Popeye domain-containing protein 2, also known as Popeye protein 2, is a protein encoded by the POPDC2 gene in humans. This gene encodes the POP family member of proteins that contains three putative transmembrane domains. This membrane-associated protein is mainly expressed in bone and myocardium. The Popeye domain located in the cytoplasmic portion of the protein shows limited sequence homology with other proteins, while in the Popeye protein, the sequence protection rate is high, about 40%-60%.
|Basic Information of POPDC2|
|Protein Name||Popeye domain-containing protein 2|
|Aliases||Popeye protein 2|
|Organism||Homo sapiens (Human)|
Bacterial CAP or CRP proteins, the closest related non-POPDC proteins, act as a circulating nucleotide regulatory transcription factor that regulates the expression of genes that encode enzymes involved in carbohydrate metabolism. The cyclic AMP binding domain of these proteins and the energetic watergate domain showed approximately 25% identity and 60% similarity. There are significant structural similarities between the Popeye domain and the cAMP binding domain of eukaryotic protein kinase A (PKA) and the HCN channel. The genetic inactivation of Popdc2 in mice resulted in mild and chronic arrhythmias, which were heavily dependent on stress. Normal ECG was observed at rest. Gene inactivation in zebrafish also leads to arrhythmia phenotypes and skeletal muscle development defects. Popdc2 is expressed in skeletal muscle and heart. The global loss of popdc2 affects skeletal muscle development, leading to abnormal facial and trunk muscle formation.
Fig.1 The structure of Popeye domain-containing protein 2.
This study reveals that binding these two factors to these overlapping sites is mutually exclusive, which provides a simple tuning mechanism for spatial and temporal synchronization of the common target pool between nkx2-5 and MEIS1.
These results show that this family of cAMP-binding proteins may play multiple roles in striated muscle.
These results suggest that popdc2 is an important gene that is critical for muscle differentiation and cardiac morphogenesis. It is also necessary for the development of the heart conduction system.
This study reveals that the molecular basis of stress bradycardia in Popdc mice will provide new clues to the etiology of cardiac pacemaker disease.
This research identifies a family of membrane-bound cAMP-binding proteins, which regulate the subcellular localization of effector proteins, participate in tissue signaling complexes and ensure proper membrane physiology of cardiomyocytes.
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