| First Author | West RR | Year | 1991 |
| Journal | J Biol Chem | Volume | 266 |
| Issue | 32 | Pages | 21886-96 |
| PubMed ID | 1718985 | Mgi Jnum | J:11537 |
| Mgi Id | MGI:59960 | Doi | 10.1016/s0021-9258(18)54720-7 |
| Citation | West RR, et al. (1991) A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences. J Biol Chem 266(32):21886-96 |
| abstractText | cDNAs encoding human and mouse microtubule-associated protein 4 (MAP 4) were isolated. MAP 4 is encoded by a single gene. Multiple MAP 4 mRNAs are transcribed that are differentially expressed among mouse tissues. Open reading frames for the human and mouse MAP 4 clones indicate three distinct regions consisting of related sequences with different motifs. Approximately 30% of the protein is tandem related repeats of approximately 14 amino acids. Another region contains clusters of serine and proline. Four 18-mer repeats characteristic of the microtubule-binding domains of MAP 2 and tau are located at the carboxyl-terminal portion of MAP 4. Amino acid sequence analysis revealed that human and mouse MAP 4 are homologs of the bovine 190-kDa MAP/MAP U (Aizawa, H., Emori, Y., Murofushi, H., Kawasakai, H., Sakai, H., and Suzuki, K. (1990) J. Biol. Chem. 265, 13849-13855). Mouse and human MAP 4 and the bovine 190-kDa MAP are approximately 75% similar, indicating that these proteins are all members of the same class. Domains with extremely high conservation (greater than or equal to 88%) are: 1) the extreme amino terminus; 2) a proline-rich region between the KDM and S,P domains; 3) the microtubule-binding domain; and 4) the extreme carboxyl terminus. |
