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Comparison of four regions in the replicase gene of heterologous infectious bronchitis virus strains.

Infectious bronchitis virus (IBV) produces six subgenomic (sg) mRNAs, each containing a 64 nucleotide (nt) leader sequence, derived from the 5' end of the genome by a discontinuous process. Several putative functional domains such as a papain-like proteinase (PL(pro)), main protease (M(pro)), RNA-dependent RNA polymerase (RdRp), and RNA helicase encoded by the replicase gene are important for virus replication. We have sequenced four regions of the replicase genes corresponding to the 5'-terminal sequence, PL(pro), M(pro), and RdRp domains from 20 heterologous IBV strains, and compared them with previously published coronavirus sequences. All the coronavirus 5'-termini and PL(pro) domains were divergent, unlike the M(pro) and the RdRp domains that were highly conserved with 28% and 48% conserved residues, respectively. Among IBV strains, the 5' untranslated region including the leader sequence was highly conserved (>94% identical); whereas, the N-terminal coding region and the PL(pro) domains were highly variable ranging from 84.6% to 100%, and 77.6% to 100% identity, respectively. The IBV M(pro) and RdRp domains were highly conserved with 82.7% and 92.7% conserved residues, respectively. The BJ strain was the most different from other IBVs in all four regions of the replicase. Phylogeny-based clustering based on replicase genes was identical to the antigen-based classification of coronaviruses into three groups. However, the IBV strain classification based on replicase gene domains did not correlate with that of the type-specific antigenic groups. The replicase gene sequences of many IBVs recovered from infected chickens were identical to those of vaccine viruses irrespective of serotype, suggesting that either there has been an exchange of genetic material among vaccine and field isolates or that there is a convergent evolution to a specific replicase genotype. There was no correlation between the genotype of any region of the replicase gene and pathotype, suggesting that the replicase is not the sole determinant of IBV pathogenicity.

5' Untranslated Regions↗

Interphotoreceptor retinoid-binding protein--an old gene for new eyes.

Evolving 40 times independently, eyes are striking examples of convergent evolution in that 11-cis retinaldehyde is always used for photon capture, yet the mechanism for its regeneration may be dramatically different in between systems. In particular, insects, cephalopods and vertebrates show varying physical separation of the cis-->trans photoisomerization and chromphore reisomerization. In the vertebrate retina, these two processes are actually distributed between different cells. This compartmentalization is made possible by the phylogenetic innovation of the two-layered optic cup of the vertebrate retina. This unprecedented design created the subretinal space as a novel anatomical compartment allowing photoreceptors access to the retinal pigment epithelium (RPE) and Müller cells, the two cell types which share the burden of 11-cis retinoid regeneration. To take advantage of this arrangement, early vertebrates appear to have recruited for retinoid binding, the betabetaalpha-spiral fold proven useful in enoyl-CoA isomerase/hydratases, and the carboxy-terminal proteases for stabilizing hydrophobic ligands. Quadruplication of this functional domain within a single polypeptide lead to the emergence of interphotoreceptor retinoid-binding protein (IRBP). IRBP is the main soluble component of the IPM, and is prevented from diffusing out of the subretinal space because its large size excludes it from the photoreceptor/Müller cell zonulae adheretes. Despite this physical entrapment, IRBP is rapidly turned over within the IPM through a process that coordinates secretion of the protein by the photoreceptors, and its removal from the matrix by RPE and photoreceptor endocytosis. The present review will summarize what is known about the structure and function of IRBP to anticipate future avenues of research.

Animals↗

Compensation for longitudinal chromatic aberration in the eye of the firefly squid, Watasenia scintillans.

The camera eyes of fishes and cephalopods have come forth by convergent evolution. In a variety of vertebrates capable of color vision, longitudinal chromatic aberration (LCA) of the optical system is corrected for by the exactly tuned longitudinal spherical aberration (LSA) of the crystalline lens. The LSA leads to multiple focal lengths, such that several wavelengths can be focused on the retina. We investigated whether that is also the case in the firefly squid (Watasenia scintillans), a cephalopod species that is likely to have color vision. It was found that the lens of W. scintillans is virtually free of LSA and uncorrected for LCA. However, the eye does not suffer from LCA because of a banked retina. Photoreceptors sensitive to short and long wavelengths are located at appropriate distances from the lens, such that they receive well-focused images. Such a design is an excellent solution for the firefly squid because a large area of the retina is monochromatically organized and it allows for double use of the surface area in the dichromatically organized part of the retina. However, it is not a universal solution since compensation for LCA by a banked retina requires that eye size and/or spectral separation between photopigments is small.

