ID TBA2_MOUSE STANDARD; PRT; 451 AA. AC P05213; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tubulin alpha-2 chain (Alpha-tubulin 2). GN TUBA2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87064538; PubMed=3785200; RA Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.; RT "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis- RT specific expression of two sister genes."; RL Mol. Cell. Biol. 6:2409-2419(1986). RN [2] RP SEQUENCE OF 100-451 FROM N.A. RX MEDLINE=85289512; PubMed=3839797; RA Lewis S.A., Lee M.G.S., Cowan N.J.; RT "Five mouse tubulin isotypes and their regulated expression during RT development."; RL J. Cell Biol. 101:852-861(1985). 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: UBIQUITOUSLY EXPRESSED WITH HIGHEST LEVELS IN CC SPLEEN, THYMUS AND IMMATURE BRAIN. CC -!- SIMILARITY: BELONGS TO THE TUBULIN FAMILY. 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; M13446; AAA40500.1; -. DR EMBL; M28727; AAA40507.1; -. DR PIR; I77425; I77425. DR PIR; S29013; A61275. DR MGD; MGI:107804; Tuba2. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubules; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (POTENTIAL). FT SITE 451 451 INVOLVED IN POLYMERIZATION. FT CONFLICT 135 136 FL -> LF (IN REF. 2). SQ SEQUENCE 451 AA; 50165 MW; 61655B4EC20D317F CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y //