Q9Z1P2
Gene name |
Actn1 |
Protein name |
Alpha-actinin-1 |
Names |
Alpha-actinin cytoskeletal isoform , F-actin cross-linking protein , Non-muscle alpha-actinin-1 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:81634 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
740-892 (EF-hand domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for Q9Z1P2
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q9Z1P2-F1 | Predicted | AlphaFoldDB |
No variants for Q9Z1P2
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q9Z1P2 |
No associated diseases with Q9Z1P2
13 regional properties for Q9Z1P2
Type | Name | Position | InterPro Accession |
---|---|---|---|
conserved_site | Actinin-type actin-binding domain, conserved site | 33 - 42 | IPR001589-1 |
conserved_site | Actinin-type actin-binding domain, conserved site | 107 - 131 | IPR001589-2 |
domain | Calponin homology domain | 31 - 135 | IPR001715-1 |
domain | Calponin homology domain | 144 - 250 | IPR001715-2 |
repeat | Spectrin repeat | 275 - 383 | IPR002017-1 |
repeat | Spectrin repeat | 394 - 498 | IPR002017-2 |
repeat | Spectrin repeat | 510 - 620 | IPR002017-3 |
repeat | Spectrin repeat | 632 - 732 | IPR002017-4 |
domain | EF-hand domain | 746 - 822 | IPR002048 |
domain | EF-hand, Ca insensitive | 822 - 888 | IPR014837 |
repeat | Spectrin/alpha-actinin | 277 - 622 | IPR018159-1 |
repeat | Spectrin/alpha-actinin | 633 - 732 | IPR018159-2 |
binding_site | EF-Hand 1, calcium-binding site | 759 - 771 | IPR018247 |
Functions
17 GO annotations of cellular component
Name | Definition |
---|---|
brush border | The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell. |
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. |
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. |
cortical actin cytoskeleton | The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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. |
dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
fascia adherens | A cell-cell junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighbouring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes. |
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). |
glutamatergic synapse | A synapse that uses glutamate as a neurotransmitter. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
sarcomere | 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. |
stress fiber | A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber. |
Z disc | Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
11 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. |
calcium ion binding | Binding to a calcium ion (Ca2+). |
cytoskeletal regulatory protein binding | Binding to a protein involved in modulating the reorganization of the cytoskeleton. |
double-stranded RNA binding | Binding to double-stranded RNA. |
integrin binding | Binding to an integrin. |
nuclear receptor coactivator activity | A transcription coactivator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound nuclear receptor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
protein domain specific binding | Binding to a specific domain of a protein. |
protein homodimerization activity | Binding to an identical protein to form a homodimer. |
structural constituent of postsynapse | The action of a molecule that contributes to the structural integrity of a postsynapse. |
transmembrane transporter binding | Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other. |
vinculin binding | Binding to vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane. |
8 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. |
