SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0CAC1C_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCACNA1C
DescriptionVoltage-dependent l-type calcium channel alpha-1c subunit (voltage- gated calcium channel alpha subunit cav1.2) (calcium channel, l type, alpha-1 polypeptide, isoform 1, cardiac muscle).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005891 voltage-gated calcium channel complex (TAS)
0005515 protein binding (IPI)
0005245 voltage-gated calcium channel activity (TAS)
0008016 regulation of heart contraction rate (TAS)
0006810 transport (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/525313547.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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
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. L-type calcium channels are formed from alpha-1S.lpha-1C and alpha-1D subunits. The variability in the C-terminal region of the alpha-1C subunit generated by alternative splicing influences the kinetics.alcium- and voltage-dependence of L-type channels . The N-terminus is also a site of significant structural diversity .
  IPR005451:L-type voltage-dependent calcium channel alpha 1C 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
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 .
  IPR005446:L-type voltage-dependent calcium channel alpha 1 subunit
This domain consists of a duplication of two EF-hand units.here each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain . These include: calbindin D9K.100 proteins such as calcyclin.olcalcin phl p 7 (a calcium-binding pollen allergen).steonectin.arvalbumin.almodulin family of proteins (troponin C.altractin.dc4p.yosin essential chain.alcineurin.ecoverin.eurocalcin).lasmodial-specific CaII-binding protein Cbp40.enta-EF-Hand proteins (sorcin.rancalcin.alpain).s well as multidomain proteins such as phosphoinositide-specific phospholipase C.ystrophin.b1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
  IPR011992:EF-Hand type
IPR005821:Ion_trans 
Evalue:-75.3872146606445 
Location:161-404IPR005821:Ion_trans 
Evalue:-74.2924270629883 
Location:1273-1523IPR005821:Ion_trans 
Evalue:-69.1023712158203 
Location:955-1185IPR005821:Ion_trans 
Evalue:-60.1487426757813 
Location:558-752IPR005451:LVDCCAlpha1C 
Evalue:0 
Location:1899-2118IPR011992:EF-Hand_type 
Evalue:0 
Location:1534-1575IPR002077:CACHANNEL 
Evalue:0 
Location:405-429IPR002077:CACHANNEL 
Evalue:0 
Location:1187-1207IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:808-827IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:788-807IPR005446:LVDCCALPHA1 
Evalue:0 
Location:501-519IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:1788-1806IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:64-80IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:828-844IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:1807-1823IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:33-48IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:17-32IPR005451:LVDCCALPHA1C 
Evalue:0 
Location:1727-1739IPR001696:NACHANNEL 
Evalue:0 
Location:0-0
SequencesProtein: CAC1C_HUMAN (2221 aa)
mRNA: NM_000719 Z34819 Z34821
Local Annotation
Synapse Ontology
?
sdb:0188 calcium channel  (Evidence:keywords,domains)
?
sdb:0195 calcium-dependent neuronal response  (Evidence:keywords,domains)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords,domains)
?
sdb:0223 transmitter release  (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 assignmentK04850
  Level 3 annotation:
    calcium channel, voltage-dependent, L type, alpha 1C subunit
  Level 2 annotation:
    Calcium signaling pathway
    Ion channels
    Long-term potentiation
    Type II diabetes mellitus
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 105 residues, 2032724-2033038Exon2: 110 residues, 2094650-2094974Exon3: 36 residues, 2099753-2099857Exon4: 48 residues, 2428402-2428542Exon5: 48 residues, 2436993-2437133Exon6: 55 residues, 2465530-2465689Exon7: 67 residues, 2472616-2472813Exon8: 36 residues, 2484268-2484372Exon9: 59 residues, 2492238-2492411Exon10: 32 residues, 2529369-2529460Exon11: 11 residues, 2536377-2536404Exon12: 55 residues, 2545848-2546009Exon13: 77 residues, 2546995-2547221Exon14: 71 residues, 2561016-2561224Exon15: 42 residues, 2562248-2562369Exon16: 40 residues, 2563929-2564044Exon17: 42 residues, 2564802-2564923Exon18: 25 residues, 2565261-2565331Exon19: 46 residues, 2572639-2572772Exon20: 45 residues, 2575300-2575430Exon21: 22 residues, 2576656-2576716Exon22: 37 