Primary Information |
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BoMiProt ID | Bomi252 |
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Protein Name | 2',3'-cyclic-nucleotide 3'-phosphodiesterase |
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Organism | Bos taurus |
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Uniprot ID | P06623 |
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Milk Fraction | Whey, MFGM |
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Ref Sequence ID | NP_851336.1 |
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Aminoacid Length | 400 |
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Molecular Weight | 44875 |
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FASTA Sequence |
Download |
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Gene Name | CNP |
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Gene ID | 280752 |
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Protein Existence Status | Reviewed:Experimental evidence at transcript level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | most abundantly
in myelin of oligodendrocytes in the CNS and to a lesser extent
Schwann cells of the PNS |
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Protein Function | hydrolyse 2', 3'-cyclic nucleotides (but not 3',5'-
cyclic nucleotides) in vitro resulting in the production of 2'-
derivatives; enzymic activity associated with mitochondrial
membranes isolated from liver; can interact with the actin-based cytoskeleton; regarded as a specific marker of oligodendrocytes
and Schwann cells and it is clear that the majority
of CNP protein in the developing and adult brain is present in
myelin |
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Biochemical Properties | extrinsic membrane-associated protein,
synthesized on free ribosomes; possesses no obvious hydrophobic domains;not found as a soluble protein
in brain; infused caffeine (a
nonspecific PDE inhibitor |
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Significance in milk | important functional enzyme of the
bovine mammary gland; implicated in
milk fat production; lactation is improved by modulating
the cyclic nucleotide intracellular second messengers which are hydrolyzed into their
inactive form by the phosphodiesterase |
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PTMs | isoprenoid derived from meva-
Ionic acid; only the smaller of the two
CNP isoforms (CNP1) is isoprenylated; C-terminal Cys-Thr-
Ile-Ile (conserved in rat, mouse, bovine, and human CNP)
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | 1-10,296-302,386-388 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | isoprenylation and carboxyl methylation of the cys might account for this property
of CNP; isoprenylation is
permissive for the well-known avid association of
CNP with membrane - Inhibition
of isoprenoid synthesis by Lovastatin blocks the binding
of newly synthesized CNP to cell membranes |
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Additional Comments | mtCNPase is able to regulate the functioning of the mitochondrial permeability transition pore (mPTP), and thus is involved in the mechanisms of cell death, both apoptosis and necrosis. Its participation in the development of various diseases and pathological conditions, such as aging, heart disease and alcohol dependence, is also reviewed. |
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Bibliography | 1. Dostaler-Touchette, V. et al. (2009) ‘Cyclic adenosine monophosphate (cAMP)-specific phosphodiesterase is functional in bovine mammary gland.’, Journal of dairy science, 92(8), pp. 3757–65. doi: 10.3168/jds.2009-2065. 2. McFerran, B. and Burgoyne, R. (1997) ‘2’,3’-Cyclic nucleotide 3’-phosphodiesterase is associated with mitochondria in diverse adrenal cell types.’, Journal of cell science, 110 ( Pt 23), pp. 2979–85. Available at: http://www.ncbi.nlm.nih.gov/pubmed/9359886 (Accessed: 5 October 2019). |