Q8K2H4 · ACAP1_MOUSE

  • Protein
    Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
  • Gene
    Acap1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration (By similarity).

Miscellaneous

Cells overexpressing Acap1 show accumulation of an electron dense coat containing Acap1 and Cltc on internal membranes as well as accumulation of Tfrc in pericentriolar recycling endosomes. Adipocytes with reduced level of Acap1 or Cltc fail to transport SLC2A4/GLUT4 from recycling endosomes to the cell surface upon insulin stimulation.

Activity regulation

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.

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 Componentrecycling endosome membrane
Molecular FunctionGTPase activator activity
Molecular Functionmetal ion binding
Biological Processlipid catabolic process
Biological Processsignal transduction

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
  • Alternative names
    • Centaurin-beta-1 (Cnt-b1)

Gene names

    • Name
      Acap1
    • Synonyms
      Centb1, Kiaa0050

Organism names

  • Taxonomic identifier
  • Strains
    • NOD
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8K2H4
  • Secondary accessions
    • Q3U441
    • Q571H6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis448Loss of catalytic activity. No loss of accumulation of coat proteins on internal membranes upon overexpression of Acap1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003063841-740Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Modified residue4853'-nitrotyrosine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Banana-shaped homodimer laterally assembling into tetramers, the tetramers further pack helically onto the membrane. Interacts with GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1 recycling.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, zinc finger, compositional bias, repeat.

TypeIDPosition(s)Description
Domain1-226BAR
Region1-382Required for formation of endosomal tubules when overexpressed with PIP5K1C
Domain265-360PH
Domain405-527Arf-GAP
Region405-740Required for interaction with GULP1
Zinc finger420-443C4-type
Region525-562Disordered
Region525-566Prevents interaction with ITGB1 when S-554 is not phosphorylated
Compositional bias536-550Pro residues
Repeat606-635ANK 1
Repeat639-668ANK 2
Repeat672-702ANK 3

Domain

PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain of one ACAP1 dimer inserts into the membrane, while the other PH domain acts primaryly to interact with adjacent ACAP1 dimers (By similarity).
The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions (By similarity).

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    740
  • Mass (Da)
    81,704
  • Last updated
    2002-10-01 v1
  • Checksum
    798A87CBCC5F8513
MTVKLDFEECLKDSPRFRASIELVETEVSELETRLEKLLKLGSCLLESGQHYLAAGRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGFREARRDFWRGAENLEAALTHNAEVPRRRVQEAEEAGTALRTARAGYRSRALDYALQVNVIEDKRKFDIMEFVLRLVEAQATYFQQGHEELNRLAQYRKELGTQLHNLVLNSARQKRDMEQRHVLLKQKELGGEEPEPSLKEGPSGLVMEGHLFKRASNAFKTWSRRWFTIQNNQLVYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCFLQADSERLLQLWVSAVQSSIASAFSQAHLENSPRGPGQVSGYHAPGSAATLACGGAARGRESGGVGQVAAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVIINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGPPRGHPPVPPKPPIRPHSGIVRSKSECPSDDMGSLHPGALLFQAAGHPPSLPTMADALAHGADVNWVNVGQGNATPLIRATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFLKRGADLGARDTEGRDPLTIAMETTNADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict522in Ref. 1; BAE32594
Compositional bias536-550Pro residues
Sequence conflict584in Ref. 4; BAD90138

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK154449
EMBL· GenBank· DDBJ
BAE32594.1
EMBL· GenBank· DDBJ
mRNA
AL596185
EMBL· GenBank· DDBJ
CAI35146.1
EMBL· GenBank· DDBJ
Genomic DNA
AL845465
EMBL· GenBank· DDBJ
CAI35146.1
EMBL· GenBank· DDBJ
Genomic DNA
AL845465
EMBL· GenBank· DDBJ
CAM13886.1
EMBL· GenBank· DDBJ
Genomic DNA
AL596185
EMBL· GenBank· DDBJ
CAM13886.1
EMBL· GenBank· DDBJ
Genomic DNA
BC031462
EMBL· GenBank· DDBJ
AAH31462.1
EMBL· GenBank· DDBJ
mRNA
AK220213
EMBL· GenBank· DDBJ
BAD90138.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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