Cloned (Comment) | Organism |
---|---|
gene CNP1, two isozymes, which originate from two alternative promoters and 3',5'-cAMP-regulated splicing of one of the mRNA variants produced from the CNP1 gene on chromosome 17 | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
structure analysis | Mus musculus |
structure analysis | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of inactive mutants truncated after amino acid 164 | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | isoform I | Homo sapiens | 5829 | - |
membrane | membrane-anchored enzyme present on the cytosolic side of non-compact myelin | Oryctolagus cuniculus | 16020 | - |
mitochondrion | isoform II, intermembrane space | Homo sapiens | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2',3'-cyclic AMP + H2O | Mus musculus | - |
2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | Homo sapiens | - |
2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | Rattus norvegicus | - |
2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | Oryctolagus cuniculus | - |
2'-AMP | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | Mus musculus | - |
nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | Homo sapiens | - |
nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | Rattus norvegicus | - |
nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | Oryctolagus cuniculus | - |
nucleoside 2'-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
two isozymes, difference between the variants is the presence of a 20-amino-acid N-terminal mitochondrial targeting sequence in the 48-kDa isoform II, which is removed after mitochondrial import to produce a truncated 46-kDa variant that corresponds to the cytosolic isoform I of 400 amino-acids, gene CNP1 | - |
Mus musculus | - |
- |
- |
Oryctolagus cuniculus | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Mus musculus | - |
brain | - |
Homo sapiens | - |
brain | - |
Rattus norvegicus | - |
brain | - |
Oryctolagus cuniculus | - |
myelin membrane | the enzyme is most abundant protein in non-compact myelin and the third-most abundant protein overall in CNS myellin | Homo sapiens | - |
myelin membrane | the enzyme is one of the most abundant proteins in CNS myelin | Mus musculus | - |
myelin membrane | the enzyme is one of the most abundant proteins in CNS myelin | Rattus norvegicus | - |
myelin membrane | the enzyme is one of the most abundant proteins in CNS myelin | Oryctolagus cuniculus | - |
olfactory ensheathing cell | - |
Homo sapiens | - |
peripheral nervous system | - |
Mus musculus | - |
peripheral nervous system | - |
Homo sapiens | - |
peripheral nervous system | - |
Rattus norvegicus | - |
peripheral nervous system | - |
Oryctolagus cuniculus | - |
Schwann cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2',3'-cyclic AMP + H2O | - |
Mus musculus | 2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | - |
Homo sapiens | 2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | - |
Rattus norvegicus | 2'-AMP | - |
? | |
2',3'-cyclic AMP + H2O | - |
Oryctolagus cuniculus | 2'-AMP | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | - |
Mus musculus | nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | - |
Homo sapiens | nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | - |
Rattus norvegicus | nucleoside 2'-phosphate | - |
? | |
nucleoside 2',3'-cyclic phosphate + H2O | - |
Oryctolagus cuniculus | nucleoside 2'-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2',3'-cyclic nucleotide 3'-phosphodiesterase | - |
Mus musculus |
2',3'-cyclic nucleotide 3'-phosphodiesterase | - |
Homo sapiens |
2',3'-cyclic nucleotide 3'-phosphodiesterase | - |
Rattus norvegicus |
2',3'-cyclic nucleotide 3'-phosphodiesterase | - |
Oryctolagus cuniculus |
CNPase | - |
Mus musculus |
CNPase | - |
Homo sapiens |
CNPase | - |
Rattus norvegicus |
CNPase | - |
Oryctolagus cuniculus |
General Information | Comment | Organism |
---|---|---|
evolution | the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms | Mus musculus |
evolution | the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms | Homo sapiens |
evolution | the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms | Rattus norvegicus |
evolution | the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms | Oryctolagus cuniculus |
malfunction | a C-terminally truncated variant of CNPase, as well as a mutant unable to membrane-associate, are affected in oligodendrocyte process outgrowth, formation and branching | Mus musculus |
malfunction | changes in enzyme expression levels are linked to Alzheimer's disease, Down's syndrome, and catatonia-depression syndrome. A single-nucleotide polymorphism that does not alter the amino-acid sequence of the enzyme, but rather decreases its expression levels, has been suggested to play a role in schizophrenia | Homo sapiens |
malfunction | truncations after amino acid 164 in recombinant rat enzyme result in a loss of phosphodiesterase activity | Rattus norvegicus |
additional information | structure of the 2'-cyclic AM-bound enzyme active site and its catalytic mechanism, overview | Mus musculus |
additional information | structure of the CNPase phosphodiesterase domain and its catalytic mechanism, overview | Rattus norvegicus |
physiological function | in early stages of myelination, the enzyme is essential in oligodendrocyte process formation and branching, as well as for oligodendrocyte process outgrowth via its membrane association, as well as its ability to interact with the cytoskeleton. The role of CNPase after active myelination is related to axonal maintenance. Accumulation of 2',3'-cAMP is found in very young CNPase-deficient mice used to study traumatic brain injury, which develops post-traumatic axonal degeneration similar to that of older CNPase-deficient mice that do not experience brain trauma | Mus musculus |
physiological function | the enzyme is possible auto-antigen in multiple sclerosis. CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C. The mitochondrial, fully-processed isoform II does not drive morphological differentiation in cell cultures as isoform I does in oligodendrocytes. The enzyme, together with 2',3'-cAMP, is suggested to modulate the mitochondrial permeability transition, a proapoptotic event, in which Ca2+ is released from the mitochondrial matrix to the intermembrane space and cytoplasm | Homo sapiens |