Q9Z1P2 · ACTN1_RAT
- ProteinAlpha-actinin-1
- GeneActn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids892 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-actinin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9Z1P2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000073433 | 1-892 | Alpha-actinin-1 | |||
Sequence: MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHSRQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITGDELRRELPPDQAEYCIARMAPYAGPDSVPGALDYMSFSTALYGESDL | ||||||
Modified residue | 6 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 12 | Phosphotyrosine; by FAK1 | ||||
Sequence: Y | ||||||
Modified residue | 95 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 195 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 471 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 676 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 677 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 890 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP (By similarity).
Interacts with DDN (PubMed:16464232).
Interacts with PSD. Interacts with MICALL2 (By similarity).
Interacts with DNM2 and CTTN (PubMed:21210813).
Interacts with PDLIM1 (PubMed:22659164).
Interacts with PDLIM2 (PubMed:15505042).
Interacts with PDLIM4 (via PDZ domain) (PubMed:14729062).
Interacts with IGSF8 (By similarity).
Interacts with DDN (PubMed:16464232).
Interacts with PSD. Interacts with MICALL2 (By similarity).
Interacts with DNM2 and CTTN (PubMed:21210813).
Interacts with PDLIM1 (PubMed:22659164).
Interacts with PDLIM2 (PubMed:15505042).
Interacts with PDLIM4 (via PDZ domain) (PubMed:14729062).
Interacts with IGSF8 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-247 | Actin-binding | ||||
Sequence: MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYH | ||||||
Domain | 31-135 | Calponin-homology (CH) 1 | ||||
Sequence: KQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFA | ||||||
Domain | 144-250 | Calponin-homology (CH) 2 | ||||
Sequence: TSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFS | ||||||
Repeat | 274-384 | Spectrin 1 | ||||
Sequence: QLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLN | ||||||
Region | 274-733 | Interaction with DDN | ||||
Sequence: QLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHSRQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVEN | ||||||
Repeat | 394-499 | Spectrin 2 | ||||
Sequence: HLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALER | ||||||
Repeat | 509-620 | Spectrin 3 | ||||
Sequence: QLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTE | ||||||
Repeat | 630-733 | Spectrin 4 | ||||
Sequence: RLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVEN | ||||||
Domain | 746-781 | EF-hand 1 | ||||
Sequence: EQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYD | ||||||
Domain | 787-822 | EF-hand 2 | ||||
Sequence: QGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETAD |
Sequence similarities
Belongs to the alpha-actinin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length892
- Mass (Da)102,960
- Last updated1999-05-01 v1
- Checksum2360D496D0A84095
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AV34 | A0A8I6AV34_RAT | Actn1 | 890 | ||
Q6GMN8 | Q6GMN8_RAT | Actn1 | 887 | ||
A0A8I6GDI3 | A0A8I6GDI3_RAT | Actn1 | 859 | ||
A0A8I6A472 | A0A8I6A472_RAT | Actn1 | 907 | ||
Q6T487 | Q6T487_RAT | Actn1 | 914 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF115386 EMBL· GenBank· DDBJ | AAD12064.1 EMBL· GenBank· DDBJ | mRNA |