Cloning and characterization of a novel, human cellular retinaldehyde-binding protein CRALBP-like (CRALBPL) gene
Autor: | Bo Wan, Jinhu Guo, Guangming Ye, Wen-Qi Pan, Long Yu, Ya-Hui Kong, Kai Qu, Xianghua Liu |
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Rok vydání: | 2006 |
Předmět: |
Protein family
Base Sequence GAS6 Binding protein Molecular Sequence Data Brain Chromosome Mapping Bioengineering General Medicine Biology SYT1 Applied Microbiology and Biotechnology Molecular biology Recombinant Proteins GATAD2B HSPA2 CRAL-TRIO domain Humans Amino Acid Sequence RNA Messenger Cloning Molecular Carrier Proteins Biotechnology HSPA9 HeLa Cells |
Zdroj: | Biotechnology letters. 28(17) |
ISSN: | 0141-5492 |
Popis: | 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. |
Databáze: | OpenAIRE |
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