P11048 · LMNA_XENLA

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).

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentintermediate filament
Cellular Componentnuclear envelope
Cellular Componentnuclear lamina
Cellular Componentnuclear matrix
Cellular Componentnucleoplasm
Molecular Functionstructural constituent of cytoskeleton
Biological Processheterochromatin formation
Biological Processnuclear envelope organization
Biological Processnuclear migration
Biological Processnuclear pore localization
Biological Processprotein localization to nuclear envelope

Names & Taxonomy

Protein names

  • Recommended name
    Lamin-A

Gene names

    • Name
      lmna

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    P11048

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for modified residue, chain, lipidation, propeptide.

Type
IDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00000638151-662Lamin-A
Modified residue18Phosphoserine
Modified residue388Phosphoserine
Modified residue662Cysteine methyl ester
Lipidation662S-farnesyl cysteine
PropeptidePRO_0000403466663-665Removed 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

Expression

Gene expression databases

    • 373673Expressed in stomach and 16 other cell types or tissues

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
IDPosition(s)Description
Region1-29Head
Domain27-383IF rod
Region30-66Coil 1A
Region67-76Linker 1
Region77-214Coil 1B
Region215-238Linker 2
Region239-383Coil 2
Region381-441Disordered
Region384-664Tail
Compositional bias388-410Polar residues
Compositional bias411-425Basic and acidic residues
Motif413-418Nuclear localization signal
Domain425-542LTD
Region550-581Disordered
Region602-641Disordered
Compositional bias603-641Polar residues

Sequence similarities

Belongs to the intermediate filament family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    665
  • Mass (Da)
    74,919
  • Last updated
    1989-07-01 v1
  • Checksum
    9FA64F2F1AF99293
METPGQKRATRSTHTPLSPTRITRLQEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVISREVTGIKSAYETELADARKTLDSVAKERARLQLELSKIREEHKELKARNAKKESDLLTAQARLKDLEALLNSKDAALTTALGEKRNLENEIRELKAHIAKLEASLADTKKQLQDEMLRRVDTENRNQTLKEELEFQKSIYNEEMRETKRRHETRLVEVDNGRQREFESKLADALHELRAQHEGQIGLYKEELGKTYNAKLENAKQSAERNSSLVGEAQEEIQQSRIRIDSLSAQLSQLQKQLAAREAKLRDLEDAYARERDSSRRLLADKDREMAEMRARMQQQLDEYQELLDIKLALDMEINAYRKLLEGEEERLRLSPSPNTQKRSARTIASHSGAHISSSASKRRRLEEGESRSSSFTQHARTTGKVSVEEVDPEGKYVRLRNKSNEDQSLGNWQIKRQIGDETPIVYKFPPRLTLKAGQTVTIWASGAGATNSPPSDLVWKAQSSWGTGDSIRTALLTSSNEEVAMRKLVRTVVINDEDDEDNDDMEHHHHHHHHHHDGQNSSGDPGEYNLRSRTIVCTSCGRPAEKSVLASQGSGLVTGSSGSSSSSVTLTRTYRSTGGTSGGSGLGESPVTRNFIVGNGQRAQVAPQNCSIM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias388-410Polar residues
Compositional bias411-425Basic and acidic residues
Compositional bias603-641Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X06345
EMBL· GenBank· DDBJ
CAA29652.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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