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. 2000 Mar 6;148(5):1047–1062. doi: 10.1083/jcb.148.5.1047

Figure 1.

Sequence analysis of SdpII. a, The amino acid sequence of the shortest and the longest of the four splice variants of the novel rat proteins SdpII, SdpII-s, and SdpII-l, respectively, is shown aligned to SdpI (GenBank/EMBL/DDBJ accession number AF104402), the chicken protein FAP52 (GenBank/EMBL/DDBJ accession number Z50798), and murine PACSIN 2 (GenBank/EMBL/DDBJ accession number AAD41780). Boxes indicate residues of ≥80% identity between all five sequences. b, Schematic cartoon of the domain structure of SdpII. Members of the syndapin protein family share a similar domain structure with a highly conserved SH3 domain at the COOH terminus, two predicted coiled coil domains, and several NPF motifs. The multidomain protein is alternatively spliced at at least two different sites (amino acids 303–304 and/or amino acids 346–386 of SdpII-l). c, Comparison of sequence identities between SdpII and related proteins. The COOH-terminal SH3 domain, corresponding to amino acids 430–488 in SdpII-l, represents the part of the protein that is most highly conserved between members of the syndapin protein family. These sequence data for SdpII are available from GenBank/EMBL/DDBJ under accession numbers AF139492, AF139493, AF139494, and AF139495.