Q6DRP4 · CCM2_DANRE

Function

function

Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions. May also function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity).

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
Biological Processanterior/posterior axis specification
Biological Processcardiac jelly development
Biological Processcell-cell junction assembly
Biological Processheart contraction
Biological Processheart development
Biological Processvasculogenesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cerebral cavernous malformations protein 2 homolog
  • Alternative names
    • Malcavernin
    • Valentine

Gene names

    • Name
      ccm2
    • Synonyms
      vtn

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q6DRP4
  • Secondary accessions
    • Q0Z802
    • Q568L2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

The heart chambers in mutant animals are huge, constituted of a monolayered myocardium lined by endocardium.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis197Loss of function in heart development. Loss of HEG-binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000894231-455Cerebral cavernous malformations protein 2 homolog

Proteomic databases

Expression

Developmental stage

Expressed in the ventricular zone of the brain at 28 hours post fertilization (hpf) and, at lower levels, in the posterior cardinal vein and in the posterior intermediate inner cell mass. At 48 hpf, still detected in the vein. At 28 and 48 hpf, expressed at low levels in a region near the dorsal aorta.

Gene expression databases

Interaction

Subunit

Part of a complex with MAP2K3, MAP3K3 and RAC1. Binds RAC1 directly and independently of its nucleotide-bound state (By similarity).
Interacts with HEG1 and KRIT1; KRIT1 greatly facilitates the interaction with HEG1

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain60-247PID
Region272-299Disordered
Region292-385Harmonin homology domain
Compositional bias399-419Polar residues
Region399-432Disordered

Domain

The C-terminal region constitutes an independently folded domain that has structural similarity with the USH1C (harmonin) N-terminus, despite very low sequence similarity.

Sequence similarities

Belongs to the CCM2 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q6DRP4-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    455
  • Mass (Da)
    49,827
  • Last updated
    2004-08-16 v1
  • Checksum
    463DE4DFD566071C
MEEDVKKVKKPGIVSPFKRVFLKGEKGRDKKALEKSTERRALHTFSLSLPDHRIDPDILLNDYIEKEVKYLGQLTSVPGYLNPSSRTEVLQLIDNARKSHQLAGQLTSEQDAVVSLSAYNVKLVWRDGEDIILRVPIHDIAAVSYIRDDSLHLVVLKTAQEPGGSPCHSTEMSKSPTLSSLSESGAVLVEVCCLLVLAVDNKAAAEELCLLLSQVFQIVYTESTIDFLDRAIFDGATTPTRHLSIYSEDSSSKVDVKDVFEAEASTFSFQSSLEAGHSSSPSPTSAPASPQTKTASESELSTTAAELLQDYMTTLRTKLSSKEIQQFATLLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRYKRTTSSASDSTTNGNGAAGGSDEGTATSEGDEWDRMISDISNDIEALGSSMDQDGVPS

Q6DRP4-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict319in Ref. 3; AAH92812
Alternative sequenceVSP_015804362-455in isoform 2
Compositional bias399-419Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ677878
EMBL· GenBank· DDBJ
ABG29499.1
EMBL· GenBank· DDBJ
mRNA
AY648715
EMBL· GenBank· DDBJ
AAT68033.1
EMBL· GenBank· DDBJ
mRNA
BC092812
EMBL· GenBank· DDBJ
AAH92812.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp