title: The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue.
abstract: 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.
authors: Department of Human Genetics, University of Michigan, Ann Arbor 48109-0618.
authors: L A
authors: LA
authors: Skaggs
authors: N C
authors: NC
authors: Bergenhem
authors: P J
authors: PJ
authors: Venta
authors: R E
authors: RE
authors: Tashian
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002256:Carbonic Anhydrases; D004247:DNA; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
chemical_list: D009419:Nerve Tissue Proteins; D004247:DNA; D002256:Carbonic Anhydrases