Q61542
PR
Gene name |
Stard3 |
Protein name |
StAR-related lipid transfer protein 3 |
Names |
Protein ES 64, Protein MLN 64, START domain-containing protein 3, StARD3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:59045 |
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 Q61542
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q61542-F1 | Predicted | AlphaFoldDB |
16 variants for Q61542
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389194031 | 11 | D>V | No | EVA | |
| rs27071069 | 18 | A>G | No | EVA | |
| rs264104258 | 35 | H>Y | No | EVA | |
| rs3389213432 | 85 | Q>E | No | EVA | |
| rs3389198899 | 144 | E>K | No | EVA | |
| rs3389208871 | 149 | G>W | No | EVA | |
| rs3389159912 | 170 | L>H | No | EVA | |
| rs3389168386 | 195 | G>E | No | EVA | |
| rs3389208882 | 248 | A>E | No | EVA | |
| rs3389194036 | 303 | L>P | No | EVA | |
| rs3389133885 | 368 | T>S | No | EVA | |
| rs3389198943 | 373 | K>* | No | EVA | |
| rs3389168419 | 390 | I>T | No | EVA | |
| rs261226992 | 399 | R>Q | No | EVA | |
| rs3389168414 | 423 | S>R | No | EVA | |
| rs3389206902 | 441 | E>K | No | EVA |
No associated diseases with Q61542
Functions
11 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| endoplasmic reticulum-endosome membrane contact site | A contact site between the endoplasmic reticulum membrane and the endosome membrane. |
| endosome | A vacuole to which materials ingested by endocytosis are delivered. |
| 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. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| late endosome | A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center. |
| late endosome membrane | The lipid bilayer surrounding a late endosome. |
| 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. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| organelle membrane contact site | A zone of apposition between the membranes of an organelle with another membrane, either another membrane of the same organelle, a membrane of another organelle, or the plasma membrane. Membrane contact sites (MCSs) are structured by bridging complexes. They are specialized for communication, including the efficient traffic of small molecules such as Ca2+ ions and lipids, as well as enzyme-substrate interactions. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| cholesterol binding | Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. |
| cholesterol transfer activity | Removes cholesterol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cholesterol transport | The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| progesterone biosynthetic process | The chemical reactions and pathways resulting in the formation of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants. |
| vesicle tethering to endoplasmic reticulum | The initial, indirect interaction between a transport vesicle membrane and the membrane of the endoplasmic reticulum. This interaction is mediated by tethering factors (or complexes), which interact with both membranes. Interaction can occur via direct binding to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior fusion. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O95772 | STARD3NL | STARD3 N-terminal-like protein | Homo sapiens (Human) | PR |
| Q14849 | STARD3 | StAR-related lipid transfer protein 3 | Homo sapiens (Human) | PR |
| Q9DCI3 | Stard3nl | STARD3 N-terminal-like protein | Mus musculus (Mouse) | PR |
| O17883 | strl-1 | Steroidogenic acute regulatory-like protein 1 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKRPGDLAC | DLERSLPALA | SLGTSLSHSQ | SLSSHFIPPP | LEKRRAISDV | RRTFCLFVTF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLLFISLLWI | IELNTNTGIR | KNLEQEVIHY | SFQSSFFDIF | VLAFFRFSGL | LLGYAVLRLQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HWWVIAVTTL | VSSAFLIVKV | ILSELLSKGA | FGYLLPIVSF | VLAWLETWFL | DFKVLPQEAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EERWYLAAQA | AVARGPLLFS | GALSEGQFYS | PPESFAGSDN | ESDEEVTGKK | SFSAQEREYI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RQGKEATAVV | DQILAQEENW | KFERSNEYGD | TVYTIEVPFH | GKTFILKTFL | PCPAELVYQE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VILQPERMVL | WNKTVTACQI | LQRVEDNTLV | SYDVSSGAAG | GVVSPRDFVN | VRRIERRRDR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLSSGIATTH | CSKPPTHKYV | RGENGPGGFI | VLKSANNPRV | CTFVWILNTD | LKGRLPRYLI |
| 430 | 440 | ||||
| HQSLGATMFE | FAFHLRQRVG | ELGARA |