Animals↗

A molecular phylogeny of the Percidae (Teleostei, Perciformes) based on mitochondrial DNA sequence.

The family Percidae is among the most speciose families of northern hemisphere fishes with > 178 178 North American species and 14 Eurasian species. Previous phylogenetic studies have been hampered by a lack of informative characters, inadequate taxonomic sampling, and conflicting data. We estimated phylogenetic relationships among 54 percid species (9 of 10 genera and all but one subgenus of darters) and four outgroup taxa using mitochondrial DNA data from the 12S rRNA and cytochrome b genes. Four primary evolutionary lineages were consistently recovered: Etheostomatinae (Ammocrypta, Crystallaria, Etheostoma, and Percina), Perca, Luciopercinae (Romanichthys, Sander, and Zingel), and Gymnocephalus. Except Etheostoma and Zingel, all polytypic genera were monophyletic. The Etheostoma subgenus Nothonotus failed to resolve with other members of the genus resulting in a paraphyletic Etheostoma. The subfamily Percinae (Gymnocephalus and Perca) was not recovered in phylogenetic analyses with Gymnocephalus sister to Luciopercinae. Etheostomatinae and Romanichthyini were never resolved as sister groups supporting convergent evolution as the cause of small, benthic, stream-inhabiting percids in North American and Eurasian waters.

Animals↗

Unraveling evolutionary lineages in the limbless fossorial skink genus Acontias (Sauria: Scincidae): are subspecies equivalent systematic units?

Subspecies in the limbless, endemic African fossorial skink genus Acontias constitute ill-defined operational taxonomic units, consequently considerable systematic debate has lingered on the systematic diversity within Acontias. In the present study, the systematic affinities among acontine taxa are explored with the utility of partial sequence data from two mitochondrial gene loci (16S rRNA and cytochrome oxidase subunit 1 (COI)) for all taxa, while two additional loci (12S rRNA, cytochrome b) were used to investigate relationships within the Acontias meleagris complex. Phylogenetic results, derived from the combined analysis, revealed two monophyletic clades. Clade 1 is comprised of small-bodied skinks while clade 2 comprised the medium bodied skinks. Within clade 2 none of the traditionally recognized subspecies formed reciprocally monophyletic groups. Furthermore, constraining the topology and enforcing sister taxa relationships between the assumed subspecies, consistently recovered a topology that was statistically significant worse, indicating that the traditionally designated subspecies groupings probably represent invalid taxonomic units, thus clearly reflecting considerable discord with current taxonomy. The burrowing life style of these lizards has probably led to marked convergent evolution and constrained the development of diagnostic morphological characters among these species. Morphological similarities in color as well as scale architecture within Acontias are labile and highly homoplaseous and do not reflect the evolutionary history of the group. Taxonomic implications of these results are discussed.

Animals↗

Phylogeny of eagles, Old World vultures, and other Accipitridae based on nuclear and mitochondrial DNA.

We assessed phylogenetic relationships for birds of prey in the family Accipitridae using molecular sequence from two mitochondrial genes (1047 bases ND2 and 1041 bases cyt-b) and one nuclear intron (1074 bases beta-fibrinogen intron 7). We sampled representatives of all 14 Accipitridae subfamilies, focusing on four subfamilies of eagles (booted eagles, sea eagles, harpy eagles, and snake eagles) and two subfamilies of Old World vultures (Gypaetinae and Aegypiinae) with nearly all known species represented. Multiple well-supported relationships among accipitrids identified with DNA differ from those traditionally recognized based on morphology or life history traits. Monophyly of sea eagles (Haliaeetinae) and booted eagles (Aquilinae) was supported; however, harpy eagles (Harpiinae), snake eagles (Circaetinae), and Old World vultures were found to be non-monophyletic. The Gymnogene (Polyboroides typus) and the Crane Hawk (Geranospiza caerulescens) were not found to be close relatives, presenting an example of convergent evolution for specialized limb morphology enabling predation on cavity nesting species. Investigation of named subspecies within Hieraaetus fasciatus and H. morphnoides revealed significant genetic differentiation or non-monophyly supporting recognition of H. spilogaster and H. weiskei as distinctive species.

Animals↗

Phylogenetic relationships and divergence time estimate of African anguilliform catfish (Siluriformes: Clariidae) inferred from ribosomal gene and spacer sequences.

The catfish family Clariidae comprises species in which the body shape ranges from fusiform to anguilliform. Recent studies have shown that this body elongation is the result of convergent evolution. This paper aims to study the evolution towards anguilliformity in a phylogenetic framework. Sequences of 29 taxa were analyzed using the neighbor-joining, maximum-likelihood, maximum-parsimony, and Bayesian inference algorithms and the parsimony algorithm in POY. The study yields phylogenetic hypotheses showing well-supported clades. Anguilliformity appears to have arisen at least four times, each time having a sister group relation with a fusiform Clarias-like ancestor. Divergence time estimation indicates that the African Clariidae started radiating between 123 and 56 My ago.

Africa↗

A multidisciplinary approach reveals cryptic diversity in Western Palearctic Tetramorium ants (Hymenoptera: Formicidae).

Diversity of ants of the Tetramorium caespitum/impurum complex was investigated in a multidisciplinary study. Focusing on morphologically hardly distinguishable Western Palearctic samples, we demonstrate the genetic and phenotypic diversity, demarcate phylogenetic entities, and discuss the clades in terms of biogeography. Sequences of 1113bp of the mitochondrial COI gene revealed 13 lineages. COII data, worker morphometry and male genitalia morphology corroborated the COI results for seven lineages; the remaining six were disregarded because of small sample size. A comparison with published data on cuticular hydrocarbons showed correspondence. The seven entities show different distribution patterns, though some ranges overlap in Central Europe. Since no major discrepancy between the results of the different disciplines became apparent, we conclude that the seven entities within the T. caespitum/impurum complex represent seven species. Geographical evidence allows the identification of T. caespitum and T. impurum, and we therefore designate neotypes and redescribe the two species in terms of morphology and mtDNA. As the revision of about 50 taxon names would go beyond the scope of this study, we refer to the remaining five species under code names. We discuss our findings in terms of plesiomorphy and convergent evolution by visualizing the mtDNA phylogeny in morphological space.

Animals↗

The Petrolisthes galathinus complex: species boundaries based on color pattern, morphology and molecules, and evolutionary interrelationships between this complex and other Porcellanidae (Crustacea: Decapoda: Anomura).

While the amphi-American porcellanid crab Petrolistes galathinus has been traditionally viewed as a highly variable species containing several different color forms, we consider it to be a complex of at least 6 morphologically similar species with similar ecological requirements, but diagnosable through coloration. Here we surveyed sequence variation of the mitochondrial 16S rRNA gene, compared the morphology of adults and of the first larval stage (Zoea I), and explored shape variation of the sternal plate using geometric morphometric methods, to investigate boundaries among the species in the complex, and to confirm the validity of color and color pattern for distinguishing them. Sequences and larval morphological characters of other porcellanids were included to investigate the correspondence between genetic divergence and morphology of adults and larvae. The molecular and morphometric results support the validity of the species in the complex, and of color pattern for their distinction. The close relationship between the complex and the putative ancenstral porcellanid Parapetrolisthes tortugensis was indicated by the molecular and larval-morphology results. The adult morphology of this species is interpreted as a result of convergent evolution driven by a relatively rapid ecological adaptation to conditions in deeper waters. The nesting position in the phylogenetic trees of Petrocheles australiensis outside the Porcellanidae clade questions the monophyly of this family.

Animals↗

Microscopical evaluation of the crystalline lens of the squid (Loligo opalescens) during embryonic development.

The similarity between the cephalopod lens and the teleost (vertebrate) lens can be considered an optical example of convergent evolution. However, the embryology and ultrastructure of the cephalopod lens appear to be different from that of vertebrates, and perhaps unique to the animal kingdom. Using light and scanning electron microscopy, the morphogenesis of the squid (Loligo opalescens) lens is characterized. Results indicate that the posterior lens primordium appears first during development and is derived from cellular processes which extend from a middle group, group 2, of lentigenic (ectodermal) cells. The processes extend from the basal aspect of the lentigenic cells, project down into the optic vesicle during early stages of development, and fuse to form the posterior lens primordium. During later stages, the processes extend from surrounding lentigenic cells and are applied to the stalk of the lens, where they form bud-shaped protrusions. Once applied to the lens, the processes form lens elements that later fuse into plate-like elements evident in later-staged embryo and adult lenses. The anterior lens primordium is derived from an anterior group, group 1, of lentigenic cells, during later stages of development. Lentigenic processes extend from these lentigenic cells and are laid down in a circumferential fashion to form the anterior lens cap. As in the posterior lens, evidence indicates that the anterior lens elements fuse to form plate-like elements. The ultrastructure and morphogenesis of the cephalopod lens is discussed and contrasted with other strategies of lens development.

Animals↗

A novel plant alpha4-fucosyltransferase (Vaccinium myrtillus L.) synthesises the Lewis(a) adhesion determinant.

We have partially characterised an alpha4-fucosyltransferase (alpha4-FucT) from Vaccinium myrtillus, which catalysed the biosynthesis of the Lewis(a) adhesion determinant. The enzyme was stable up to 50 degrees C. The optimum pH was 7.0, both in the presence and in the absence of Mn(2+). The enzyme was inhibited by Mn(2+) and Co(2+), and showed resistance towards inhibition with N-ethylmaleimide. It transferred fucose to N-acetylglucosamine in the type I Galbeta3GlcNAc motif from oligosaccharides linked to a hydrophobic tail and glycoproteins (containing the type I motif). Sialylated oligosaccharides containing the type II Galbeta4GlcNAc motif were not acceptors. The catalytic mechanism of the plant alpha4-FucT possibly involves a His residue, and it must have arisen by convergent evolution relative to its mammalian counterparts.

Cell Adhesion↗

Obligate intracellular parasites: Rickettsia prowazekii and Chlamydia trachomatis.

Transitions to obligate intracellular parasitism have occurred at numerous times in the evolutionary past. The genome sequences of two obligate intracellular parasites, Rickettsia prowazekii and Chlamydia trachomatis, were published last year. A comparative analysis of these two genomes has revealed examples of reductive convergent evolution, such as a massive loss of genes involved in biosynthetic functions. In addition, both genomes were found to encode transport systems for ATP and ADP, not otherwise found in bacteria. Here, we discuss adaptations to intracellular habitats by comparing the information obtained from the recently published genome sequences of R. prowazekii and C. trachomatis.

Animals↗

Sequence and structure classification of kinases.

Kinases are a ubiquitous group of enzymes that catalyze the phosphoryl transfer reaction from a phosphate donor (usually ATP) to a receptor substrate. Although all kinases catalyze essentially the same phosphoryl transfer reaction, they display remarkable diversity in their substrate specificity, structure, and the pathways in which they participate. In order to learn the relationship between structural fold and functional specificities in kinases, we have done a comprehensive survey of all available kinase sequences (>17,000) and classified them into 30 distinct families based on sequence similarities. Of these families, 19, covering nearly 98% of all sequences, fall into seven general structural folds for which three-dimensional structures are known. These fold groups include some of the most widespread protein folds, such as Rossmann fold, ferredoxin fold, ribonuclease H fold, and TIM beta/alpha-barrel. On the basis of this classification system, we examined the shared substrate binding and catalytic mechanisms as well as variations of these mechanisms in the same fold groups. Cases of convergent evolution of identical kinase activities occurring in different folds are discussed.

Amino Acid Sequence↗

Structure and function of 3 alpha-hydroxysteroid dehydrogenase.

