O35094
Gene name |
Timm44 (Mimt44, Tim44) |
Protein name |
Mitochondrial import inner membrane translocase subunit TIM44 |
Names |
|
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:29635 |
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 O35094
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O35094-F1 | Predicted | AlphaFoldDB |
No variants for O35094
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O35094 | |||||
No associated diseases with O35094
1 regional properties for O35094
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tim44-like domain | 297 - 446 | IPR007379 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cardiac muscle cell differentiation | The process in which a cardiac muscle precursor cell acquires specialized features of a cardiac muscle cell. Cardiac muscle cells are striated muscle cells that are responsible for heart contraction. |
| intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
| protein import into mitochondrial matrix | The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together. |
| response to 3,3',5-triiodo-L-thyronine | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a 3,3',5-triiodo-L-thyronine stimulus. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O35857 | Timm44 | Mitochondrial import inner membrane translocase subunit TIM44 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAAALRGGW | CRCPRRCLGS | GIQFLSSHNL | PRGGSSYQIS | RPGGELTLTK | SYSSGSRKGF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSGLLDNIKQ | ELAQNKEMKE | SIKKFRDEAK | KLEESDALQE | ARRKYKTIES | ETVRTSEAIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KKLGELTGTV | KESLDEVSKS | DLGRKIKEGV | EEAARTAKQS | AESVSKGGEK | LGKTAAFKAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SQGVESVKKE | IDESVLGHTG | TYRRPERLRK | RTEFAGAKFK | ESKVFEANEE | ALGVVLHKDS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KWYQQWKDFK | DNNVVFNRFF | EMKMKYDESD | NVLIRASRAL | TDKVTDLLGG | LFSKTEMSEV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTEILRVDPT | FDKDRFLHQC | ETDIIPNILE | AMISGELDIL | KDWCYEATYN | QLAHSIQQAK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ALGLQFHSRI | LDISNVDLAM | GKMMEQGPVL | IVTFQAQLVM | VIKNPKGEVF | DGDPDKVLRM |
| 430 | 440 | 450 | |||
| LYVWALCRDQ | EELNPYAAWR | LLDISASSTE | QIL |