ID TBA3_MOUSE STANDARD; PRT; 450 AA. AC P05214; DT 13-AUG-1987 (REL. 05, CREATED) DT 13-AUG-1987 (REL. 05, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE TUBULIN ALPHA-3 AND ALPHA-7 CHAINS. GN TUBA3 AND TUBA7. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87064538. RA VILLASANTE A., WANG D., DOBNER P., DOLPH P., LEWIS S.A., COWAN N.J.; RL MOL. CELL. BIOL. 6:2409-2419(1986). CC -!- FUNCTION: TUBULIN IS THE MAJOR CONSTITUENT OF MICROTUBULES. IT CC BINDS TWO MOLES OF GTP, ONE AT AN EXCHANGEABLE SITE ON THE BETA CC CHAIN AND ONE AT A NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- TISSUE SPECIFICITY: ALPHA-3 AND ALPHA-7 ARE IDENTICAL BUT CODED BY CC TWO DIFFERENT GENES, THEY ARE TESTIS-SPECIFIC. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13442; G202212; -. DR EMBL; M13443; G202219; -. DR PROSITE; PS00227; TUBULIN. KW MICROTUBULES; GTP-BINDING; MULTIGENE FAMILY. FT NP_BIND 142 148 GTP (POTENTIAL). FT SITE 450 450 INVOLVED IN POLYMERIZATION. SQ SEQUENCE 450 AA; 49959 MW; 6874CAA4 CRC32; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY //