPD | GSNQQQVTCY | GYKDANNEWF | FNRERGLPSW | SENETDIEYL | KPGTSYRLVH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KSTGRNLHTH | PVAAPVSKTQ | WEVSGYGDNV | VGDNKDNWVI | EIMDQRGDED | PEKLHTLTTS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FRIKNLEMGC | YLAQTGNSLP | EWGFRQQEVV | CMKNPFKRDK | RTWWNIETHE | NERLPPRPED |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FQYPKTNFLK | DFIHLNLAMM | ATNNALVPDP | DKFDYLASSA | WQWPTLNVGL | RLCGWGDDNP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KYFLLGTPAS | TWASSVAVLA | FMATVVILLI | RWQRQYVDLR | NPSNWNVFLM | GGFYPLLAWG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LHYMPFVIMS | RVTYVHHYLP | ALYFALIILA | YCFDAGLQKW | SRSKCGRIMR | FVLYAGFMAL |
| 730 | 740 | 750 | |||
| VIGCFWYFSP | ISFGMEGPSS | NFRYLNWFST | WDIADKQEA |