Q9WV92
PR
Gene name |
Epb41l3 |
Protein name |
Band 4.1-like protein 3 |
Names |
CD9 partner 1, CD9P-1, Glu-Trp-Ile EWI motif-containing protein F, EWI-F, Prostaglandin F2-alpha receptor regulatory protein, Prostaglandin F2-alpha receptor-associated protein, 4.1B, Differentially expressed in adenocarcinoma of the lung protein 1, DAL-1, DAL1P, mDAL-1, Erythrocyte membrane protein band 4.1-like 3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13823 |
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 Q9WV92
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9WV92-F1 | Predicted | AlphaFoldDB |
45 variants for Q9WV92
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389479201 | 4 | E>* | No | EVA | |
| rs3389479201 | 4 | E>K | No | EVA | |
| rs3389444530 | 39 | G>C | No | EVA | |
| rs237081847 | 43 | S>G | No | EVA | |
| rs220110851 | 44 | L>R | No | EVA | |
| rs248208469 | 44 | L>V | No | EVA | |
| rs237743810 | 45 | N>K | No | EVA | |
| rs51524782 | 52 | A>T | No | EVA | |
| rs108654408 | 60 | A>P | No | EVA | |
| rs220182187 | 86 | E>D | No | EVA | |
| rs3389425764 | 99 | S>L | No | EVA | |
| rs3389477513 | 137 | R>H | No | EVA | |
| rs3389489624 | 204 | L>I | No | EVA | |
| rs3389457031 | 207 | D>N | No | EVA | |
| rs3412897965 | 221 | I>S | No | EVA | |
| rs3389485022 | 225 | R>W | No | EVA | |
| rs3389470352 | 234 | A>G | No | EVA | |
| rs3389478469 | 269 | K>T | No | EVA | |
| rs3413135167 | 274 | K>T | No | EVA | |
| rs3389477522 | 292 | M>I | No | EVA | |
| rs1133826107 | 362 | G>* | No | EVA | |
| rs3389470363 | 410 | L>M | No | EVA | |
| rs3389472535 | 457 | V>L | No | EVA | |
| rs3389470048 | 487 | Q>H | No | EVA | |
| rs3389425774 | 520 | V>L | No | EVA | |
| rs3389478406 | 584 | T>I | No | EVA | |
| rs3389479469 | 591 | T>I | No | EVA | |
| rs3389479382 | 611 | D>V | No | EVA | |
| rs244519404 | 695 | I>V | No | EVA | |
| rs3389481428 | 702 | V>M | No | EVA | |
| rs3389444538 | 703 | M>K | No | EVA | |
| rs3389478498 | 716 | R>M | No | EVA | |
| rs222190681 | 719 | V>A | No | EVA | |
| rs3389494296 | 726 | P>S | No | EVA | |
| rs261306874 | 732 | T>S | No | EVA | |
| rs227988381 | 773 | A>V | No | EVA | |
| rs45817405 | 775 | T>A | No | EVA | |
| rs3389470047 | 777 | R>C | No | EVA | |
| rs3389489469 | 797 | S>T | No | EVA | |
| rs3389478481 | 802 | S>N | No | EVA | |
| rs50471218 | 803 | I>V | No | EVA | |
| rs3389472588 | 846 | M>L | No | EVA | |
| rs3389444500 | 885 | G>R | No | EVA | |
| rs3389457291 | 911 | V>A | No | EVA | |
| rs3389481423 | 916 | V>L | No | EVA |
No associated diseases with Q9WV92
7 regional properties for Q9WV92
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Signal transduction response regulator, receiver domain | 612 - 730 | IPR001789 |
| domain | GAF domain | 157 - 315 | IPR003018 |
| domain | Histidine kinase/HSP90-like ATPase | 453 - 585 | IPR003594 |
| domain | Signal transduction histidine kinase, dimerisation/phosphoacceptor domain | 340 - 406 | IPR003661 |
| domain | Signal transduction histidine kinase-related protein, C-terminal | 509 - 523 | IPR004358-1 |
| domain | Signal transduction histidine kinase-related protein, C-terminal | 544 - 562 | IPR004358-2 |
| domain | Histidine kinase domain | 348 - 585 | IPR005467 |
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell junction | A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella. |
| cell-cell junction | A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| juxtaparanode region of axon | A region of an axon near a node of Ranvier that is between the paranode and internode regions. |
| paranode region of axon | An axon part that is located adjacent to the nodes of Ranvier and surrounded by lateral loop portions of myelin sheath. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| postsynaptic density | An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| cytoskeletal protein-membrane anchor activity | The binding activity of a molecule that brings together a cytoskeletal protein or protein complex and a plasma membrane lipid or membrane-associated protein, in order to maintain the localization of the cytoskeleton at a specific cortical membrane location. |
| structural constituent of cytoskeleton | The action of a molecule that contributes to the structural integrity of a cytoskeletal structure. |
14 GO annotations of biological process
| Name | Definition |
|---|---|
| actomyosin structure organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments. |
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| axon development | The progression of an axon over time. Covers axonogenesis (de novo generation of an axon) and axon regeneration (regrowth), as well as processes pertaining to the progression of the axon over time (fasciculation and defasciculation). |
| cortical actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