actin filament network formation | The assembly of a network of actin filaments; actin filaments on different axes and with differing orientations are crosslinked together to form a mesh of filaments. |
actin filament 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. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
focal adhesion assembly | The aggregation and bonding together of a set of components to form a focal adhesion, a complex of intracellular signaling and structural proteins that provides a structural link between the internal actin cytoskeleton and the ECM, and also function as a locus of signal transduction activity. |
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. |
platelet formation | The process in which platelets bud from long processes extended by megakaryocytes. |
platelet morphogenesis | Generation and organization of a platelet, a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. |
18 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q3ZC55 | ACTN2 | Alpha-actinin-2 | Bos taurus (Bovine) | SS |
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 |
Q90734 | ACTN4 | Alpha-actinin-4 | Gallus gallus (Chicken) | SS |
P20111 | ACTN2 | Alpha-actinin-2 | Gallus gallus (Chicken) | SS |
P05094 | ACTN1 | Alpha-actinin-1 | Gallus gallus (Chicken) | SS |
P18091 | Actn | Alpha-actinin, sarcomeric | Drosophila melanogaster (Fruit fly) | SS |
O43707 | ACTN4 | Alpha-actinin-4 | Homo sapiens (Human) | SS |
Q08043 | ACTN3 | Alpha-actinin-3 | Homo sapiens (Human) | SS |
P35609 | ACTN2 | Alpha-actinin-2 | Homo sapiens (Human) | EV |
P12814 | ACTN1 | Alpha-actinin-1 | Homo sapiens (Human) | SS |
O88990 | Actn3 | Alpha-actinin-3 | Mus musculus (Mouse) | SS |
P57780 | Actn4 | Alpha-actinin-4 | Mus musculus (Mouse) | SS |
Q9JI91 | Actn2 | Alpha-actinin-2 | Mus musculus (Mouse) | SS |
Q7TPR4 | Actn1 | Alpha-actinin-1 | Mus musculus (Mouse) | SS |
Q9QXQ0 | Actn4 | Alpha-actinin-4 | Rattus norvegicus (Rat) | SS |
Q9QWN8 | Sptbn2 | Spectrin beta chain, non-erythrocytic 2 | Rattus norvegicus (Rat) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MDHYDSQQTN | DYMQPEEDWD | RDLLLDPAWE | KQQRKTFTAW | CNSHLRKAGT | QIENIEEDFR |
70 | 80 | 90 | 100 | 110 | 120 |
DGLKLMLLLE | VISGERLAKP | ERGKMRVHKI | SNVNKALDFI | ASKGVKLVSI | GAEEIVDGNV |
130 | 140 | 150 | 160 | 170 | 180 |
KMTLGMIWTI | ILRFAIQDIS | VEETSAKEGL | LLWCQRKTAP | YKNVNIQNFH | ISWKDGLGFC |
190 | 200 | 210 | 220 | 230 | 240 |
ALIHRHRPEL | IDYGKLRKDD | PLTNLNTAFD | VAERYLDIPK | MLDAEDIVGT | ARPDEKAIMT |
250 | 260 | 270 | 280 | 290 | 300 |
YVSSFYHAFS | GAQKAETAAN | RICKVLAVNQ | ENEQLMEDYE | KLASDLLEWI | RRTIPWLENR |
310 | 320 | 330 | 340 | 350 | 360 |
VPENTMQAMQ | QKLEDFRDYR | RLHKPPKVQE | KCQLEINFNT | LQTKLRLSNR | PAFMPSEGRM |
370 | 380 | 390 | 400 | 410 | 420 |
VSDINNAWGC | LEQAEKGYEE | WLLNEIRRLE | RLDHLAEKFR | QKASIHEAWT | DGKEAMLRQK |
430 | 440 | 450 | 460 | 470 | 480 |
DYETATLSEI | KALLKKHEAF | ESDLAAHQDR | VEQIAAIAQE | LNELDYYDSP | SVNARCQKIC |
490 | 500 | 510 | 520 | 530 | 540 |
DQWDNLGALT | QKRREALERT | EKLLETIDQL | YLEYAKRAAP | FNNWMEGAME | DLQDTFIVHT |
550 | 560 | 570 | 580 | 590 | 600 |
IEEIQGLTTA | HEQFKATLPD | ADKERLAILG | IHNEVSKIVQ | TYHVNMAGTN | PYTTITPQEI |
610 | 620 | 630 | 640 | 650 | 660 |
NGKWDHVRQL | VPRRDQALTE | EHSRQQHNER | LRKQFGAQAN | VIGPWIQTKM | EEIGRISIEM |
670 | 680 | 690 | 700 | 710 | 720 |
HGTLEDQLSH | LRQYEKSIVN | YKPKIDQLEG | DHQLIQEALI | FDNKHTNYTM | EHIRVGWEQL |
730 | 740 | 750 | 760 | 770 | 780 |
LTTIARTINE | VENQILTRDA | KGISQEQMNE | FRASFNHFDR | DHSGTLGPEE | FKACLISLGY |
790 | 800 | 810 | 820 | 830 | 840 |
DIGNDPQGEA | EFARIMSIVD | PNRLGVVTFQ | AFIDFMSRET | ADTDTADQVM | ASFKILAGDK |
850 | 860 | 870 | 880 | 890 | |
NYITGDELRR | ELPPDQAEYC | IARMAPYAGP | DSVPGALDYM | SFSTALYGES | DL |