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Cloning and Characterization of a Novel, Human Cellular Retinaldehyde-binding Protein CRALBP-like (CRALBPL) Gene
- Kong, Ya-Hui, Ye, Guang-Ming, Qu, Kai, Pan, Wen-Qi, Liu, Xiang-Hua, Wan, Bo, Guo, Jin-Hu, Yu, Long
- Biotechnology letters 2006 v.28 no.17 pp. 1327-1333
- Western blotting, adults, amino acids, brain, cDNA libraries, complementary DNA, genes, humans, molecular weight, open reading frames
- Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.