Secondary literature sources for ANX
The following references were automatically generated.
- Dragani B, Aceto A
- About the role of conserved amino acid residues in the calcium-binding site of proteins.
- Arch Biochem Biophys. 1999; 368: 211-3
- Morgan RO, Fernandez MP
- Expression profile and structural divergence of novel human annexin 31.
- FEBS Lett. 1998; 434: 300-4
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Systematic analysis of expressed sequence tags in dbEST yielded an expression profile of the ten known human annexins and led to the discovery of a novel subfamily expressed mainly in differentiating tissues. Full-length cDNAs encoded a 338-amino acid protein with less than 40% identity to other annexins, an atypical amino acid composition, and an insertion and deletion in internal repeat 3. The most striking feature was a complete ablation of all four type II calcium-binding sites in the conserved tetrad core. Annexin 31 thus constitutes a unique, natural probe for investigating the role of membrane binding in annexin function.
- Morgan RO, Pilar Fernandez M
- Distinct annexin subfamilies in plants and protists diverged prior to animal annexins and from a common ancestor.
- J Mol Evol. 1997; 44: 178-88
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Annexin homologues in the kingdoms of Planta and Protista were characterized by molecular sequence analysis to determine their phylogenetic and structural relationship with annexins of Animalia. Sequence fragments from 19 plant annexins were identified in sequence databases and composite sequences were also assembled from expressed sequence tags for Arabidopsis thaliana. Length differences in protein aminotermini and evidence for unique exon splice sites indicated that plant annexins were distinct from those of animals. A third annexin gene of Giardia lamblia (Anx21-Gla) was identified as a distant relative to other protist annexins and to those of higher eukaryotes, thus providing a suitable outgroup for evolutionary reconstruction of the family tree. Rooted evolutionary trees portrayed protist, plant, and Dictyostelium annexins as early, monophyletic ramifications prior to the appearance of closely related animal annexin XIII. Molecular phylogenetic analyses of DNA and protein sequence alignments revealed at least seven separate plant subfamilies, represented by Anx18 (alfalfa, previously classified), Anx22 (thale cress), Anx23 (thale cress, cotton, rape and cabbage), Anx24 (bell pepper and tomato p34), Anx25 (strawberry, horseradish, pea, soybean, and castor bean), Anx26-Zma, and Anx27-Zma (maize). Other unique subfamilies may exist for rice, tomato p35, apple, and celery annexins. Consensus sequences compiled for each eukaryotic kingdom showed some breakdown of the "annexin-fold" motif in repeats 2 and 3 of protist and plant annexins and a conserved codon deletion in repeat 3 of plants. The characterization of distinct annexin genes in plants and protists reflects their comparable diversity among animal species and offers alternative models for the comparative study of structure-function relationships within this important gene family.
- Hoshino T, Mizutani A, Chida M, Hidaka H, Mizutani J
- Plant annexin form homodimer during Ca(2+)-dependent liposome aggregation.
- Biochem Mol Biol Int. 1995; 35: 749-55
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The annexin (p35) was isolated from the fruits of green pepper (Capsicum annum). The partial amino acid sequence of p35 was analyzed. p35 had an endonexin fold as annexin consensus sequences. Purified p35 had other annexin like characters such as strongly bind to phosphatidylserine and phosphatidylinositol, phospholipase A2 inhibition and liposome aggregation. The zero-length crosslinking assay revealed that p35 formed a homodimer during Ca(2+)-dependent liposome aggregation.
- Morgan RO, Fernandez MP
- Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia.
- Mol Biol Evol. 1995; 12: 967-79
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The homologous repeats of annexin tetrads are believed to have originated by successive duplication and fusion from a putative monomeric precursor, but neither the nature of their ancestor nor the events leading to the formation of different subfamilies have been elucidated. We have performed molecular phylogenetic analysis of aligned annexin nucleotide and amino acids sequences to characterize subfamily branching, to delineate the temporal order of appearance of individual repeat units, and to gain insight into the origin and nature of the primordial unit. All extant annexins appear to have a common tetrad precursor that may have originated from a progenitor unit resembling repeat 3, followed by the generation of repeats 4, 1, and 2 from a more evolved progenitor with subsequent fusion. Repeat sequences of the earliest human annexins VII and XIII were used to identify alpha-giardin genes as primitive homologues from the unicellular protozoan Giardia lamblia, which diverged from eukaryote lineage 1-1.5 billion yr ago. The significant homology between alpha-giardins and annexins suggested that the cell membrane adhesive role of these proteins may be a common, fundamental property of the annexin C-terminal core region. Purported annexin VII of Dictyostelium discoideum was reclassified as new annexin XIV, three Caenorhabditis elegans genes were assigned to new subfamilies XV, XVI, and XVII, and plant annexin XVIII from Medicago sativa was among the earliest diverging subfamilies. Annexins I and II were found to be closely related, but analysis of protein mutation rates confirmed that the former is evolving up to three times more rapidly. The inclusion of early phyla in annexin taxonomy provides a useful basis for assessing the structural and functional changes associated with annexin evolution.
- Flaherty KM, Zozulya S, Stryer L, McKay DB
- Three-dimensional structure of recoverin, a calcium sensor in vision.
- Cell. 1993; 75: 709-16
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Recoverin, a recently discovered member of the EF hand superfamily, serves as a calcium sensor in vision. We report here the crystal structure of recombinant unmyristoylated recoverin at 1.9 A resolution. The four EF hands of the protein are arranged in a compact array that contrasts with the dumbbell shape of calmodulin and troponin C. A calcium ion is bound to EF hand 3, while EF hand 2 can bind samarium but not calcium in this crystal form. The other two EF hands have novel structural features that prevent or impair calcium binding. A concave hydrophobic surface formed by EF hands 1 and 2 may participate in the read out of calcium signals by recoverin and its homologs.
- Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA
- Rat annexin V crystal structure: Ca(2+)-induced conformational changes.
- Science. 1993; 261: 1321-4
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Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.
- Barton GJ, Newman RH, Freemont PS, Crumpton MJ
- Amino acid sequence analysis of the annexin super-gene family of proteins.
- Eur J Biochem. 1991; 198: 749-60
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The annexins are a widespread family of calcium-dependent membrane-binding proteins. No common function has been identified for the family and, until recently, no crystallographic data existed for an annexin. In this paper we draw together 22 available annexin sequences consisting of 88 similar repeat units, and apply the techniques of multiple sequence alignment, pattern matching, secondary structure prediction and conservation analysis to the characterisation of the molecules. The analysis clearly shows that the repeats cluster into four distinct families and that greatest variation occurs within the repeat 3 units. Multiple alignment of the 88 repeats shows amino acids with conserved physicochemical properties at 22 positions, with only Gly at position 23 being absolutely conserved in all repeats. Secondary structure prediction techniques identify five conserved helices in each repeat unit and patterns of conserved hydrophobic amino acids are consistent with one face of a helix packing against the protein core in predicted helices a, c, d, e. Helix b is generally hydrophobic in all repeats, but contains a striking pattern of repeat-specific residue conservation at position 31, with Arg in repeats 4 and Glu in repeats 2, but unconserved amino acids in repeats 1 and 3. This suggests repeats 2 and 4 may interact via a buried saltbridge. The loop between predicted helices a and b of repeat 3 shows features distinct from the equivalent loop in repeats 1, 2 and 4, suggesting an important structural and/or functional role for this region. No compelling evidence emerges from this study for uteroglobin and the annexins sharing similar tertiary structures, or for uteroglobin representing a derivative of a primordial one-repeat structure that underwent duplication to give the present day annexins. The analyses performed in this paper are re-evaluated in the Appendix, in the light of the recently published X-ray structure for human annexin V. The structure confirms most of the predictions and shows the power of techniques for the determination of tertiary structural information from the amino acid sequences of an aligned protein family.
- Pollard HB, Burns AL, Rojas E
- Synexin, a new member of the annexin gene family, is a calcium channel and membrane fusion protein.
- Prog Clin Biol Res. 1990; 349: 159-72
- Moss SE, Crumpton MJ
- Structural and functional investigation of p68--a protein of the lipocortin/calpactin family.
- Adv Exp Med Biol. 1990; 269: 79-83
- Ernst JD, Hoye E, Blackwood RA
- Use of a novel strategy for the preparation and characterization of an antipeptide antibody capable of recognizing members of the annexin family.
- Biochem Biophys Res Commun. 1989; 161: 959-64
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Annexins are structurally-related proteins which bind phospholipids in a Ca2+-dependent manner. We have used a novel coupling strategy to prepare an antiserum directed against a 17-amino acid synthetic peptide that resembles the sequence of a highly-conserved portion of these proteins. This antipeptide serum specifically recognizes 5 of 6 human annexins on Western blots, despite differences between the protein and peptide sequences of 3 or 4 amino acids. The antiserum does not recognize endonexin II, whose sequence differs from that of the peptide by 6 amino acids. The availability of multiple proteins with known amino acid sequence has allowed analysis of structural requirements for recognition by this antibody. In some situations, use of such an antibody may allow the identification of a protein as a member of a family.
- Burgoyne RD, Geisow MJ
- The annexin family of calcium-binding proteins. Review article.
- Cell Calcium. 1989; 10: 1-10
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The annexins are a family of calcium-binding proteins. Data from protein and cDNA sequencing have shown that at least five distinct but closely related mammalian annexins exist each of which possesses four or eight homologous internal repeats which may be calcium-and phospholipid-binding domains. The proteins are present within a wide range of tissues and cell types, with each cell type having all or a subset of the proteins. The proteins are localised on the inner surface of the plasma membrane associated with the cytoskeleton and in some cases also with intracellular structures. Some members of the family are major substrates for tyrosine and serine kinases. The precise functions of the proteins are unknown but they are likely to play important roles in cellular regulation. Previously suggested functions are inhibition of phospholipase A2, membrane-cytoskeletal linkage and control of membrane fusion events in exocytosis. It is also suggested that they may be involved in the regulation of cell surface receptors.
- Schlaepfer DD, Mehlman T, Burgess WH, Haigler HT
- Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein.
- Proc Natl Acad Sci U S A. 1987; 84: 6078-82
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A protein with an apparent Mr of 33,000 was previously purified from the EGTA eluate of a human placental particulate fraction. We now report the amino acid sequence of approximately one-third of this protein and show that it has extensive homology with a newly defined family of Ca2+-binding proteins termed annexins. The partial sequence of the placental protein could be aligned with the sequence of either lipocortin I or calpactin I such that 49% and 58%, respectively, of the residues were identical. A comparison of the partial sequences of the placental protein with the partial sequence of bovine endonexin revealed 74% sequence identity. Based on this close relationship, the placental protein was named endonexin II. Equilibrium dialysis showed that endonexin II bound Ca2+ (Kd greater than 0.5 mM) and the affinity was increased by phosphatidylserine liposomes (kd approximately equal to 100 microM). In addition, endonexin II bound to phosphatidylserine- and phosphatidylethanolamine-containing liposomes in a Ca2+-dependent manner, and the binding was cooperative with respect to Ca2+ concentration (Hill constant greater than 3). The Ca2+- and phospholipid-binding properties of endonexin II raise the possibility that each of the four internally repeated sequences that have been demonstrated within this family of proteins contains a Ca2+-binding site.
