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Publication : The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue.

First Author  Skaggs LA Year  1993
Journal  Gene Volume  126
Issue  2 Pages  291-2
PubMed ID  8482548 Mgi Jnum  J:12433
Mgi Id  MGI:60680 Doi  10.1016/0378-1119(93)90385-g
Citation  Skaggs LA, et al. (1993) The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue. Gene 126(2):291-2
abstractText  A recently reported mRNA, encoding 'carbonic anhydrase-related polypeptide' (CARP) from the Purkinje cells of mouse cerebellum, was shown to have a 30-40% deduced amino acid sequence identity with the carbonic anhydrases (CA) of mammals. In order to compare the mouse and human CARP sequences, we used the polymerase chain reaction (PCR) to amplify human CARP sequences from several cDNA libraries (salivary gland, testis and placenta). The sequence has an 89.3% sequence identity with mouse CARP at the nucleotide level and 97.9% at the amino acid level. This extremely high evolutionary conservation suggests an important function for the CARP gene product.
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