Q9N4M4 · ANC1_CAEEL

  • Protein
    Nuclear anchorage protein 1
  • Gene
    anc-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a central role in nuclear and mitochondrial anchoring (PubMed:10375507, PubMed:12169658, PubMed:22298703, PubMed:6889924).
Probably connects nuclei to the cytoskeleton by interacting with unc-84 at the nuclear envelope and with F-actin in the cytoplasm, creating a bridge across the nuclear envelope between the cytoskeleton and the nucleus (PubMed:15773756).
Has a role in positioning of the cell body of the PVQ lumbar interneuron (PubMed:22298703).

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 Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentnuclear envelope
Cellular Componentnuclear outer membrane
Cellular Componentperinuclear region of cytoplasm
Molecular Functionactin binding
Molecular Functionkinesin binding
Molecular Functionprotein-folding chaperone binding
Biological Processcytoskeleton organization
Biological Processlocalization
Biological Processnuclear migration
Biological Processnucleus localization
Biological Processnucleus organization
Biological Processpronuclear migration

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Nuclear anchorage protein 1
  • Short names
    Anchorage 1 protein
  • Alternative names
    • Nesprin homolog

Gene names

    • Name
      anc-1
    • ORF names
      ZK973.6

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q9N4M4
  • Secondary accessions
    • O61841
    • O61842
    • Q6IMP3

Proteomes

Organism-specific databases

Subcellular Location

Nucleus outer membrane
; Single-pass type IV membrane protein
Note: The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, most probably the outer nuclear membrane, or with mitochondrial membrane.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-8494Cytoplasmic
Transmembrane8495-8513Helical; Anchor for type IV membrane protein
Topological domain8514-8545Perinuclear space

Keywords

Phenotypes & Variants

Disruption phenotype

Nuclear anchorage is lost resulting in free-floating nuclei that often cluster as the animal flexes. An increase in PVQ cell bodies mispositioned to the anterior is apparent between three-fold embryos and L1 larvae. Pharyngeal cells show defects including mispositioned organelles.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001635931-8545Nuclear anchorage protein 1

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitously expressed in all postembryonic cells.

Developmental stage

First expressed in L1 larvae, and thereafter throughout adulthood.

Gene expression databases

Interaction

Subunit

Interacts with F-actin via its N-terminal domain. Most likely interacts with unc-84; the interaction is probably required to recruit anc-1 to the nuclear envelope.

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain, compositional bias, coiled coil, repeat.

TypeIDPosition(s)Description
Region1-325Actin-binding
Domain23-130Calponin-homology (CH) 1
Compositional bias148-193Polar residues
Region148-197Disordered
Domain222-328Calponin-homology (CH) 2
Coiled coil754-774
Coiled coil1072-1101
Coiled coil1215-1236
Coiled coil1324-1384
Coiled coil1574-1629
Coiled coil1725-1754
Coiled coil1950-1981
Coiled coil2103-2580
Coiled coil2682-2712
Coiled coil2852-2949
Coiled coil3002-3119
Region3010-3033Disordered
Coiled coil3178-3295
Repeat3241-41431
Region3241-81996 X tandem repeat
Coiled coil3346-3417
Coiled coil3482-3552
Coiled coil3587-3703
Coiled coil3781-3839
Coiled coil3902-4022
Region3913-3936Disordered
Coiled coil4114-4198
Repeat4144-50972
Coiled coil4249-4320
Region4372-4395Disordered
Coiled coil4436-4506
Coiled coil4541-4657
Coiled coil4735-4793
Coiled coil4856-4976
Region4867-4890Disordered
Coiled coil5035-5152
Repeat5098-60003
Coiled coil5203-5274
Coiled coil5339-5409
Coiled coil5444-5560
Coiled coil5638-5696
Coiled coil5759-5879
Region5770-5793Disordered
Coiled coil5938-6055
Repeat6001-69034
Coiled coil6106-6177
Coiled coil6242-6312
Coiled coil6347-6463
Coiled coil6541-6599
Coiled coil6662-6782
Region6673-6696Disordered
Coiled coil6841-6958
Repeat6904-78065
Coiled coil7009-7080
Coiled coil7145-7215
Coiled coil7250-7366
Coiled coil7444-7502
Coiled coil7565-7685
Region7576-7599Disordered
Coiled coil7744-7861
Repeat7807-81996
Coiled coil7912-7983
Coiled coil8048-8118
Coiled coil8153-8204
Coiled coil8273-8329
Coiled coil8370-8390
Region8391-8418Disordered
Region8449-8480Disordered
Domain8486-8545KASH

Domain

The large coiled coil domains are composed of 6 nearly exact repeats of 903 residues. The last repeat is partial. These repeats are conserved in Hawaii (CB4856), Australia (AB4) and Germany (RC301) strains. The length of the repeat may be maintained because of a selective advantage to keep the protein large and allow a single molecule to extend more than 0.5 micrometers.
The KASH domain, which contains a potential transmembrane domain, is essential for the nuclear envelope targeting.

Sequence similarities

Belongs to the nesprin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    8,545
  • Mass (Da)
    956,482
  • Last updated
    2003-03-28 v3
  • Checksum
    02A94D994BEE19E3

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2C9C3A7A0A2C9C3A7_CAEELanc-18538
A0A2C9C2Z1A0A2C9C2Z1_CAEELanc-17540

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias148-193Polar residues
Sequence conflict7849in Ref. 1; DAA04553

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY157938
EMBL· GenBank· DDBJ
AAN35200.1
EMBL· GenBank· DDBJ
mRNA
BK000642
EMBL· GenBank· DDBJ
DAA04553.1
EMBL· GenBank· DDBJ
mRNA
BX284601
EMBL· GenBank· DDBJ
CCD73568.1
EMBL· GenBank· DDBJ
Genomic DNA
AY126454
EMBL· GenBank· DDBJ
AAM95163.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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