9.B.68 The Putative Na-independent Organic Solute Carrier Protein (OSCP1) Family

Kobayashi et al. (2005) reported the isolation of a novel organic solute carrier from a human placenta cDNA library. The 379 aas protein has an N-terminal hydrophobic peak but otherwise appears hydrophilic. When expressed in Xenopus laevis oocytes, high-affinity transport of PAH and TEA (see below) was observed. Because of its hydrophilic nature, it seems possible that it stimulated uptake via endogenous frog transporters.

This family belongs to the .



Kobayashi, Y., A. Shibusawa, H. Saito, N. Ohshiro, M. Ohbayashi, N. Kohyama, and T. Yamamoto. (2005). Isolation and functional characterization of a novel organic solute carrier protein, hOSCP1. J. Biol. Chem. 280: 32332-32339.


TC#NameOrganismal TypeExample

The putative Na+-independent organic solute transporter (takes up or stimulates uptake of p-amino hippurate (PAH) (Km = 35.0 µM), tetraethylammonium (Km = 62 µM) and other organic solutes in frog oocytes). The protein exhibits one N-terminal TMS but is otherwise hydrophilic (Kobayashi et al., 2005).


OSCP1 of human placenta (379 aas; Q8WVF1)