P12847
PR
Gene name |
Myh3 |
Protein name |
Myosin-3 |
Names |
Myosin heavy chain 3 , Myosin heavy chain, fast skeletal muscle, embryonic |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
rno:24583 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
80-780 (Myosin head, motor domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P12847
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P12847-F1 | Predicted | AlphaFoldDB |
No variants for P12847
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P12847 | |||||
No associated diseases with P12847
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| contractile fiber | Fibers, composed of actin, myosin, and associated proteins, found in cells of smooth or striated muscle. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| myofibril | The contractile element of skeletal and cardiac muscle; a long, highly organized bundle of actin, myosin, and other proteins that contracts by a sliding filament mechanism. |
| myosin complex | A protein complex, formed of one or more myosin heavy chains plus associated light chains and other proteins, that functions as a molecular motor; uses the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments; has magnesium-ATPase activity and binds actin. Myosin classes are distinguished based on sequence features of the motor, or head, domain, but also have distinct tail regions that are believed to bind specific cargoes. |
| myosin filament | A supramolecular fiber containing myosin heavy chains, plus associated light chains and other proteins, in which the myosin heavy chains are arranged into a filament. |
| myosin II complex | A myosin complex containing two class II myosin heavy chains, two myosin essential light chains and two myosin regulatory light chains. Also known as classical myosin or conventional myosin, the myosin II class includes the major muscle myosin of vertebrate and invertebrate muscle, and is characterized by alpha-helical coiled coil tails that self assemble to form a variety of filament structures. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| microfilament motor activity | A motor activity that generates movement along a microfilament, driven by ATP hydrolysis. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| ATP metabolic process | The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator. |
| muscle contraction | A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. |
| skeletal muscle contraction | A process in which force is generated within skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. In the skeletal muscle, the muscle contraction takes advantage of an ordered sarcomeric structure and in most cases it is under voluntary control. |
46 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9BE40 | MYH1 | Myosin-1 | Bos taurus (Bovine) | SS |
| Q9BE41 | MYH2 | Myosin-2 | Bos taurus (Bovine) | SS |
| Q27991 | MYH10 | Myosin-10 | Bos taurus (Bovine) | SS |
| Q9BE39 | MYH7 | Myosin-7 | Bos taurus (Bovine) | SS |
| P10587 | MYH11 | Myosin-11 | Gallus gallus (Chicken) | SS |
| P14105 | MYH9 | Myosin-9 | Gallus gallus (Chicken) | SS |
| P02565 | MYH1B | Myosin-1B | Gallus gallus (Chicken) | SS |
| P13538 | Myosin heavy chain, skeletal muscle, adult | Gallus gallus (Chicken) | SS | |
| Q99323 | zip | Myosin heavy chain, non-muscle | Drosophila melanogaster (Fruit fly) | SS |
| P05661 | Mhc | Myosin heavy chain, muscle | Drosophila melanogaster (Fruit fly) | SS |
| P35579 | MYH9 | Myosin-9 | Homo sapiens (Human) | SS |
| P12882 | MYH1 | Myosin-1 | Homo sapiens (Human) | SS |
| Q9UKX2 | MYH2 | Myosin-2 | Homo sapiens (Human) | SS |
| Q9Y623 | MYH4 | Myosin-4 | Homo sapiens (Human) | SS |
| A7E2Y1 | MYH7B | Myosin-7B | Homo sapiens (Human) | SS |
| Q9Y2K3 | MYH15 | Myosin-15 | Homo sapiens (Human) | SS |
| P12883 | MYH7 | Myosin-7 | Homo sapiens (Human) | EV |
| P35580 | MYH10 | Myosin-10 | Homo sapiens (Human) | SS |
| P35749 | MYH11 | Myosin-11 | Homo sapiens (Human) | SS |
| P13535 | MYH8 | Myosin-8 | Homo sapiens (Human) | SS |
| P13533 | MYH6 | Myosin-6 | Homo sapiens (Human) | SS |
| Q9UKX3 | MYH13 | Myosin-13 | Homo sapiens (Human) | SS |
| Q7Z406 | MYH14 | Myosin-14 | Homo sapiens (Human) | SS |
| P11055 | MYH3 | Myosin-3 | Homo sapiens (Human) | SS |
| Q8VDD5 | Myh9 | Myosin-9 | Mus musculus (Mouse) | SS |
| Q5SX39 | Myh4 | Myosin-4 | Mus musculus (Mouse) | SS |
| P13542 | Myh8 | Myosin-8 | Mus musculus (Mouse) | SS |
| Q02566 | Myh6 | Myosin-6 | Mus musculus (Mouse) | SS |
| O08638 | Myh11 | Myosin-11 | Mus musculus (Mouse) | SS |
| A2AQP0 | Myh7b | Myosin-7B | Mus musculus (Mouse) | SS |
| Q61879 | Myh10 | Myosin-10 | Mus musculus (Mouse) | SS |
| Q91Z83 | Myh7 | Myosin-7 | Mus musculus (Mouse) | SS |
| Q6URW6 | Myh14 | Myosin-14 | Mus musculus (Mouse) | SS |
| Q5SX40 | Myh1 | Myosin-1 | Mus musculus (Mouse) | SS |
| P13541 | Myh3 | Myosin-3 | Mus musculus (Mouse) | SS |
| P79293 | MYH7 | Myosin-7 | Sus scrofa (Pig) | SS |
| Q9TV63 | MYH2 | Myosin-2 | Sus scrofa (Pig) | SS |
| Q29RW1 | Myh4 | Myosin-4 | Rattus norvegicus (Rat) | SS |
| P02564 | Myh7 | Myosin-7 | Rattus norvegicus (Rat) | SS |
| Q9JLT0 | Myh10 | Myosin-10 | Rattus norvegicus (Rat) | SS |
| P02563 | Myh6 | Myosin-6 | Rattus norvegicus (Rat) | SS |
| Q62812 | Myh9 | Myosin-9 | Rattus norvegicus (Rat) | SS |
| P02567 | myo-1 | Myosin-1 | Caenorhabditis elegans | SS |
| P02566 | unc-54 | Myosin-4 | Caenorhabditis elegans | SS |
| P12845 | myo-2 | Myosin-2 | Caenorhabditis elegans | SS |
| P12844 | myo-3 | Myosin-3 | Caenorhabditis elegans | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEEQDLSEV | ELSPVGSEEP | RCLSPGSAPS | LGPDGGGGGS | GLRASPGPGE | LGKVKKEQQD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GEADDDKFPV | CIREAVSQVL | SGYDWTLVPM | PVRVNGASKS | KPHVKRPMNA | FMVWAQAARR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLADQYPHLH | NAELSKTLGK | LWRLLNESDK | RPFIEEAERL | RMQHKKDHPD | YKYQPRRRKN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GKAAQGEAEC | PGGEAEQGGA | AAIQAHYKSA | HLDHRHPEEG | SPMSDGNPEH | PSGQSHGPPT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PPTTPKTELQ | SGKADPKRDG | RSLGEGGKPH | IDFGNVDIGE | ISHEVMSNME | TFDVTELDQY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPPNGHPGHV | GSYSAAGYGL | GSALAVASGH | SAWISKPPGV | ALPTVSPPGV | DAKAQVKTET |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TGPQGPPHYT | DQPSTSQIAY | TSLSLPHYGS | AFPSISRPQF | DYSDHQPSGP | YYGHAGQASG |
| 430 | 440 | 450 | 460 | ||
| LYSAFSYMGP | SQRPLYTAIS | DPSPSGPQSH | SPTHWEQPVY | TTLSRP |