Introduction of CATSPERD
CATSPERD is also known as CATSPERδ. Mouse CATSPERδ encoded by tmem146-l is predicted to be 805 amino acids in length with a predicted molecular weight of 91 kDa (pI 6.68). Hydrophilicity plots of mouse and human CATSPERδ suggest that mouse CATSPERδ has one signal peptide, a large extracellular domain of 699 amino acids followed by a transmembrane-spanning domain and ending in an intracellular tail of 60 amino acids. The predicted transmembrane topology is similar to CATSPERγ. The amino acid sequence of mouse CATSPERδ is not similar to any other protein with known function. CATSPER α, β and γ subunits have the same evolutionary pattern; their orthologs are present in the genomes of mammals, as well as sea squirts (Ciona intestinalis), and sea urchins (Strongylocentrotus purpuratus). In contrast, CatSperδ orthologues are found only in mammals and a reptile (Anolis carolinensis, a green lizard), implying that CatSperδ imparts a species-specific function.
|Basic Information of CATSPERD|
|Protein Name||Cation channel sperm-associated protein subunit delta|
|Aliases||CatSper-delta, CatSperdelta, Transmembrane protein 146|
|Organism||Homo sapiens (Human)|
Function of CATSPERD Membrane Protein
CatSperβ, γ, and δ mRNAs appear in unison 6d before CatSperα subunit mRNAs in young mice. In mice lacking CatSperδ, CATSPERβ and CATSPERγ form a stable complex while CATSPER1 is substantially reduced, suggesting that CATSPERδ is important for the stability of CATSPER1 and CATSPER complex formation. Most importantly, CatSperδ-null mice spermatozoa lack ICatSper, fail to hyperactivate, and are infertile, demonstrating that CATSPERδ is required for proper CATSPER complex formation and ion channel function.
Application of CATSPERD Membrane Protein in Literature
In this article, the authors show that CATSPERδ is an essential element of the CATSPER channel complex and propose that CATSPERδ is required for proper CATSPER channel assembly and/or transport.
This article reviews the recent results of studying CatSper functional properties. In order to achieve a deep understanding of the molecular basis of CatSper function, further studies are required to do.
In this paper, the expression, localization, structure and regulation of CatSper protein and its effect on sperm activation and male reproduction were reviewed.
This study suggests that [Ca2+]i homeostasis is regulated by PKA-dependent phosphorylation by activating CatSper channel complexes.
CATSPERD Preparation Options
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