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0CAC1I_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCACNA1I
DescriptionVoltage-dependent t-type calcium channel alpha-1i subunit (voltage- gated calcium channel alpha subunit cav3.3) (ca(v)3.3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005891 voltage-gated calcium channel complex (NAS)
0008332 low voltage-gated calcium channel activity (NAS)
0006816 calcium ion transport (NAS)
0007165 signal transduction (TAS)
0006810 transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Cation channels are transport proteins responsible for the movement of cations through the membrane. These proteins contain 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times.hereas in others (e.g. K channels) the protein forms as a tetramer in the membrane. Calcium channel proteins are involved in the control of neurotransmitterrelease from neurons .nd play an important role in the regulation ofa variety of cellular functions.ncluding membrane excitability.usclecontraction and synaptic transmission . The channel proteins arecomposed of 4 tightly-coupled subunits (alpha-1.lpha-2.eta and gamma).he alpha-1 subunit from each creating the pore for the import ofextracellular calcium ions. The alpha-1 subunit shares sequencecharacteristics with all voltage-dependent cation channels.nd exploitsthe same 6-helix bundle structural motif - in both sodium and calciumchannels.his motif is repeated 4 times within the sequence to give a24-helix bundle. There are several tissue-specific pharmacologically andelectrophysiologically distinct isoforms of calcium channels.oded forby separate genes in a multi-gene family. In skeletal muscle.achtightly-bound assembly of alpha.eta and gamma subunits associates with4 others to form a pentameric macromolecule .
  IPR002077:Ca2+ channel, alpha subunit
InterPro domains unassigned to SynO:
This group of proteins is found in sodium.otassium.nd calcium ion channels proteins. The proteins have 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some Na channels proteins the domain is repeated four times.hereas in others (e.g. K channels) the protein forms a tetramer in the membrane. A bacterial structure of the protein is known for the last two helices but is not included in the Pfam family due to it lacking the first four helices.
  IPR005821:Ion transport
Voltage-dependent sodium channels are transmembrane (TM) proteinsresponsible for the depolarising phase of the action potential in mostelectrically excitable cells . They may exist in 3 states : theresting state.here the channel is closed; the activated state.here thechannel is open; and the inactivated state.here the channel is closedand refractory to opening. Several different structurally and functionallydistinct isoforms are found in mammals.oded for by a multigene family.hese being responsible for the different types of sodium ion currentsfound in excitable tissues.The structure of sodium channels is based on 4 internal repeats of a 6-helixbundle (in which 5 of the membrane-spanning segments are hydrophobic andthe other is positively charged).orming a 24-helical bundle. The chargedsegments are believed to be localised within clusters formed by their 5 hydrophobic neighbours: it is postulated that the charged domain may be thevoltage sensor region.ossibly moving outward on depolarisation.ausing aconformational change. This model.roposed by Noda et al. .ontrastswith that of Sato and Matsumoto .n which the TM segments are juxtaposedoctagonally. The basic structural motif (the 6-helix bundle) is also found in potassium and calcium channel alpha subunits.Cation channels are transport proteins responsible for the movement of cations through the membrane. These proteins contain 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times.hereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
  IPR001696:Na+ channel
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel conductance and toxin binding properties. Each type of K+ channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes . In prokaryotic cells.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+ channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+ channels; and three types of calcium (Ca)-activated K+ channels (BK.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In addition.here are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels.
  IPR003091:Voltage-dependent potassium channel
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli.uch as action potentials.llows Ca2+ ions to enter neurons down a steep electrochemical gradient.roducing transient intracellular Ca2+ signals. Many of the processes that occur in neurons.ncluding transmitter release.ene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The activity of this pore is modulated by 4 tightly-coupled subunits: an intracellular beta subunit; a transmembrane gammasubunit; and a disulphide-linked complex of alpha-2 and delta subunits.hich are proteolytically cleaved from the same gene product. Voltage-gated calcium channels are classified as T.... and R.nd are distinguished by their sensitivity to pharmacological blocks.ingle-channel conductance kinetics.nd voltage-dependence. On the basis of their voltage activation properties.he voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L... and R-type) threshold-activated channels . Generally.he channel proteins are composed of 4 tightly-coupled subunits (alpha-1.lpha-2.eta and gamma).he alpha-1 subunit from each creating the pore for the import of extracellular calcium ions. The alpha-1 subunit shares sequence characteristics with all voltage-dependent cation channels.nd exploits the same 6-helix bundle structural motif - in both sodium and calcium channels.his motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats. of the transmembrane (TM) segments (S1.2.3.5.6) are hydrophobic and one is positively charged (S4) - the latter is characterised by charged amino acids at very third position.nd probably represents the voltage-sensor. Several genes encoding alpha-1 subunits have been identified.ach forming a distinct electrophysiological channel. T-type calcium channels are composed of alpha-1G and alpha-1H subunits. They exhibit unique voltage- dependent kinetics.mall single channel conductance.apid inactivation.low deactivation and a relatively high permeability to calcium . They are primarily responsible for rebound burst firing in central neurons and are implicated in normal brain functions.uch as slow wave sleep.nd in diseased states.uch as epilepsy . They also play an important role in hormone secretion and smooth muscle excitability .
