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0CPNE6_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionCopine-6 (copine vi) (neuronal-copine) (n-copine).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005509 calcium ion binding (TAS)
0005215 transporter activity (TAS)
0006629 lipid metabolism (TAS)
0007399 neurogenesis (TAS)
0007268 synaptic transmission (TAS)
0016192 vesicle-mediated transport (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
This represents a conserved region approximately 180 residues long within eukaryotic copines. Copines are Ca2+-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking.nd may also be involved in cell division and growth .
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
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
SequencesProtein: CPNE6_HUMAN (557 aa)
mRNA: NM_006032
Local Annotation
Synapse Ontology
A process that modulates synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
sdb:0035 regulation of synaptic plasticity  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 32 residues, 23610595-23610690Exon2: 59 residues, 23611981-23612153Exon3: 62 residues, 23612547-23612727Exon4: 27 residues, 23613099-23613174Exon5: 27 residues, 23613339-23613414Exon6: 30 residues, 23613579-23613663Exon7: 32 residues, 23613754-23613844Exon8: 37 residues, 23614220-23614325Exon9: 31 residues, 23614553-23614640Exon10: 22 residues, 23614875-23614935Exon11: 46 residues, 23615197-23615331Exon12: 20 residues, 23615408-23615463Exon13: 19 residues, 23615554-23615606Exon14: 46 residues, 23615927-23616061Exon15: 81 residues, 23616202-23616439Exon16: 60 residues, 23616641-23616816Exon17: 68 residues, 23616936-23617135Exon18: 2 residues, -Jump to CPNE6_HUMAN  
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Loci Cluster (Details)Loci: 2827 23633322-23643177 ~-10K 10904(PCK2)(+)Loci: 4123 23748628-23755020 ~-6K 10927(CHMP4A)(-)Loci: 4124 23804585-23810583 ~-6K 10943(RABGGTA)(-)Loci: 2826 23610595-23617135 ~-7K 10902(CPNE6)(+)Link out to UCSC