residues, 2581280-2581387Exon23: 31 residues, 2584507-2584595Exon24: 38 residues, 2585105-2585213Exon25: 19 residues, 2586037-2586090Exon26: 51 residues, 2586410-2586557Exon27: 69 residues, 2587937-2588139Exon28: 55 residues, 2589967-2590126Exon29: 39 residues, 2591329-2591440Exon30: 30 residues, 2613723-2613807Exon31: 13 residues, 2627901-2627934Exon32: 45 residues, 2631066-2631195Exon33: 24 residues, 2633261-2633327Exon34: 32 residues, 2634573-2634665Exon35: 57 residues, 2644251-2644417Exon36: 44 residues, 2645007-2645135Exon37: 34 residues, 2646112-2646209Exon38: 36 residues, 2648359-2648462Exon39: 36 residues, 2653967-2654069Exon40: 44 residues, 2656520-2656648Exon41: 47 residues, 2657159-2657294Exon42: 119 residues, 2658870-2659223Exon43: 45 residues, 2661976-2662105Exon44: 37 residues, 2665162-2665269Exon45: 36 residues, 2665592-2665696Exon46: 113 residues, 2667873-2668206Exon47: 682 residues, 2670326-2672368Exon48: 2 residues, -Jump to CAC1C_HUMANExon1: 17 residues, 2032989-2033038Exon2: 109 residues, 2094650-2094972Exon3: 37 residues, 2099751-2099857Exon4: 48 residues, 2428402-2428542Exon5: 48 residues, 2436993-2437133Exon6: 55 residues, 2465530-2465689Exon7: 67 residues, 2472616-2472813Exon8: 36 residues, 2484268-2484372Exon9: 59 residues, 2492238-2492411Exon10: 32 residues, 2529369-2529460Exon11: 11 residues, 2536377-2536404Exon12: 55 residues, 2545848-2546009Exon13: 77 residues, 2546995-2547221Exon14: 71 residues, 2561016-2561224Exon15: 42 residues, 2562248-2562369Exon16: 40 residues, 2563929-2564044Exon17: 42 residues, 2564802-2564923Exon18: 25 residues, 2565261-2565331Exon19: 46 residues, 2572639-2572772Exon20: 45 residues, 2575300-2575430Exon21: 22 residues, 2576656-2576716Exon22: 22 residues, 2576863-2576923Exon23: 37 residues, 2581280-2581387Exon24: 31 residues, 2584507-2584595Exon25: 38 residues, 2585105-2585213Exon26: 19 residues, 2586037-2586090Exon27: 51 residues, 2586410-2586557Exon28: 69 residues, 2587937-2588139Exon29: 55 residues, 2589967-2590126Exon30: 39 residues, 2591329-2591440Exon31: 30 residues, 2613055-2613139Exon32: 30 residues, 2613723-2613807Exon33: 13 residues, 2627901-2627934Exon34: 45 residues, 2631066-2631195Exon35: 24 residues, 2633261-2633327Exon36: 32 residues, 2634573-2634665Exon37: 57 residues, 2644251-2644417Exon38: 44 residues, 2645007-2645135Exon39: 34 residues, 2646112-2646209Exon40: 36 residues, 2648359-2648462Exon41: 36 residues, 2653967-2654069Exon42: 44 residues, 2656520-2656648Exon43: 47 residues, 2657159-2657294Exon44: 119 residues, 2658870-2659223Exon45: 45 residues, 2661976-2662105Exon46: 37 residues, 2665162-2665269Exon47: 36 residues, 2665592-2665696Exon48: 113 residues, 2667873-2668206Exon49: 133 residues, 2670326-2670720Exon50: 2 residues, -Jump to CAC1C_HUMANExon1: 17 residues, 2032989-2033038Exon2: 109 residues, 2094650-2094972Exon3: 37 residues, 2099751-2099857Exon4: 48 residues, 2428402-2428542Exon5: 48 residues, 2436993-2437133Exon6: 55 residues, 2465530-2465689Exon7: 67 residues, 2472616-2472813Exon8: 36 residues, 2484268-2484372Exon9: 59 residues, 2492238-2492411Exon10: 32 residues, 2529369-2529460Exon11: 11 residues, 2536377-2536404Exon12: 55 residues, 2545848-2546009Exon13: 77 residues, 2546995-2547221Exon14: 71 residues, 2561016-2561224Exon15: 42 residues, 2562248-2562369Exon16: 40 residues, 2563929-2564044Exon17: 42 residues, 2564802-2564923Exon18: 25 residues, 2565261-2565331Exon19: 46 residues, 2572639-2572772Exon20: 45 residues, 2575300-2575430Exon21: 22 residues, 2576656-2576716Exon22: 37 residues, 2581280-2581387Exon23: 31 residues, 2584507-2584595Exon24: 38 residues, 2585105-2585213Exon25: 19 residues, 2586037-2586090Exon26: 51 residues, 2586410-2586557Exon27: 69 residues, 2587937-2588139Exon28: 55 residues, 2589967-2590126Exon29: 39 residues, 2591329-2591440Exon30: 30 residues, 2613055-2613139Exon31: 30 residues, 2613723-2613807Exon32: 13 residues, 2627901-2627934Exon33: 45 residues, 2631066-2631195Exon34: 24 residues, 2633261-2633327Exon35: 32 residues, 2634573-2634665Exon36: 57 residues, 2644251-2644417Exon37: 44 residues, 2645007-2645135Exon38: 34 residues, 2646112-2646209Exon39: 36 residues, 2648359-2648462Exon40: 36 residues, 2653967-2654069Exon41: 44 residues, 2656520-2656648Exon42: 47 residues, 2657159-2657294Exon43: 119 residues, 2658870-2659223Exon44: 45 residues, 2661976-2662105Exon45: 37 residues, 2665162-2665269Exon46: 36 residues, 2665592-2665696Exon47: 113 residues, 2667873-2668206Exon48: 133 residues, 2670326-2670720Exon49: 2 residues, -Jump to CAC1C_HUMAN