Q8R426 · KCIP1_RAT

  • Protein
    A-type potassium channel modulatory protein KCNIP1
  • Gene
    Kcnip1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels (PubMed:14980206).
Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner (PubMed:14980206).
Modulates KCND2/Kv4.2 currents (PubMed:14980206).
In vitro, modulates KCND1/Kv4.1 currents (By similarity).
Increases the presence of KCND2 at the cell surface (PubMed:14980206).

Features

Showing features for binding site.

122720406080100120140160180200220
TypeIDPosition(s)Description
Binding site146Ca2+ 1 (UniProtKB | ChEBI)
Binding site148Ca2+ 1 (UniProtKB | ChEBI)
Binding site150Ca2+ 1 (UniProtKB | ChEBI)
Binding site152Ca2+ 1 (UniProtKB | ChEBI)
Binding site157Ca2+ 1 (UniProtKB | ChEBI)
Binding site194Ca2+ 2 (UniProtKB | ChEBI)
Binding site196Ca2+ 2 (UniProtKB | ChEBI)
Binding site198Ca2+ 2 (UniProtKB | ChEBI)
Binding site205Ca2+ 2 (UniProtKB | ChEBI)

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 Componentcytoplasmic side of plasma membrane
Cellular Componentdendrite
Cellular Componentneuronal cell body
Cellular Componentpotassium channel complex
Cellular Componentvoltage-gated potassium channel complex
Molecular Functioncalcium ion binding
Molecular Functionpotassium channel activity
Molecular Functionpotassium channel regulator activity
Molecular Functionprotein-containing complex binding
Molecular Functiontransmembrane transporter binding
Biological Processpositive regulation of action potential
Biological Processregulation of potassium ion transmembrane transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    A-type potassium channel modulatory protein KCNIP1
  • Alternative names
    • Kv channel-interacting protein 1 (KChIP1
      )
    • Potassium channel-interacting protein 1

Gene names

    • Name
      Kcnip1
    • Synonyms
      Kchip1

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q8R426
  • Secondary accessions
    • Q793P9
    • Q8CIR1
    • Q8R425

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis214-227Abolishes interaction with KCND2.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000738201-227A-type potassium channel modulatory protein KCNIP1

Proteomic databases

Expression

Tissue specificity

Detected in hippocampus and in the molecular layer of the dentate gyrus (at protein level) (PubMed:15356203).
Isoform 1 and isoform 2 are predominantly expressed at equal levels in brain. Colocalizes with KCND3 in inhibitory interneurons in cortex and hippocampus and in striatal interneurons.

Interaction

Subunit

Component of heteromultimeric potassium channels (PubMed:14980206, PubMed:15356203).
Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity).
Part of a heterooctamer composed of the tetrameric channel and four KCNIP1 chains (By similarity).
Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. Self-associates to form homodimers and homotetramers. Interacts with KCNIP2 isoform 3 in a calcium-dependent manner (By similarity).
Interacts with KCND2; this interaction mediates the capture of both the N- and C-terminus of KCND2, thus preventing KCND2 N-type inactivation and modulates the channel gating kinetics (PubMed:10676964, PubMed:11423117, PubMed:14980206).
Interacts with KCND3; each KCNIP1 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction stabilizes the tetrameric form and modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:10676964).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain38-94EF-hand 1; degenerate
Domain97-132EF-hand 2
Domain133-168EF-hand 3
Domain181-216EF-hand 4
Region214-227Interaction with KCND2

Sequence similarities

Belongs to the recoverin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8R426-1

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.

  • Name
    1
  • Synonyms
    KChIP1b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    227
  • Mass (Da)
    26,817
  • Last updated
    2005-08-16 v2
  • Checksum
    92A2F0D72A120197
MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDDLEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM

Q8R426-2

  • Name
    2
  • Synonyms
    KChIP1a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2K0U3A0A0G2K0U3_RATKcnip1232
A0A8I6ALG6A0A8I6ALG6_RATKcnip1225
A0A0G2K701A0A0G2K701_RATKcnip1203
A0A0H2UHE0A0A0H2UHE0_RATKcnip1236

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict10in Ref. 3; AAN34942
Alternative sequenceVSP_01504821-31in isoform 2
Sequence conflict37in Ref. 1; BAB03308
Sequence conflict107in Ref. 2; AAL92564/AAL92565

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB046443
EMBL· GenBank· DDBJ
BAB03308.1
EMBL· GenBank· DDBJ
mRNA
AY082657
EMBL· GenBank· DDBJ
AAL92564.1
EMBL· GenBank· DDBJ
mRNA
AY082658
EMBL· GenBank· DDBJ
AAL92565.1
EMBL· GenBank· DDBJ
mRNA
AY142709
EMBL· GenBank· DDBJ
AAN34942.1
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.
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