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1Q8IZS9_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionVoltage-gated calcium channel alpha(2)delta-4 subunit.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016020 membrane (IEA)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is found at the N terminus of proteins containing von Willebrand factor type A (VWA. and Cache () domains. It has been found in vertebrates.rosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits .
  IPR013608:VWA N-terminal
Cache is a signaling domain that is found in animal calcium channel subunits and a certain class of prokaryotic chemotaxis receptors.
The von Willebrand factor is a large multimeric glycoprotein found in bloodplasma. Mutant forms are involved in the aetiology of bleeding disorders . In von Willebrand factor.he type A domain (vWF) is the prototype fora protein superfamily. The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands . Foldrecognition algorithms were used to score sequence compatibility with alibrary of known structures: the vWF domain fold was predicted to be adoubly-wound.pen.wisted beta-sheet flanked by alpha-helices . 3D structures have been determined for the I-domains of integrins CD11b(with bound magnesium) and CD11a (with bound manganese) . The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this siterepresents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands . The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved.ut the manner in which the metal ion is coordinated differs slightly .
  IPR002035:von Willebrand factor, type A
SequencesProtein: Q8IZS9_HUMAN (1120 aa)
mRNA: BX537437
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK04861
  Level 3 annotation:
    calcium channel, voltage-dependent, alpha 2/delta subunit 4
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 599 residues, 1771391-1773186Exon2: 29 residues, 1774725-1774806Exon3: 40 residues, 1775092-1775207Exon4: 41 residues, 1776844-1776962Exon5: 9 residues, 1779101-1779122Exon6: 19 residues, 1779426-1779479Exon7: 19 residues, 1779812-1779865Exon8: 27 residues, 1780469-1780545Exon9: 25 residues, 1781000-1781071Exon10: 23 residues, 1789704-1789767Exon11: 17 residues, 1789969-1790014Exon12: 22 residues, 1791088-1791150Exon13: 29 residues, 1820165-1820246Exon14: 44 residues, 1823828-1823956Exon15: 34 residues, 1826020-1826116Exon16: 33 residues, 1833377-1833471Exon17: 34 residues, 1835438-1835536Exon18: 17 residues, 1835610-1835656Exon19: 24 residues, 1838003-1838071Exon20: 22 residues, 1839571-1839633Exon21: 26 residues, 1854030-1854102Exon22: 31 residues, 1854677-1854764Exon23: 27 residues, 1857741-1857816Exon24: 29 residues, 1858382-1858463Exon25: 28 residues, 1859230-1859308Exon26: 46 residues, 1862293-1862427Exon27: 28 residues, 1863669-1863748Exon28: 40 residues, 1864194-1864308Exon29: 32 residues, 1864413-1864503Exon30: 27 residues, 1865391-1865466Exon31: 52 residues, 1865649-1865800Exon32: 22 residues, 1866435-1866496Exon33: 46 residues, 1886866-1886998Exon34: 56 residues, 1887301-1887464Exon35: 22 residues, 1889332-1889392Exon36: 41 residues, 1892449-1892566Exon37: 29 residues, 1894280-1894362Exon38: 154 residues, 1897673-1898131Exon39: 2 residues, -Jump to Q8IZS9_HUMAN  
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