FIG. 2.

Sequence of DEF-1. (A) Eight unique, overlapping clones were used to obtain the DEF-1 composite sequence. One clone (R19) lacked the sequence SRR at amino acids 304 to 306. The sequence from other clones and an apparent human DEF-1 partial sequence in the EST database suggested that the SRR sequence is an alternative exon (data not shown). The number of the last amino acid in a line is noted on the right. Key: overline, peptide sequenced; underline, putative alternative exon; aqua, pleckstrin homology domain (amino acids 326 to 419); purple, zinc finger (amino acids 457 to 480); red, C2 domain (amino acids 498 to 557); yellow, ankyrin-related motifs (amino acids 604 to 623, 640 to 659, 673 to 692); green, SH3 consensus binding sequences (amino acids 791 to 800, 803 to 809, 828 to 835, 895 to 901, 993 to 999); brown, proline-rich repeat (amino acids 934 to 1001); blue, SH3 domain (amino acids 1074 to 1123). (B) Putative structure of proline-rich motif in DEF-1. The sequence of amino acids 976 to 1001 is drawn in a left-handed poly-proline type II helix. Standard amino acid abbreviations are used.