Q95KF7 · CLVS2_MACFA

Function

function

Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity).

Miscellaneous

Binding to PtdIns(3,5)P2 is not required for localization.

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 Componentclathrin-coated vesicle
Cellular Componentearly endosome membrane
Cellular Componentendosome
Cellular Componenttrans-Golgi network
Molecular Functionphosphatidylinositol-3,5-bisphosphate binding
Biological Processlysosome organization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Clavesin-2
  • Alternative names
    • Retinaldehyde-binding protein 1-like 2

Gene names

    • Name
      CLVS2
    • Synonyms
      RLBP1L2
    • ORF names
      QccE-21404, QtrA-13887

Organism names

Accessions

  • Primary accession
    Q95KF7
  • Secondary accessions
    • Q9BE37

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002976521-327Clavesin-2
Modified residue325Phosphoserine

Keywords

Expression

Gene expression databases

Interaction

Subunit

Forms a complex with clathrin heavy chain and gamma-adaptin.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain96-257CRAL-TRIO
Region287-327Disordered

Domain

The CRAL-TRIO domain is required for targeting to the membrane and for binding PtdIns(3,5)P2.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    327
  • Mass (Da)
    38,000
  • Last updated
    2007-08-21 v2
  • Checksum
    FF40A5A222A4DB1C
MTHLQAGLSPETLEKARLELNENPDTLHQDIQEVRDMVITRPDIGFLRTDDAFILRFLRARKFHHFEAFRLLAQYFEYRQQNLDMFKSFKATDPGIKQALKDGFPGGLANLDHYGRKILVLFAANWDQSRYTLVDILRAILLSLEAMIEDPELQVNGFVLIIDWSNFTFKQASKLTPSMLRLAIEGLQDSFPARFGGIHFVNQPWYIHALYTVIRPFLKEKTRKRIFLHGNNLNSLHQLIHPEILPSEFGGMLPPYDMGTWARTLLDHEYDDDSEYNVDSYSMPVKEVEKELSPKSMKRSQSVVDPTVLKRMDKNEEENMQPLLSLD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7N9CD90A0A7N9CD90_MACFACLVS2303

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict101in Ref. 1; BAB46902
Sequence conflict198in Ref. 1; BAB41140
Sequence conflict241in Ref. 1; BAB41140

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB060190
EMBL· GenBank· DDBJ
BAB41140.1
EMBL· GenBank· DDBJ
mRNA
AB060902
EMBL· GenBank· DDBJ
BAB46902.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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