In venomous invertebrates, such as spiders, small proteins rich in cysteine residues and disulfide bonds are known for their function as toxins, often adopt a compact structural fold referred to as the inhibitory cystine knot (ICK), and target a diversity of ion channels and receptors in prey nervous systems. However, small cysteine-rich proteins with disulfide bonds may adopt a range of potential structures beyond the ICK and serve a multiplicity of functions beyond roles as toxins, though these structures and functions remain obscure in spiders. In the common house spider genome, we identified 709 small, cysteine-rich proteins. These proteins exhibited a wide range of predicted disulfide connectivity patterns, indicating the likelihood that they may adopt distinct structural forms. A total of 147 distinct protein domains were identified in these small, cysteine-rich proteins, the most common of which was thyroglobulin, although the majority of domains (94) occurred in only a single protein. Patterns of expression across tissues of small, cysteine-rich house spider proteins were variable, but 143 had strongly biased expression in either the venom gland, the silk gland, or the ovary, with the majority (99) having strongly biased expression in the silk gland. Furthermore, of the 165 small, cysteine-rich proteins that had significant homology to a known toxin, only 10 had strongly biased expression in the venom gland, whereas 61 had strongly biased expression in the silk gland, a pattern which suggests the potential for alternative functions beyond roles as toxins, and as yet undiscovered functions in silk.