A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins

Abstract

A group of calcium-binding proteins which bind to biomembranes has recently been identified in widely different cells and tissues (refs 1-7, reviewed in ref. 8). Three of these proteins (p70, p36 and p32.5) cross-react with antiserum to calelectrin, a Ca2+-binding protein (relative molecular mass 34,000 (34K] from the ray Torpedo marmorata, giving rise to their designation as calelectrin-related proteins. We now report that calelectrin, p36 and p32.5 contain a 17-amino-acid consensus sequence which is conserved and present in multiple copies. We suggest that this sequence may be common to other members of this new group of Ca2+-binding proteins and may underlie their unusual mode of combination with biomembranes.

Vascular anticoagulant β: a novel human Ca2+/phospholipid binding protein that inhibits coagulation and phospholipase A2 activity

“…Originally an annexin was defined as a protein that potentiates Ca2 +-dependent aggregation of phospholipid vesicles and/or that contains a particular consensus sequence [31]. Recent determinations of amino acid sequences show that an annexin is structurally organized into a variable Nterminal segment of 18-45 amino acids, preceding a core region consisting of four repeatcd units of 67/68 amino acids, each unit containing the consensus sequence, and being connected via short linker peptides.…”

Membrane‐bound annexin V isoforms (CaBP33 and CaBP37) and annexin VI in bovine tissues behave like integral membrane proteins

“…Each annexin is made of an N-terminal tail of variable length and unique to individual annexins, which is supposed to play a role in the diversification of the biological functions of single species, and of a core. This latter is made of four, in the ease of the 32-37 kDa annexins, or eight, in the case of the 67-73 kDa annexins, internal repeats 70 residues in length, each of which contains a highly conserved consensus sequence, the endonexin fold, which is suggested to take part in the coordination of binding of both Ca 2+ and phospholipids [3][4][5]. Unlike the Ca-'+-binding pro~:eins of the EF-hand type, Ca-'*-binding to annexins does not induce the exposure of hydrophobic domains; rather~ Ca 2. would cross-bridge any annexin to the negatively charged headgroups of acidic phospholipids and/or certain annexins to target proteins [1][2][3].…”

Isolation of two 67 kDa calcium‐binding proteins from pig lung differing in affinity for phospholipids and in anti‐phospholipase A2 activity

“…Greater knowledge of these proteins was recently obtained, mainly through data on their amino acid sequence [3,8,9]. These revealed the existence of two different lipocortins detected respectively as a [35][36][37] [12]. These include 32.5 kDa endonexin, also referred to as protein II, 35 kDa and 67 kDa calelectrins (the latter also called protein III), which are able to modulate aggregation of chromaffin secretory granules (other name: chromobinding [13]).…”