  IPR005445:T-type voltage-dependent calcium channel alpha 1 subunit
IPR005821:Ion_trans 
Evalue:-66.0409622192383 
Location:1206-1430IPR005821:Ion_trans 
Evalue:-63.7447280883789 
Location:117-397IPR005821:Ion_trans 
Evalue:-55.5228805541992 
Location:1521-1729IPR005821:Ion_trans 
Evalue:-54.8239097595215 
Location:674-861IPR003091:KCHANNEL 
Evalue:0 
Location:1480-1508IPR005445:TVDCCALPHA1 
Evalue:0 
Location:59-75IPR005445:TVDCCALPHA1 
Evalue:0 
Location:1442-1457IPR005445:TVDCCALPHA1 
Evalue:0 
Location:430-444IPR005445:TVDCCALPHA1 
Evalue:0 
Location:658-671IPR001696:NACHANNEL 
Evalue:0 
Location:0-0
SequencesProtein: CAC1I_HUMAN (2223 aa)
mRNA: NM_021096
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords,domains)
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords,domains)
?
sdb:0223 transmitter release  (Evidence:keywords,domains)
modulate the ability to generate LTP
sdb:0252 modulation of the ability to generate LTP  (Evidence:keywords,domains)
The action potential at the presynaptic region induces the opening of calcium channel, and the resulting calcium transient stimulates synaptic vesicle exocytosis.
sdb:0272 opening of Calcium channels  (Evidence:keywords,domains)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
KO assignmentK04856
  Level 3 annotation:
    calcium channel, voltage-dependent, T type, alpha 1I subunit
  Level 2 annotation:
    Calcium signaling pathway
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 79 residues, 38296703-38296939Exon2: 39 residues, 38324101-38324213Exon3: 46 residues, 38326470-38326604Exon4: 34 residues, 38345260-38345358Exon5: 55 residues, 38360515-38360675Exon6: 107 residues, 38366817-38367133Exon7: 33 residues, 38368747-38368840Exon8: 106 residues, 38372519-38372832Exon9: 37 residues, 38373772-38373877Exon10: 143 residues, 38375451-38375876Exon11: 52 residues, 38384102-38384254Exon12: 64 residues, 38384881-38385067Exon13: 41 residues, 38385383-38385501Exon14: 54 residues, 38385647-38385803Exon15: 33 residues, 38386294-38386388Exon16: 69 residues, 38387058-38387261Exon17: 159 residues, 38387915-38388386Exon18: 35 residues, 38388726-38388827Exon19: 43 residues, 38389668-38389792Exon20: 25 residues, 38390041-38390110Exon21: 63 residues, 38390689-38390874Exon22: 44 residues, 38391448-38391575Exon23: 44 residues, 38391831-38391957Exon24: 32 residues, 38394242-38394332Exon25: 66 residues, 38395988-38396181Exon26: 52 residues, 38396753-38396905Exon27: 38 residues, 38398149-38398259Exon28: 46 residues, 38398899-38399033Exon29: 25 residues, 38399913-38399984Exon30: 28 residues, 38403291-38403370Exon31: 42 residues, 38403937-38404059Exon32: 115 residues, 38405057-38405396Exon33: 51 residues, 38405672-38405819Exon34: 43 residues, 38406880-38407003Exon35: 57 residues, 38408446-38408612Exon36: 67 residues, 38410252-38410449Exon37: 1326 residues, 38411711-38415684Exon38: 2 residues, -Jump to CAC1I_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3318 38075899-38111525 ~-36K 24775(SYNGR1)(+)Loci: 3319 38296703-38415684 ~-119K 24788(CACNA1I)(+)Loci: 4573 38468995-38619740 ~-151K 24792(-)Loci: 4572 37949664-37970936 ~-21K 24769(PDGFB)(-)Link out to UCSC