P11048 · LMNA_XENLA
- ProteinLamin-A
- Genelmna
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids665 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:3762708).
Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (By similarity).
The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (By similarity).
Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (By similarity).
The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (By similarity).
Miscellaneous
There are at least five different lamins in Xenopus: the somatic lamins L(I)/lmnb1.S, L(II)/lmnb2.L, and A/lmna.L; the oocyte germinal vesicle lamin L(III)/lmnb3.L; and the male germ cells lamin l(IV).
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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Aspect | Term | |
---|---|---|
Cellular Component | intermediate filament | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear lamina | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleoplasm | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | heterochromatin formation | |
Biological Process | nuclear envelope organization | |
Biological Process | nuclear migration | |
Biological Process | nuclear pore localization | |
Biological Process | protein localization to nuclear envelope |
Names & Taxonomy
Protein names
- Recommended nameLamin-A
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionP11048
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | |||
Chain | PRO_0000063815 | 1-662 | Lamin-A | ||
Modified residue | 18 | Phosphoserine | |||
Modified residue | 388 | Phosphoserine | |||
Modified residue | 662 | Cysteine methyl ester | |||
Lipidation | 662 | S-farnesyl cysteine | |||
Propeptide | PRO_0000403466 | 663-665 | Removed in mature form | ||
Post-translational modification
Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration. Phosphorylation by CDK1 at Ser-18 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown.
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Homodimer. Lamin dimers then assemble into dimeric head-to-tail polymers. Ultimately, two head-to-tail polymers assemble laterally into a protofilament with a uniformly shaped rod of 3.5 nm in diameter.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-29 | Head | |||
Domain | 27-383 | IF rod | |||
Region | 30-66 | Coil 1A | |||
Region | 67-76 | Linker 1 | |||
Region | 77-214 | Coil 1B | |||
Region | 215-238 | Linker 2 | |||
Region | 239-383 | Coil 2 | |||
Region | 381-441 | Disordered | |||
Region | 384-664 | Tail | |||
Compositional bias | 388-410 | Polar residues | |||
Compositional bias | 411-425 | Basic and acidic residues | |||
Motif | 413-418 | Nuclear localization signal | |||
Domain | 425-542 | LTD | |||
Region | 550-581 | Disordered | |||
Region | 602-641 | Disordered | |||
Compositional bias | 603-641 | Polar residues | |||
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length665
- Mass (Da)74,919
- Last updated1989-07-01 v1
- Checksum9FA64F2F1AF99293
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 388-410 | Polar residues | |||
Compositional bias | 411-425 | Basic and acidic residues | |||
Compositional bias | 603-641 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X06345 EMBL· GenBank· DDBJ | CAA29652.1 EMBL· GenBank· DDBJ | mRNA |