Sequence of the human 40-kDa keratin reveals an unusual structure with very high sequence identity to the corresponding bovine keratin
Description
The complete amino acid and DNA sequences of the human 40-kDa keratin are reported. The DNA sequence encodes a protein of 44,098 Da, which is unique in that it lacks the terminal non-α-helical tail segment found in all other keratins. When the human 40-kDa keratin amino acid sequence is compared to the corresponding bovine keratin, the overall identity is 89%. The coil-forming regions are 89% identical and the head regions are 88% identical. This similarity is also evident in the DNA sequence of the coding region, the 5' upstream sequences, and the 3' noncoding sequences. The high degree of cross-species identity between bovine and human 40-kDa keratins suggests that there is strong evolutionary pressure to conserve the structure of this keratin. This in turn suggests an important and universal role for this intermediate filament subunit in all species
Additional details
Publishing Information
- Journal Title
- Proceedings of the National Academy of Sciences of the United States of America
- Journal Volume
- 85
- Journal Issue
- 4
- Series
- Proc. Natl. Acad. Sci. U.S.A.
- Journal Page Range
- 1114-1118
- ISSN
- 0027-8424
- CODEN
- PNASA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 20026153
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- BIOLOGICAL EVOLUTION; CATTLE; DNA SEQUENCING; KERATIN; MAN; PHOSPHORUS 32; PROTEIN STRUCTURE; RECOMBINANT DNA
- Descriptors DEC
- ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; DAYS LIVING RADIOISOTOPES; DNA; DOMESTIC ANIMALS; ISOTOPES; LIGHT NUCLEI; MAMMALS; NUCLEI; NUCLEIC ACIDS; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; PHOSPHORUS ISOTOPES; PRIMATES; PROTEINS; RADIOISOTOPES; RUMINANTS; SCLEROPROTEINS; STRUCTURAL CHEMICAL ANALYSIS; VERTEBRATES