Q08929
Gene name |
GUP2 (YPL189W) |
Protein name |
Membrane-bound O-acyltransferase GUP2 |
Names |
Glycerol uptake protein 2 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YPL189W |
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 Q08929
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q08929-F1 | Predicted | AlphaFoldDB |
13 variants for Q08929
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s16-189162 | 4 | L>V | No | SGRP | |
| s16-189265 | 38 | N>S | No | SGRP | |
| s16-189303 | 51 | V>I | No | SGRP | |
| s16-189313 | 54 | T>I | No | SGRP | |
| s16-189499 | 116 | L>P | No | SGRP | |
| s16-189525 | 125 | P>A | No | SGRP | |
| s16-189708 | 186 | A>T | No | SGRP | |
| s16-190366 | 405 | Q>L | No | SGRP | |
| s16-190509 | 453 | V>M | No | SGRP | |
| s16-190726 | 525 | R>I | No | SGRP | |
| s16-190806 | 552 | V>L | No | SGRP | |
| s16-190867 | 572 | N>S | No | SGRP | |
| s16-190893 | 581 | A>T | No | SGRP |
No associated diseases with Q08929
No regional properties for Q08929
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q08929 | |||
4 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 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyltransferase activity | Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). |
| O-acyltransferase activity | Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule. |
| symporter activity | Enables the active transport of a solute across a membrane by a mechanism whereby two or more species are transported together in the same direction in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glycerol transmembrane transport | The directed movement of glycerol across a membrane. Glycerol is 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids. |
| 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. |
2 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSMLRIWSCI | VHFFSVQALD | SRIKPDIEFK | RRQRIFINSS | KEENGSSSSA | VTVTRNPVLS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SNSPSPPLWN | TWEFRLYYLA | FTVVVPFMIK | AALATSSESN | PNYYKFSGLL | AHGWILGRKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DNSDPQYRFF | RSNFFLLAIL | ILLQIILKKV | FVKFSKIPKT | KFDFACGLVF | VCFMYGINSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLFTHAFIFF | TLAHSLKRKR | LIAAFAIWSY | GIFTLFINQK | MKNLPFNNIA | IILSPMDQWY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KGIVPRWDFF | FNFTLLRLLS | YSMDFLERWH | EQLSRQPSID | YDDRRPEFRK | SLSGSTLQTI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YESGKNVLEE | KERLVAEHHI | QDYNFINFIA | YITYAPLFLV | GPIITFNDYL | YQSENKLPSL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TKKNIGFYAL | KVFSSLLLME | IILHYIYVGA | IARTKAWNND | TPLQQAMIAL | FNLNIMYLKL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LIPWRLFRLW | AMVDGIDAPE | NMLRCVDNNY | STVGFWRAWH | TSFNKWVIRY | IYVPFGGSNN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KILTSFAVFS | FVAIWHDIQL | RVLFWGWLTV | LLLLGETYIT | NCFSRYRFRS | WYRFVCGIGA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AINICMMMII | NVYGFCLGAE | GTKLLLKGIF | NNSHSPEFLT | AVMVSLFIAV | QVMFEIREEE |
| KRHGINLKC |