Mammalian 3 alpha-hydroxysteroid dehydrogenases (3 alpha-HSDs) inactivate circulating steroid hormones, and in target tissues regulate the occupancy of steroid hormone receptors. Molecular cloning indicates that 3 alpha-HSDs are members of the aldo-keto reductase (AKR) superfamily and display high sequence identity (> 60%). Of these, the most extensively characterized is rat liver 3 alpha-HSD. X-ray crystal structures of the apoenzyme and the E.NADP+ complex have been determined and serve as structural templates for other 3 alpha-HSDs. These structures reveal that rat liver 3 alpha-HSD adopts an (alpha/beta)8-barrel protein fold. NAD(P)(H) lies perpendicular to the barrel axis in an extended conformation, with the nicotinamide ring at the core of the barrel, and the adenine ring at the periphery of the structure. The nicotinamide ring is stabilized by interaction with Y216, S166, D167, and Q190, so that the A-face points into the vacant active site. The 4-pro-(R) hydrogen transferred in the oxidoreduction of steroids is in close proximity to a catalytic tetrad that consists of D50, Y55, K84, and H117. A water molecule is within hydrogen bond distance of H117 and Y55, and its position may mimic the position of the carbonyl of a 3-ketosteroid substrate. The catalytic tetrad is conserved in members of the AKR superfamily and resides at the base of an apolar cleft implicated in binding steroid hormone. The apolar cleft consists of a side of apolar residues (L54, W86, F128, and F129), and opposing this side is a flexible loop that contains W227. These constraints suggest that the alpha-face of the steroid would orient itself along that side of the cleft containing W86. Site-directed mutagenesis of the catalytic tetrad indicates that Y55 and K84 are essential for catalysis. Y55S and Y55F mutants are catalytically inactive, but still form binary (E.NADPH) and ternary (E.NADH.Testosterone) complexes; by contrast K84R and K84M mutants are catalytically inactive, but do not bind steroid hormone. The reliance on a Tyr/Lys pair is reminiscent of catalytic mechanisms proposed for other AKR members as well as for HSDs that belong to the short-chain dehydrogenase/reductase (SDR) family, in which Tyr is the general acid, with its pKa being lowered by Lys. Superimposition of the nicotinamide rings in the structures of 3 alpha-HSD (an AKR) and 3 alpha, 20 beta-HSD (an SDR) show that the Tyr/Lys pairs are positionally conserved, suggesting convergent evolution across protein families to a common mechanism for HSD catalysis. W86Y and W227Y mutants bind testosterone to the E.NADH complex, with effective increases in Kd of 8- and 20-fold. These data provide the first evidence that the side of the apolar cleft containing W86 and the opposing flexible loop containing W227 are parts of the steroid-binding site. Detailed mutagenesis studies of the apolar cleft and elucidation of a ternary complex structure will ultimately provide details of the determinants that govern steroid hormone recognition. These determinants could provide a rational basis for structure-based inhibitor design.

3-Hydroxysteroid Dehydrogenases↗

Helicoidal architecture of fish eggshell.

Previous publications show arced patterns in electron micrographs of either microfibrils or canals in sectioned fish eggshells, but these have been misinterpreted. We show here that such patterns in the inner layer of cod (Gadus morrhua), plaice (Pleuronectes platessa) and trout (Salmo gairdneri) eggs arise from a helicoidal structure. This consists of a laminate of protein microfibrils, with the direction of ply processing like the steps of a spiral staircase and with the same sense as a left-handed corkscrew. Mechanically, this is an ideal way to strengthen a spherical shell, to resist deforming forces equally from any direction. Radial canals which traverse this layer are forced into flattened and twisted ribbons. Both the helicoidal microfibrillar structure and the canal shape in fish eggshells show remarkable convergent evolution with similar structures in insect cuticles. Trout eggs were resistant to deforming forces as high as 380,000 N/m2. Fish eggshells, like those of many other organisms, are mechanically well designed.

Animals↗

A wide-angle gradient index optical model of the crystalline lens and eye of the octopus.

Cephalopods and fish have had no common ancestor since the Cambrian, and their eyes are a classic example of convergent evolution. The octopus has no cornea, and immerson renders the trout cornea optically ineffective. As a result, the nearly spherical lens is responsible for all refraction in these eyes. In spite of the fact that the octopus lens consists of two joined parts, while the trout lens consists of one part, we show here that their optical properties are very similar. An index gradient bends rays within these lenses, adding power and correcting spherical aberration. High spherical symmetry in both lenses strongly reduces other monochromatic aberrations and yields a wide field of vision, advantageous in attack and evasion. The octopus Mattheissen's ratio, 2.83, an inverse measure of light-gathering power, lies above the trout value of 2.38 but within the range of values reported for fish. Strong uncorrected longitudinal chromatic aberration is nearly identical in both animals as a result of similar lens protein optical properties, and will limit resolution. We discuss how animal lifestyle requirements and lens material properties influence the design of these eyes.

Accommodation, Ocular↗

Tailed bacteriophages: the order caudovirales.

