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
0CAC1A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCACNA1A
DescriptionVoltage-dependent p/q-type calcium channel alpha-1a subunit (voltage- gated calcium channel alpha subunit cav2.1) (calcium channel, l type, alpha-1 polypeptide isoform 4) (brain calcium channel i) (bi).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (ISS)
0005245 voltage-gated calcium channel activity (ISS)
0007204 elevation of cytosolic calcium ion concentr... (ISS)
0007399 neurogenesis (TAS)
0007268 synaptic transmission (TAS)
0006810 transport (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/1566570154.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
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. P- and Q-type channels are formed from alpha-1A subunits and function in transmitter release . P-type channels are prevalent in cerebellar Purkinje cells.ut are also expressed in many central and peripheral neurons.uch as the spinal cord and visual cortex. By contrast.-type channels are found in cerebellar granule neurones and the hippocampus. Different mutations in the alpha-1A subunit produce 3 human diseases: (1) episodic ataxia type-2; (2) familial hemiplegic migraine; and (3) spinocerebellar ataxia type-6. All 3 diseases result in cerebellar atrophy.ut they differ in the extent and rate of progression of neuronal degeneration
  IPR005448:P/Q-type voltage-dependent calcium channel alpha 1 subunit
IPR005821:Ion_trans 
Evalue:-69.958610534668 
Location:135-359IPR005821:Ion_trans 
Evalue:-69.7212448120117 
Location:1600-1810IPR005821:Ion_trans 
Evalue:-68.1487426757813 
Location:1279-1510IPR005821:Ion_trans 
Evalue:-57.7447280883789 
Location:521-713IPR002077:CACHANNEL 
Evalue:0 
Location:360-384IPR005448:PQVDCCALPHA1 
Evalue:0 
Location:1192-1213IPR005448:PQVDCCALPHA1 
Evalue:0 
Location:879-899IPR002077:CACHANNEL 
Evalue:0 
Location:1512-1532IPR005448:PQVDCCALPHA1 
Evalue:0 
Location:918-936IPR005448:PQVDCCALPHA1 
Evalue:0 
Location:1023-1037IPR001696:NACHANNEL 
Evalue:0 
Location:0-0
SequencesProtein: CAC1A_HUMAN (2505 aa)
mRNA: NM_000068 NM_023035
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (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 assignmentK04344
  Level 3 annotation:
    calcium channel, voltage-dependent, P/Q type, alpha 1A subunit
  Level 2 annotation:
    Calcium signaling pathway
    Ion channels
    Long-term depression
    Type II diabetes mellitus
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 252 residues, 13179114-13179867Exon2: 86 residues, 13180569-13180823Exon3: 64 residues, 13181125-13181312Exon4: 14 residues, 13182430-13182466Exon5: 40 residues, 13183916-13184030Exon6: 48 residues, 13184197-13184336Exon7: 38 residues, 13184444-13184554Exon8: 35 residues, 13186046-13186147Exon9: 38 residues, 13186314-13186422Exon10: 37 residues, 13196480-13196586Exon11: 34 residues, 13200512-13200609Exon12: 44 residues, 13201895-13202023Exon13: 52 residues, 13203523-13203674Exon14: 40 residues, 13206734-13206850Exon15: 24 residues, 13207022-13207088Exon16: 41 residues, 13207427-13207544Exon17: 30 residues, 13216995-13217079Exon18: 39 residues, 13224804-13224915Exon19: 57 residues, 13226908-13227073Exon20: 69 residues, 13229163-13229365Exon21: 48 residues, 13231377-13231515Exon22: 55 residues, 13233263-13233424Exon23: 35 residues, 13234547-13234647Exon24: 37 residues, 13247663-13247770Exon25: 22 residues, 13248882-13248942Exon26: 45 residues, 13255080-13255210Exon27: 48 residues, 13256881-13257020Exon28: 156 residues, 13258316-13258780Exon29: 272 residues, 13270357-13271167Exon30: 37 residues, 13272363-13272470Exon31: 24 residues, 13275359-13275427Exon32: 41 residues, 13275580-13275698Exon33: 26 residues, 13279595-13279668Exon34: 46 residues, 13279933-13280065Exon35: 39 residues, 13280229-13280342Exon36: 39 residues, 13284482-13284595Exon37: 72 residues, 13288925-13289135Exon38: 33 residues, 13302057-13302150Exon39: 21 residues, 13304682-13304739Exon40: 40 residues, 13306191-13306307Exon41: 36 residues, 13307619-13307723Exon42: 66 residues, 13331419-13331613Exon43: 53 residues, 13337130-13337283Exon44: 32 residues, 13343501-13343593Exon45: 48 residues, 13424689-13424829Exon46: 37 residues, 13426920-13427026Exon47: 192 residues, 13477745-13478317Exon48: 2 residues, -Jump to CAC1A_HUMANExon1: 250 residues, 13179114-13179862Exon2: 86 residues, 13180569-13180823Exon3: 64 residues, 13181125-13181312Exon4: 14 residues, 13182430-13182466Exon5: 40 residues, 13183916-13184030Exon6: 48 residues, 13184197-13184336Exon7: 38 residues, 13184444-13184554Exon8: 35 residues, 13186046-13186147Exon9: 38 residues, 13186314-13186422Exon10: 37 residues, 13196480-13196586Exon11: 34 residues, 13200512-13200609Exon12: 44 residues, 13201895-13202023Exon13: 52 residues, 13203523-13203674Exon14: 40 residues, 13206734-13206850Exon15: 24 residues, 13207022-13207088Exon16: 41 residues, 13207427-13207544Exon17: 30 residues, 13216995-13217079Exon18: 39 residues, 13224804-13224915Exon19: 57 residues, 13226908-13227073Exon20: 69 residues, 13229163-13229365Exon21: 48 residues, 13231377-13231515Exon22: 55 residues, 13233263-13233424Exon23: 35 residues, 13234547-13234647Exon24: 37 residues, 13247663-13247770Exon25: 22 residues, 13248882-13248942Exon26: 45 residues, 13255080-13255210Exon27: 48 residues, 13256881-13257020Exon28: 156 residues, 13258316-13258780Exon29: 272 residues, 13270357-13271167Exon30: 37 residues, 13272363-13272470Exon31: 24 residues, 13275359-13275427Exon32: 41 residues, 13275580-13275698Exon33: 26 residues, 13279595-13279668Exon34: 46 residues, 13279933-13280065Exon35: 39 residues, 13280229-13280342Exon36: 39 residues, 13284482-13284595Exon37: 72 residues, 13288925-13289135Exon38: 33 residues, 13302057-13302150Exon39: 21 residues, 13304682-13304739Exon40: 40 residues, 13306191-13306307Exon41: 36 residues, 13307619-13307723Exon42: 66 residues, 13331419-13331613Exon43: 53 residues, 13337130-13337283Exon44: 32 residues, 13343501-13343593Exon45: 48 residues, 13424689-13424829Exon46: 37 residues, 13426920-13427026Exon47: 192 residues, 13477745-13478317Exon48: 2 residues, -Jump to CAC1A_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4368 12768634-12773694 ~-5K 18105(PRDX2)(-)Loci: 3091 12810347-12846765 ~-36K 18111(MAST1)(+)Loci: 3092 12862973-12871782 ~-9K 18114(GCDH)(+)Loci: 4369 13115902-13122052 ~-6K 18133(STX10)(-)Loci: 4370 13179114-13478317 ~-299K 18136(CACNA1A)(-)Loci: 4367 12734816-12747337 ~-13K 18101(HOOK2)(-)Link out to UCSC