P40416
Gene name |
ATM1 |
Protein name |
Iron-sulfur clusters transporter ATM1, mitochondrial |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YMR301C |
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
7 variants for P40416
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s13-869542 | 29 | V>I | No | SGRP | |
| s13-869441 | 62 | K>N | No | SGRP | |
| s13-869427 | 67 | F>S | No | SGRP | |
| s13-869272 | 119 | I>V | No | SGRP | |
| s13-868855 | 258 | F>I | No | SGRP | |
| s13-868098 | 510 | K>R | No | SGRP | |
| s13-867769 | 620 | T>A | No | SGRP |
No associated diseases with P40416
5 regional properties for P40416
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 153 - 165 | IPR006089-1 |
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 366 - 385 | IPR006089-2 |
| domain | Acyl-CoA oxidase/dehydrogenase, middle domain | 151 - 246 | IPR006091 |
| domain | Acyl-CoA dehydrogenase/oxidase C-terminal | 258 - 407 | IPR009075 |
| domain | Acyl-CoA dehydrogenase/oxidase, N-terminal | 36 - 147 | IPR013786 |
3 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. |
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type transporter activity | Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATPase-coupled transmembrane transporter activity | Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source. |
6 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. |
| iron-sulfur cluster assembly | The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. |
| iron-sulfur cluster export from the mitochondrion | The directed movement of iron sulfur clusters from inside the mitochondrion into the cytosol by crossing the inner mitochondrial membrane. |
| iron-sulfur cluster transmembrane transport | A process in which an iron-sulfur cluster is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. |
| mitochondrial transmembrane transport | The process in which a solute is transported from one side of a membrane to the other into, out of or within a mitochondrion. |
| transmembrane transport | The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9NP58 | ABCB6 | ATP-binding cassette sub-family B member 6 | Homo sapiens (Human) | PR |
| Q9DC29 | Abcb6 | ATP-binding cassette sub-family B member 6 | Mus musculus (Mouse) | PR |
| O70595 | Abcb6 | ATP-binding cassette sub-family B member 6 | Rattus norvegicus (Rat) | PR |
| Q9M0G9 | ABCB24 | ABC transporter B family member 24, mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FUT3 | ABCB23 | ABC transporter B family member 23, mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LVM1 | ABCB25 | ABC transporter B family member 25, mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLLLPRCPVI | GRIVRSKFRS | GLIRNHSPVI | FTVSKLSTQR | PLLFNSAVNL | WNQAQKDITH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKSVEQFSSA | PKVKTQVKKT | SKAPTLSELK | ILKDLFRYIW | PKGNNKVRIR | VLIALGLLIS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AKILNVQVPF | FFKQTIDSMN | IAWDDPTVAL | PAAIGLTILC | YGVARFGSVL | FGELRNAVFA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KVAQNAIRTV | SLQTFQHLMK | LDLGWHLSRQ | TGGLTRAMDR | GTKGISQVLT | AMVFHIIPIS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FEISVVCGIL | TYQFGASFAA | ITFSTMLLYS | IFTIKTTAWR | THFRRDANKA | DNKAASVALD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLINFEAVKY | FNNEKYLADK | YNGSLMNYRD | SQIKVSQSLA | FLNSGQNLIF | TTALTAMMYM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GCTGVIGGNL | TVGDLVLINQ | LVFQLSVPLN | FLGSVYRDLK | QSLIDMETLF | KLRKNEVKIK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NAERPLMLPE | NVPYDITFEN | VTFGYHPDRK | ILKNASFTIP | AGWKTAIVGS | SGSGKSTILK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LVFRFYDPES | GRILINGRDI | KEYDIDALRK | VIGVVPQDTP | LFNDTIWENV | KFGRIDATDE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EVITVVEKAQ | LAPLIKKLPQ | GFDTIVGERG | LMISGGEKQR | LAIARVLLKN | ARIMFFDEAT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SALDTHTEQA | LLRTIRDNFT | SGSRTSVYIA | HRLRTIADAD | KIIVLDNGRV | REEGKHLELL |
| 670 | 680 | ||||
| AMPGSLYREL | WTIQEDLDHL | ENELKDQQEL |