Q12473
Gene name |
FRE6 (YLL051C, L0593) |
Protein name |
Ferric reductase transmembrane component 6 |
Names |
Ferric-chelate reductase 6 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YLL051C |
EC number |
1.16.1.9: With NAD(+) or NADP(+) as acceptor |
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 Q12473
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q12473-F1 | Predicted | AlphaFoldDB |
21 variants for Q12473
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s12-39311 | 54 | V>L | No | SGRP | |
| s12-39123 | 116 | E>D | No | SGRP | |
| s12-39068 | 135 | S>P | No | SGRP | |
| s12-38935 | 179 | V>A | No | SGRP | |
| s12-38564 | 303 | A>T | No | SGRP | |
| s12-38538 | 311 | L>F | No | SGRP | |
| s12-38183 | 430 | L>I | No | SGRP | |
| s12-37936 | 512 | S>N | No | SGRP | |
| s12-37883 | 530 | L>V | No | SGRP | |
| s12-37833 | 546 | H>Q | No | SGRP | |
| s12-37819 | 551 | D>G | No | SGRP | |
| s12-37712 | 587 | A>T | No | SGRP | |
| s12-37649 | 608 | R>G | No | SGRP | |
| s12-37622 | 617 | L>I | No | SGRP | |
| s12-37610 | 621 | T>A | No | SGRP | |
| s12-37551 | 640 | M>I | No | SGRP | |
| s12-37529 | 648 | H>Y | No | SGRP | |
| s12-37508 | 655 | N>D | No | SGRP | |
| s12-37447 | 675 | V>A | No | SGRP | |
| s12-37448 | 675 | V>I | No | SGRP | |
| s12-37448 | 675 | V>L | No | SGRP |
No associated diseases with Q12473
5 regional properties for Q12473
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Actinin-type actin-binding domain, conserved site | 213 - 237 | IPR001589 |
| domain | Calponin homology domain | 124 - 241 | IPR001715-1 |
| domain | Calponin homology domain | 269 - 372 | IPR001715-2 |
| domain | Calponin homology domain | 393 - 499 | IPR001715-3 |
| domain | Calponin homology domain | 514 - 622 | IPR001715-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.16.1.9 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 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 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 |
|---|---|
| ferric-chelate reductase (NADPH) activity | Catalysis of the reaction: 2 Fe3+-siderophore + NADP(+) + H(+) -> 2 Fe2+-siderophore + NADPH. |
| ferric-chelate reductase activity | Catalysis of the reaction: 2 Fe3+-siderophore + electron donor -> 2 Fe3+-siderophore + electron acceptor. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| copper ion import | The directed movement of copper ions into a cell or organelle. |
| intracellular sequestering of iron ion | The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system. |
| iron ion transport | The directed movement of iron (Fe) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHRTLLFLTW | LISLTKAFNI | KLPHTEKKDH | LESNAVLACA | SYINTLKWSF | DSSVVPGFYS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TICSYSPAFD | TWSLCIFNSL | TDQIIPMDNT | SFEESLGNVR | KTCSFVDKKF | SNISLEQYYS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLNNASSHAL | EDYGSIESLS | TSIRVDRETR | SRWIRAFHAH | AYNLDISSVY | GAYLTYYFVI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VGIIAVFFHM | SHYNGLNRAL | FASRFVNYIR | GHFVLPTFLV | DKHANHFKFL | NVEVFTGLMP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NSLEAWIIFG | YTLANIIFLS | ISYIIDPYNL | IFNSHLSQFT | RLLADRSGIL | AFTQFPLIII |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FTARNSFLEF | LTGVKFNSFI | SFHKWIGRIM | VLNATIHSLS | YSLFAIINHA | FKISNKQLYW |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KFGIASITVL | CVLLVLSLGI | VRKRHYEFFL | YTHIILALLF | FYCCWQHVKI | FNGWKEWIVV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLLIWGLEKL | FRIWNILQFR | FPKATLINLN | TSNNPHDEMF | KVIIPKYNRR | WHSKPGQYCF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IYFLHPLVFW | QCHPFTIIDE | GEKCVLVIKP | KSGLTRFIYN | HILQSLNGKL | QLRVAIEGPY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GPSNLHLDKF | DHLLLLSGGT | GLPGPLDHAI | KLSRNPDKPK | SIDLIMAIKN | PSFLNGYKSE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ILELKNSRSH | VNVQVYLTQK | TAVTKAANAR | DQLIHFDDIM | TELTSFAHIG | NARPNFSNVI |
| 670 | 680 | 690 | 700 | 710 | |
| ENAIKSTPPG | DSLAVVCCGP | PVLVDDVRNT | VSQKLLGYPE | RIIEYFEEYQ | CW |