A novel member of an ancient superfamily: sponge (Geodia cydonium, Porifera) putative protein that features scavenger receptor cysteine-rich repeats. Proteins featuring scavenger receptor cysteine-rich (SRCR) domains are prominent receptors known from vertebrates and from one phylum of invertebrates, the echinoderms. In the present study we report the first putative SRCR protein from the marine sponge Geodia cydonium (Porifera), a member of the lowest phylum of contemporary Metazoans. Two forms of SRCR molecules were characterized, which apparently represent alternative splicing of the same transcript. The long putative SRCR protein, of 1536 aa, features twelve SRCR repeats, a C-terminal transmembrane domain and a cytoplasmic tail. The sequence of the short form is identical with the long form except that it lacks a coding region near the C terminus, thus the 1195 aa deduced protein consists of only the first ten SRCR domains and the last 26 C-terminal aa residues, without the transmembrane domain. Homology searches revealed that the sponge putative SRCR protein shares with bovine T-cell antigen WC1 29.2% identity in 1054 aa overlap, 33.9% identity in 475 aa overlap with sea urchin speract and 56% identity in 110 aa overlap with macrophage scavenger receptor type I. Based upon the number and location of the conserved Cys residues, the sponge SRCR domain repeats were classified as belonging to group A of the SRCR superfamily. With twelve SRCR repeats, one more than those in any of the previously described SRCR proteins, and several membrane-bound and soluble forms, it seems that the most primitive known member of this family may be the structurally most complex one among SRCR containing proteins.