Search by BoMiProt ID - Bomi252


Primary Information

BoMiProt ID Bomi252
Protein Name 2',3'-cyclic-nucleotide 3'-phosphodiesterase
Organism Bos taurus
Uniprot IdP06623
Milk FractionWhey, MFGM
Ref Sequence Id NP_851336.1
Amino Acid Lenth 400
Molecular Weight 44875
Fasta Sequence https://www.uniprot.org/uniprot/P06623.fasta
Gene Name CNP
Gene Id 280752
Protein Existence Status Reviewed:Experimental evidence at transcript level

Secondry Information

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
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
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
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
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)
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
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).