Protein Coiled-coil domain containing 42B

1 protein

1.1 primary sequence & variants/isoforms
1.2 domains , motifs
1.3 post-translational modifications
1.4 secondary structure
1.5 3° , 4° structure

protein

according saps tool, human ccdc42b protein composed of 308 amino acids of 8 exons. mature form of ccdc42b protein has molecular weight of 35.9 kdal (35,914 da). isoelectric point human ccdc42b 7.01, in ccdc42b protein carries no net charge @ particular ph. n-terminal of protein sequence composed of met (m). grand average of hydropathicity predicted -0.694 ccdc42b (human) , -0.398 drosophila melanogaster cg10750, distantly related orthologs. negative gravy confirms both proteins soluble , hydrophilic. theoretical instability index (ii) ccdc42b predicted 63.73 , cg10750 45.20, indicate that, both proteins instable in test tube. half-life of predicted 30 hours both ccdc42b , cg10750 in mammalian reticulocytes (in vitro), correspond half-life enzymes responsible controlling metabolic rate. above results confirmed both ccdc42b , cg10750 share similarities in amino acid composition , protein characteristics. thus, many characteristics of ccdc42b have been conserved across closely , distantly related species.

primary sequence & variants/isoforms

human ccdc42b gene contains 9 introns , 8 different mrna transcripts produced: 4 alternatively spliced variants , 4 un-spliced variants. alternative splicing results in encoding 2 proteins, 3 proteins , 3 non-coding proteins.

domains , motifs

ccdc42b protein of unknown function contains coiled-coil domain of unknown function (duf4200) belongs eukaryote family , located @ range of 34-159 amino acids. duf4200 domain has been conserved in eukaryote. coiled coil structure consists of 2 alpha helices wrapped around each other form twist. heptad repeat pattern (abcdefg)n forms sequence of coiled coil structure, , d hydrophobic, e , g polar of charged.

post-translational modifications

expasy proteomics tool used analyze post-transcriptional modifications of ccdc42b protein. human ccdc42b n-terminus acetylation (a2) corresponded in 5 out of 6 orthologs. drosophila has no ala, gly, ser or thr @ position 1-3, n-terminus acetylation conserved in human ccdc42b. human ccdc42b protein has conserved sumoylation site, since lysine (k) @ position 285 conserved in 5 out of 6 orthologs, closely related organisms showed conservation of lysine. phosphorylation events occur in ccdc42b, suggested involved in signaling pathways. human ccdc42b phosphorylation site of tyrosine @ position 8 (y8) conserved in 6 orthologs species (the site corresponded sulfation site). other phosphorylation sites in human ccdc42b protein conserved in orthologs (illustrated in multiple sequence alignment). same amino acid residues in human ccdc42b protein subjected competing phosphorylation , o-linked glycosylation.however, glycosylation sites occur in serine , threonine residues phosphorylated serine/ threonine kinases. thus, phosphorylation of ser/thr residues prevent o-glcnac processing. human ccdc42b protein has conserved gpi-modification site of alanine (a) @ position 293 conserved in 4 out of 6 orthologs.

post-transcriptional modification.



secondary structure

ccdc42b protein form secondary structure based upon alpha-helices. structure of ccdc42b predicted contain several alpha-helices, , other random coils. hairpin loop structures detected @ 5 utr , 3 utr region of ccdc42b. also, leucine zipper domain found overlapping coiled-coil domain. attached image shows comparison between human ccdc42b , 5 other orthologs species supports human ccdc42b composed of alpha helices secondary structure.

3° , 4° structure

according cblast, ccdc42b protein sequence aligned 2i1k_a (chain a, moesin spodoptera frugiperda reveals coiled-coil domain @ 3.0 angstrom resolution), , e-value of 1.00e-03 obtained. aligned sequences 164-243 aa ccdc42b, , 302-381 aa 2i1k_a resulted in 22% identity between both sequences in 80 amino acid residues.the structure shows aligned sequence of ccdc42b 2i1k_a. predicted structure (blue: not similar residues, red: conserved residues, gray: not aligned ccdc42b residues 2i1k_a).