P18091
SS
Gene name |
Actn (fliA, l(1)2Cb, CG4376) |
Protein name |
Alpha-actinin, sarcomeric |
Names |
F-actin cross-linking protein |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG4376 |
EC number |
|
Protein Class |
|
Descriptions
ACTN2 is a major F-actin cross-linking protein in both muscle and non-muscle cells and a major multivalent platform mediating interactions with many cytoskeletal or regulatory proteins. An interaction between the C-terminal region of ACTN2 and the Z-repeat motifs of Titin protein targets ACTN2 to the Z-disk. Full-length ACTN2 does not bind Z-repeats. ACTN2 has a region that acts as a pseudo-Z-repeat between the actin-binding domain (ABD) and the spectrin-like repeats (R1), and this region prevents ACTN2 from binding to the Z-repeat of Titin protein. This autoinhibition is relieved upon binding of the Z-disk lipid phosphatidylinositol-bisphosphate to the ABD of ACTN2.
Autoinhibitory domains (AIDs)
Target domain |
772-924 (EF-hand domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P18091
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P18091-F1 | Predicted | AlphaFoldDB |
No variants for P18091
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P18091 | |||||
No associated diseases with P18091
3 regional properties for P18091
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PDZ domain | 656 - 743 | IPR001478-1 |
| domain | PDZ domain | 747 - 823 | IPR001478-2 |
| domain | PTB/PI domain | 456 - 643 | IPR006020 |
6 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 projection | A prolongation or process extending from a cell, e.g. a flagellum or axon. |
| cortical actin cytoskeleton | The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| Z disc | Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| calcium ion binding | Binding to a calcium ion (Ca2+). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 cytoskeletal structures comprising actin filaments and their associated proteins. |
| actin filament bundle assembly | The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness. |
| muscle cell development | The process whose specific outcome is the progression of a muscle cell over time, from its formation to the mature structure. Muscle cell development does not include the steps involved in committing an unspecified cell to the muscle cell fate. |
| sarcomere organization | The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
17 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A5D7D1 | ACTN4 | Alpha-actinin-4 | Bos taurus (Bovine) | SS |
| Q0III9 | ACTN3 | Alpha-actinin-3 | Bos taurus (Bovine) | SS |
| Q3B7N2 | ACTN1 | Alpha-actinin-1 | Bos taurus (Bovine) | SS |
| Q3ZC55 | ACTN2 | Alpha-actinin-2 | Bos taurus (Bovine) | SS |
| P20111 | ACTN2 | Alpha-actinin-2 | Gallus gallus (Chicken) | SS |
| Q90734 | ACTN4 | Alpha-actinin-4 | Gallus gallus (Chicken) | SS |
| P05094 | ACTN1 | Alpha-actinin-1 | Gallus gallus (Chicken) | SS |
| O43707 | ACTN4 | Alpha-actinin-4 | Homo sapiens (Human) | SS |
| P12814 | ACTN1 | Alpha-actinin-1 | Homo sapiens (Human) | SS |
| P35609 | ACTN2 | Alpha-actinin-2 | Homo sapiens (Human) | EV |
| Q08043 | ACTN3 | Alpha-actinin-3 | Homo sapiens (Human) | SS |
| O88990 | Actn3 | Alpha-actinin-3 | Mus musculus (Mouse) | SS |
| P57780 | Actn4 | Alpha-actinin-4 | Mus musculus (Mouse) | SS |
| Q7TPR4 | Actn1 | Alpha-actinin-1 | Mus musculus (Mouse) | SS |
| Q9JI91 | Actn2 | Alpha-actinin-2 | Mus musculus (Mouse) | SS |
| Q9QXQ0 | Actn4 | Alpha-actinin-4 | Rattus norvegicus (Rat) | SS |
| Q9Z1P2 | Actn1 | Alpha-actinin-1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMMENGLSME | YGDGYMEQEE | EWEREGLLDP | AWEKQQKKTF | TAWCNSHLRK | AGTAIDNIEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DFRNGLKLML | LLEVISGETL | PKPDRGKMRF | HKIANVNKAL | DFIASKGVHL | VSIGAEEIVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GNLKMTLGMI | WTIILRFAIQ | DISVEEMTAK | EGLLLWCQRK | TAPYKNVNVQ | NFHLSFKDGL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AFCALIHRHR | PDLIDYAKLS | KDNPLENLNT | AFDVAEKYLD | IPRMLDPDDL | INTPKPDERA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IMTYVSCYYH | AFQGAQQVGN | NTALPDERAV | MTYVSSYYHC | FSGAQKAETA | ANRICKVLKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NQENERLMEE | YERLASDLLE | WIRRTMPWLN | SRQADNSLAG | VQKKLEEYRT | YRRKHKPPRV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EQKAKLETNF | NTLQTKLRLS | NRPAYLPTEG | KTVSDISNSW | KGLELAEKAF | EEWLLAETMR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LERLEHLAQK | FKHKADAHED | WTRGKEEMLQ | SQDFRQCKLN | ELKALKKKHE | AFESDLAAHQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DRVEQIAAIA | QELNTLEYHD | CVSVNARCQR | ICDQWDRLGA | LTQRRRTALD | EAERILEKID |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ILHLEFAKRA | APFNNWLDGT | REDLVDMFIV | HTMEEIQGLI | QAHDQFKATL | GEADKEFNLI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VNLVREVESI | VKQHQIPGGL | ENPYTTLTAN | DMTRKWSDVR | QLVPQRDQTL | ANELRKQQNN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EMLRRQFAEK | ANIVGPWIER | QMDAVTAIGM | GLQGSLEDQL | HRLKEYEQAV | YAYKPNIEEL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EKIHQAVQES | MIFENRYTNY | TMETLRVGWE | QLLTSINRNI | NEVENQILTR | DSKGISQEQL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| NEFRSSFNHF | DKNRTGRLSP | EEFKSCLVSL | GYSIGKDRQG | DLDFQRILAV | VDPNNTGYVH |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FDAFLDFMTR | ESTDTDTAEQ | VIDSFRILAA | DKPYILPDEL | RRELPPDQAE | YCIQRMPPYK |
| 910 | 920 | ||||
| GPNGVPGALD | YMSFSTALYG | ETDL |