The sarcoplasmic-endoplasmic reticulum calcium ATPase (SERCA) is a key intracellular calcium transporter, which regulates cellular calcium concentration [Ca2+] by transporting Ca2+ ions from the cytosol into the endoplasmic reticulum. SERCA-mediated Ca2+ sequestration controls proper folding of newly synthesized proteins within the ER as well as the timing and spatial patterning of depolarization-evoked Ca2+ responses in the cytoplasm. To understand the spatial and temporal properties of Ca2+ homeostasis in retinal neurons better, I studied expression and distribution of all three SERCA isoforms in the mouse retina using isoform-specific antibodies. No immunostaining was observed with the SERCA1 antibody. SERCA2 was expressed in photoreceptor inner segments, amacrine and ganglion cells of the mouse retina. Similar SERCA2 localization was observed in adult rat, macaque and ground squirrel retinas. Analysis of distribution of SERCA2 immunofluorescence in the developing mouse retina revealed prominent SERCA2 signals throughout postnatal development. The N89 antibodys used to identify the SERCA3 isoforms labelled cone outer segments, inner segments of photoreceptors and cell processes in the inner nuclear layer of the mouse retina. These results imply that the SERCA2 isoform controls Ca2+ sequestration into the endoplasmic reticulum in most classes of retinal neuron. A potential role for SERCA3 in cone function is suggested.