Q12333
Gene name |
FRE7 (YOL152W, AOB629) |
Protein name |
Ferric/cupric reductase transmembrane component 7 |
Names |
Ferric-chelate reductase 7 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YOL152W |
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 Q12333
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q12333-F1 | Predicted | AlphaFoldDB |
28 variants for Q12333
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s15-40847 | 34 | A>V | No | SGRP | |
| s15-41026 | 94 | T>A | No | SGRP | |
| s15-41254 | 170 | P>S | No | SGRP | |
| s15-41377 | 211 | H>Y | No | SGRP | |
| s15-41410 | 222 | E>K | No | SGRP | |
| s15-41787 | 347 | E>D | No | SGRP | |
| s15-41837 | 364 | G>D | No | SGRP | |
| s15-41837 | 364 | G>V | No | SGRP | |
| s15-41875 | 377 | A>T | No | SGRP | |
| s15-41956 | 404 | M>V | No | SGRP | |
| s15-41966 | 407 | I>T | No | SGRP | |
| s15-41969 | 408 | L>H | No | SGRP | |
| s15-41992 | 416 | I>V | No | SGRP | |
| s15-42008 | 421 | R>K | No | SGRP | |
| s15-42091 | 449 | L>F | No | SGRP | |
| s15-42111 | 455 | E>D | No | SGRP | |
| s15-42164 | 473 | R>K | No | SGRP | |
| s15-42174 | 476 | M>I | No | SGRP | |
| s15-42218 | 491 | K>T | No | SGRP | |
| s15-42239 | 498 | V>A | No | SGRP | |
| s15-42266 | 507 | I>T | No | SGRP | |
| s15-42277 | 511 | F>L | No | SGRP | |
| s15-42289 | 515 | I>L | No | SGRP | |
| s15-42290 | 515 | I>T | No | SGRP | |
| s15-42289 | 515 | I>V | No | SGRP | |
| s15-42333 | 529 | K>N | No | SGRP | |
| s15-42371 | 542 | S>L | No | SGRP | |
| s15-42535 | 597 | G>S | No | SGRP |
No associated diseases with Q12333
4 regional properties for Q12333
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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| copper ion import | The directed movement of copper ions into a cell or organelle. |
| 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. |
| reductive iron assimilation | A process in which iron is solubilized by reduction from Fe3+ to Fe2+ via a cell surface reductase and subsequent transport of the iron across the membrane by iron uptake proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIEERDLVLS | NGIHCIADIH | SELYARLKKE | SQAATPWVYQ | KQYGKFVTYF | VAVIIFLSLI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKLAFMYYDS | SEEFLPEKKN | SPTTPSVFLA | RIMTKLVAFN | RYICYRKFPT | LIFSYLGIPT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SVGTFLVVMA | TTLYTLLYCF | VPHPFYRPCA | GFGSPPLSVR | AGIMAISLVP | FVFSLSGKIN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VIGWLVGLSY | EKINIYHQWA | SILCLFFSWV | HVIPFLRQAR | HEGGYERMHQ | RWKASDMWRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVPPILFLNL | LWLSSLPIAR | RHFYEIFLQL | HWILAVGFYI | SLFYHVYPEL | NSHMYLVATI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VVWFAQLFYR | LAVKGYLRPG | RSFMASTIAN | VSIVGEGCVE | LIVKDVEMAY | SPGQHIFVRT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IDKGIISNHP | FSIFPSAKYP | GGIKMLIRAQ | KGFSKRLYES | NDDMKKILID | GPYGGIERDI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RSFTNVYLIC | SGSGISTCLP | FLQKYGPILH | KTNLEVITLD | WVVRHREDIS | WIRDEMCTLS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NNLRQLFLDG | KIVVRIYVCS | DSTVPGIIKT | FPQTIDTASD | QSDLAKREKD | TEFGQDDTES |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NSTFDKSNNE | YKGLITIIPS | KPDLNQVIND | YQIGFRNCFI | CSGSDSLRYT | VGNSVAGLQA |
| 610 | |||||
| KVFSNKNVEE | CYLHSESFGY |