Tailed bacteriophages have a common origin and constitute an order with three families, named Caudovirales. Their structured tail is unique. Tailed phages share a series of high-level taxonomic properties and show many facultative features that are unique or rare in viruses, for example, tail appendages and unusual bases. They share with other viruses, especially herpesviruses, elements of morphogenesis and life-style that are attributed to convergent evolution. Tailed phages present three types of lysogeny, exemplified by phages lambda, Mu, and P1. Lysogeny appears as a secondary property acquired by horizontal gene transfer. Amino acid sequence alignments (notably of DNA polymerases, integrases, and peptidoglycan hydrolases) indicate frequent events of horizontal gene transfer in tailed phages. Common capsid and tail proteins have not been detected. Tailed phages possibly evolved from small protein shells with a few genes sufficient for some basal level of productive infection. This early stage can no longer be traced. At one point, this precursor phage became perfected. Some of its features were perfect enough to be transmitted until today. It is tempting to list major present-day properties of tailed phages in the past tense to construct a tentative history of these viruses: 1. Tailed phages originated in the early Precambrian, long before eukaryotes and their viruses. 2. The ur-tailed phage, already a quite evolved virus, had an icosahedral head of about 60 nm in diameter and a long non-contractile tail with sixfold symmetry. The capsid contained a single molecule of dsDNA of about 50 kb, and the tail was probably provided with a fixation apparatus. Head and tail were held together by a connector. a. The particle contained no lipids, was heavier than most viruses to come, and had a high DNA content proportional to its capsid size (about 50%). b. Most of its DNA coded for structural proteins. Morphopoietic genes clustered at one end of the genome, with head genes preceding tail genes. Lytic enzymes were probably coded for. A part of the phage genome was nonessential and possibly bacterial. Were tailed phages general transductants since the beginning? 3. The virus infected its host from the outside, injecting its DNA. Replication involved transcription in several waves and formation of DNA concatemers. Novel phages were released by burst of the infected cell after lysis of host membranes by a peptidoglycan hydrolase (and a holin?). a. Capsids were assembled from a starting point, the connector, and around a scaffold. They underwent an elaborate maturation process involving protein cleavage and capsid expansion. Heads and tails were assembled separately and joined later. b. The DNA was cut to size and entered preformed capsids by a headful mechanism. 4. Subsequently, tailed phages diversified by: a. Evolving contractile or short tails and elongated heads. b. Exchanging genes or gene fragments with other phages. c. Becoming temperate by acquiring an integrase-excisionase complex, plasmid parts, or transposons. d. Acquiring DNA and RNA polymerases and other replication enzymes. e. Exchanging lysin genes with their hosts. f. Losing the ability to form concatemers as a consequence of acquiring transposons (Mu) or proteinprimed DNA polymerases (phi 29). Present-day tailed phages appear as chimeras, but their monophyletic origin is still inscribed in their morphology, genome structure, and replication strategy. It may also be evident in the three-dimensional structure of capsid and tail proteins. It is unlikely to be found in amino acid sequences because constitutive proteins must be so old that relationships were obliterated and most or all replication-, lysogeny-, and lysis-related proteins appear to have been borrowed. However, the sum of tailed phage properties and behavior is so characteristic that tailed phages cannot be confused with other viruses.

Caudovirales↗

Type 3 inositol 1,4,5-trisphosphate receptor and capacitative calcium entry.

It is well established that depletion of intracellular stores of calcium can activate calcium influx across the plasma membrane, a process known as "capacitative calcium entry'. Recent research and reviews have focussed on homologs of the Drosophila mutant, trp, as candidates for the channels underlying this phenomenon. However, there is recent evidence that the type 3 inositol 1,4,5-trisphosphate {(1,4,5)IP3} receptor can also function as a capacitative calcium entry channel, specifically: (i) in some cell types, the properties of Ca2+ store depletion-activated currents and channels resemble those of an (1,4,5)IP3 receptor;(ii) in these same cell types, (1,4,5)IP3 directly activates channels in the plasma membrane (including in one study, the same channels activated by depletion of Ca2+ stores); and (iii) expression of the type 3 receptor in Xenopus oocytes resulted in the association of this receptor with the plasma membrane, and facilitation of Ca2+ entry across the plasma membrane. The type 3 receptor may represent one type of capacitative calcium entry channel expressed in some cell types and, in other cell types, channels with markedly different properties (i.e. trp) may carry out this function. Furthermore, as there is little, if any, homology between the IP3 and trp protein families, this may represent an example of convergent evolution of function.

Animals↗