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Am J Physiol Gastrointest Liver Physiol 282: G702-G710, 2002. First published January 9, 2002; doi:10.1152/ajpgi.00458.2001
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Vol. 282, Issue 4, G702-G710, April 2002

An evolutionarily ancient Oatp: insights into conserved functional domains of these proteins

Shi-Ying Cai1, Wei Wang2, Carol J. Soroka1, Nazzareno Ballatori2,3, and James L. Boyer1,3

1 Liver Center, Yale University School of Medicine, New Haven, Connecticut 06520; 2 Department of Environmental Medicine, University of Rochester School of Medicine, Rochester, New York 14642; and 3 Mt. Desert Island Biological Laboratory, Salsbury Cove, Maine 04672

Cellular uptake of organic solutes is mediated in large part by a gene family of membrane transporters called OATPs (SLC21A). To study the structural determinants and evolutionary development of the SLC21A family, we have cloned and functionally characterized a highly expressed evolutionarily primitive Oatp from the liver of the small skate, Raja erinacea. A full-length cDNA (2.3 kb) was obtained that encodes a protein of 689 amino acids. The characteristics of this novel skate Oatp, including tissue expression, subcellular localization, substrate selectivity, Na+ dependence, and inhibitor selectivity were generally similar to liver-specific human OATP-C and rat Oatp4. However, sequence comparisons with other OATPs indicate that this skate Oatp shares only ~40-50% amino acid identity with the liver-specific OATPs/Oatps and with human OATP-F. Further computer analysis revealed that the highest amino acid identities reside in the first external (78%) and internal loops (75%) and transmembrane domains 2 (76%), 3 (62%), 4 (70%), and 11 (64%). We propose that the conserved regions of the SLC21A transporter family may be critical structural determinants of substrate specificity and function.

skate Oatp; transporter; evolution; hepatic uptake


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