Q09752
Gene name |
fnx1 (SPBC12C2.13c, SPBC21D10.04c) |
Protein name |
Multidrug resistance protein fnx1 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC12C2.13c |
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 Q09752
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q09752-F1 | Predicted | AlphaFoldDB |
No variants for Q09752
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q09752 | |||||
No associated diseases with Q09752
1 regional properties for Q09752
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Major facilitator superfamily domain | 33 - 524 | IPR020846 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
| fungal-type vacuole membrane | The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae. |
| integral component of fungal-type vacuolar membrane | The component of the fungal-type vacuole membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| basic amino acid transmembrane transporter activity | Enables the transfer of basic amino acids from one side of a membrane to the other. Basic amino acids have side chains with a positive charge at pH 7.3. |
| L-asparagine transmembrane transporter activity | Enables the transfer of L-asparagine from one side of a membrane to the other. L-asparagine is the L-enantiomer of alpha-aminosuccinamic acid. |
| L-isoleucine transmembrane transporter activity | Enables the transfer of L-isoleucine from one side of a membrane to the other. L-isoleucine is (2R*,3R*)-2-amino-3-methylpentanoic acid. |
| L-lysine transmembrane transporter activity | Enables the transfer of L-lysine from one side of a membrane to the other. L-lysine is 2,6-diaminohexanoic acid. |
| transmembrane transporter activity | Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| asparagine transmembrane import into vacuole | The directed movement of asparagine into the vacuole across the vacuolar membrane. |
| basic amino acid transport | The directed movement of basic amino acids, amino acids with a pH above 7, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| isoleucine transmembrane transport | The directed movement of isoleucine across a membrane. |
| L-lysine import into vacuole involved in cellular response to nitrogen starvation | A L-lysine import into the vacuole that is involved in cellular response to nitrogen starvation. |
| transmembrane transport | The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVDQVNLATE | QTSLLYPEVS | RKKEELSVNK | WTILPALWVG | GFLSALDMTI | VASLYPVIGS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EFKLMNNASY | IVTAYLITNT | AFQPLYGRLS | DIFGRRPTVV | FANAAFTLGT | FWCGISRSLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ELCMARALAG | IGGGGLGTMS | SIISSDIVSL | RERGTWQGIT | NIVWGIGGSL | GGPLGGLIAQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RWGWRTAFHF | QVPMGILSTI | LVAWRVRVKP | TVRNSNASLL | SRIDYLGSFL | LVTGITALVV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TFNMGGDAFP | WVSPVIITLL | VSSVLILFAF | YWVEKNIAVE | PIAPVEILSQ | PTPLNVCLGN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FFNAFCSFVI | VYELPLFFET | TLLMPSSEAG | VRIFPYVIST | SVGSLCSGLY | MKKTGRYRNL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VIAGFFFMLM | GIVSFAVLTS | FGHRTPLILI | SLCLAMTGCS | YGMNLTSTLI | AIISSLAPEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QAVATGLSYL | FRATGSVIGI | SLSQTTTLSI | LMKQLASNLK | DDPDKDDLIR | RLRESISIIP |
| 490 | 500 | 510 | 520 | 530 | |
| NLPKDIQKLV | IKSYATAFTW | TFALVAIIAF | AGFWCSLRIK | QFYLHTSVDR | S |