| cortical cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
| myelin maintenance | The process of preserving the structure and function of mature myelin. This includes maintaining the compact structure of myelin necessary for its electrical insulating characteristics as well as the structure of non-compact regions such as Schmidt-Lantermann clefts and paranodal loops. This does not include processes responsible for maintaining the nodes of Ranvier, which are not part of the myelin sheath. |
| neuron projection morphogenesis | The process in which the anatomical structures of a neuron projection are generated and organized. A neuron projection is any process extending from a neural cell, such as axons or dendrites. |
| paranodal junction assembly | Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier. |
| paranodal junction maintenance | The maintenance of a paranodal junction, a highly specialized cell-cell junction found in vertebrates, which forms between a neuron and a glial cell, and has structural similarity to Drosophila septate junctions. A paranodal junction flanks the node of Ranvier in myelinated nerve, electrically isolates the myelinated from unmyelinated nerve segments, and physically separates the voltage-gated sodium channels at the node from the cluster of potassium channels underneath the myelin sheath. |
| protein localization to juxtaparanode region of axon | Any process in which a protein is transported to, or maintained at, the juxtaparanode region of an axon. |
| protein localization to paranode region of axon | A cellular protein localization process in which a protein is transported to, or maintained at, the paranode region of an axon. |
| protein localization to plasma membrane | A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane. |
| regulation of cell growth | Any process that modulates the frequency, rate, extent or direction of cell growth. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9N179 | EPB41 | Protein 4.1 | Bos taurus (Bovine) | PR |
| O43491 | EPB41L2 | Band 4.1-like protein 2 | Homo sapiens (Human) | PR |
| P11171 | EPB41 | Protein 4.1 | Homo sapiens (Human) | PR |
| Q9H4G0 | EPB41L1 | Band 4.1-like protein 1 | Homo sapiens (Human) | PR |
| Q9Y2J2 | EPB41L3 | Band 4.1-like protein 3 | Homo sapiens (Human) | PR |
| Q8BGS1 | Epb41l5 | Band 4.1-like protein 5 | Mus musculus (Mouse) | PR |
| P52963 | Epb41l4a | Band 4.1-like protein 4A | Mus musculus (Mouse) | PR |
| Q6P5H6 | Frmd5 | FERM domain-containing protein 5 | Mus musculus (Mouse) | PR |
| Q8BHD4 | Frmd3 | FERM domain-containing protein 3 | Mus musculus (Mouse) | PR |
| O70318 | Epb41l2 | Band 4.1-like protein 2 | Mus musculus (Mouse) | PR |
| Q9Z2H5 | Epb41l1 | Band 4.1-like protein 1 | Mus musculus (Mouse) | PR |
| P48193 | Epb41 | Protein 4.1 | Mus musculus (Mouse) | PR |
| Q9WTP0 | Epb41l1 | Band 4.1-like protein 1 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTESGSDSE | SKPDQEAEPQ | EAAGPQGQAG | AQPGPEPAGG | NGSLNGEKQQ | PALEQFPEAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHSTPVKREI | GDKDRDFAAA | AAKQLEYQQF | EDDKLSQRSS | SSKLSRSPLK | IVKRPKSMQC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KVTLLDGSEY | GCDVDKRSRG | QVLFDKVCEH | LNLLEKDYFG | LTYRDAENQK | NWLDPAKEIK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KQIRSGAWHF | SFNVKFYPPD | PAQLSEDITR | YYLCLQLRDD | IVSGRLPCSF | VTLALLGSYT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VQSELGDYDP | DECGNDYISE | FRFAPNHTKE | LEDKVIELHK | SHRGMTPAEA | EMHFLENAKK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSMYGVDLHH | AKDSEGVEIM | LGVCASGLLI | YRDRLRINRF | AWPKVLKISY | KRNNFYIKIR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PGEFEQFEST | IGFKLPNHRA | AKRLWKVCVE | HHTFFRLLLP | EAPPKKFLTL | GSKFRYSGRT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QAQTRRASAL | IDRPAPYFER | SSSKRYTMSR | SLDGASVSEN | HEIYMKDSVS | AAEVGTGQYA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TTKGISQTNL | ITTVTPEKKA | EEERVEEEDR | RKKAEEATPV | TALRHEGKTD | SERTDTAADG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ETSATESDQE | EDAEIKAQDL | DKTQDELMKH | QTNISELKRT | FLETSTETAL | TNEWEKRLST |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SPVRLAARQE | DAPMIEPLVP | EETKQSSGEK | LMDGSEILSL | LESARKPTEF | IGGVSSTTQS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| WVQKLETKTE | PVEAEVESTP | HPQPLSTEKV | LQETILVEER | HVMSVHASGD | ASHTARDEVD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AAESTPTDRR | HTGKGKEGSS | VTEAAKEQRG | EEVDQSAPEQ | EQPATVSHEE | EQASTIRTSE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GLEQKSHFES | STVRVESTSV | GSISPGGAKL | EISTKEVPVV | HTETKTITYE | SSQVDPGADL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EPGVLMSAQT | ITSETTSTTT | TTHITKTVKG | GISETRIEKR | IVITGDADID | HDQALAQAIK |
| 910 | 920 | ||||
| EAKEQHPDMS | VTKVVVHKET | EITPEDGED |