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 was observed. Because of its hydrophilic nature, it seems possible that it stimulated uptake via endogenous frog transporters.

 


 

References:

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.
Examples:

TC#NameOrganismal TypeExample
9.B.68.1.1

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).

Animals

OSCP1 of human placenta (379 aas; Q8WVF1)