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Am J Physiol Gastrointest Liver Physiol (January 9, 2002). doi:10.1152/ajpgi.00458.2001
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Articles in PresS, published online ahead of print January 9, 2002
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00458.2001
Submitted on October 31, 2001
Accepted on December 10, 2001

An Evolutionarily Ancient Oatp: insights into conserved functional domains of these proteins

Shi-Ying Cai1, Wei Wang2, Carol J Soroka1, Nazzareno Ballatori3, and James L Boyer4*

1 Liver Center, Yale University School of Medicine, New Haven, CT, USA
2 Environmental Medicine, University of Rochester School of Medicine, Rochester, NY, USA
3 Environmental Medicine, University of Rochester School of Medicine, Rochester, NY, USA; Mt. Desert Island Biological Laboratory, Salsbury Cove, ME, USA
4 Liver Center, Yale University School of Medicine, New Haven, CT, USA; Mt. Desert Island Biological Laboratory, Salsbury Cove, ME, USA

* To whom correspondence should be addressed. E-mail: shiying.cai{at}yale.edu.

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 about 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.




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